UI  - 21845924
PMID- 11856308
DA  - 20020221
IS  - 0014-2956
VI  - 269
IP  - 2
DP  - 2002 Jan
TI  - Cell surface heparan sulfate proteoglycans.
PG  - 502-11
AB  - Basic fibroblast growth factor (bFGF) regulates diversified biological
      functions in rat Sertoli cells. This report demonstrates that bFGF
      inhibits steroidogenesis in developing rat Sertoli cells. Follicle
      stimulating hormone (FSH)-stimulated estradiol production was reduced by
      bFGF. Moreover, the amount of cytochrome P450 aromatase, responsible for
      the irreversible transformation of androgens into estrogens, is decreased
      by bFGF at the transcriptional level. The bFGF inhibitory effect was also
      observed in the presence of dibutyryl-cAMP, cholera toxin or RO-20-1724,
      all inducing high levels of cAMP, the second messenger of FSH. Heparan
      sulfate proteoglycans (HSPGs) were shown to be required as cofactors for
      bFGF signaling. Indeed, sodium chlorate, described to drastically decrease
      proteoglycan sulfation, abolishes the bFGF downregulation of
      FSH-stimulated estradiol synthesis previously observed. Glypican-1,
      syndecan-1 and -4, potential bFGF coreceptors, are mainly regulated at the
      transcriptional level. This report shows that the bFGF regulation of their
      expression specifically depends on the nature of HSPG and of the Sertoli
      cell developmental stage. In conclusion, HSPG are partners and the target
      of bFGF in rat Sertoli cells.
AD  - Laboratoire de Biochimie, IRBA, Universite de Caen, France.
FAU - Brucato, Sylvie
AU  - Brucato S
FAU - Bocquet, Jean
AU  - Bocquet J
FAU - Villers, Corinne
AU  - Villers C
LA  - eng
PT  - Journal Article
CY  - Germany
TA  - Eur J Biochem
JID - 0107600
SB  - IM
EDAT- 2002/02/22 10:00
MHDA- 2002/02/22 10:00
AID - 2672 [pii]
PST - ppublish
SO  - Eur J Biochem 2002 Jan;269(2):502-11.




UI  - 21839829
PMID- 11850808
DA  - 20020218
DCOM- 20020227
IS  - 0950-9232
VI  - 21
IP  - 5
DP  - 2002 Jan 24
TI  - HOXD3 enhances motility and invasiveness through the TGF-beta-dependent
      and -independent pathways in A549 cells.
PG  - 798-808
AB  - Homeobox genes regulate sets of genes that determine cellular fates in
      embryonic morphogenesis and maintenance of adult tissue architecture by
      regulating cellular motility and cell-cell interactions. Our previous
      studies showed that a specific member, HOXD3, when overexpressed,
      upregulates integrin beta3 expression in human erythroleukemia HEL cells
      and lung cancer A549 cells, and enhances their motility and invasiveness.
      We performed a microarray study of over 7075 genes to determine the
      mechanisms underlying the HOXD3-enhanced motility and invasiveness in A549
      cells. RT-PCR-based tracking gene analyses highlighted a set of
      TGF-beta-upregulated genes, which included matrix metalloproteinase-2,
      syndecan-1, CD44, and TGF-beta-induced 68 kDa protein. Exogenous TGF-beta
      also caused this pattern of upregulation in A549 cells and enhanced their
      migratory and invasive activity, confirming the involvement of TGF-beta
      signaling. However, HOXD3 reduced the expression of TGF-beta-independent
      genes coding for desmosomal components such as desmoglein, desmoplakin and
      plakoglobin which are known to suppress tumor invasion and metastasis.
      These results suggest that HOXD3 enhances the invasive and metastatic
      potential of cancer cells through the TGF-beta-dependent and -independent
      pathways.
AD  - Division of Cancer-Related Genes, Institute for Genetic Medicine, Hokkaido
      University, Kita-15, Nishi-7, Kita-ku, Sapporo 060-0815, Japan.
FAU - Miyazaki, Yasumasa J
AU  - Miyazaki YJ
FAU - Hamada, Jun-ichi
AU  - Hamada J
FAU - Tada, Mitsuhiro
AU  - Tada M
FAU - Furuuchi, Keiji
AU  - Furuuchi K
FAU - Takahashi, Yoko
AU  - Takahashi Y
FAU - Kondo, Satoshi
AU  - Kondo S
FAU - Katoh, Hiroyuki
AU  - Katoh H
FAU - Moriuchi, Tetsuya
AU  - Moriuchi T
LA  - eng
PT  - Journal Article
CY  - England
TA  - Oncogene
JID - 8711562
RN  - 0 (Homeodomain Proteins)
RN  - 0 (Hoxd-3 protein)
RN  - 0 (RNA, Neoplasm)
RN  - 0 (Transforming Growth Factor beta)
SB  - IM
MH  - *Cell Movement
MH  - Down-Regulation
MH  - Gene Expression Profiling
MH  - Homeodomain Proteins/genetics/*physiology
MH  - Neoplasm Invasiveness
MH  - Neoplasms/genetics/*metabolism/pathology
MH  - Oligonucleotide Array Sequence Analysis
MH  - RNA, Neoplasm/biosynthesis
MH  - *Signal Transduction
MH  - Support, Non-U.S. Gov't
MH  - Transfection
MH  - Transforming Growth Factor beta/biosynthesis/*pharmacology
MH  - Tumor Cells, Cultured
MH  - Up-Regulation
EDAT- 2002/02/19 10:00
MHDA- 2002/02/19 10:00
PHST- 2001/Apr/30 [received]
PHST- 2001/Oct/02 [revised]
PHST- 2001/Oct/29 [accepted]
AID - 10.1038/sj/onc/1205126 [doi]
PST - ppublish
SO  - Oncogene 2002 Jan 24;21(5):798-808.




UI  - 21818538
PMID- 11830493
DA  - 20020206
IS  - 0006-4971
VI  - 99
IP  - 4
DP  - 2002 Feb 15
TI  - Cell surface proteoglycan syndecan-1 mediates hepatocyte growth factor
      binding and promotes Met signaling in multiple myeloma.
PG  - 1405-10
AB  - Heparan sulfate proteoglycans (HSPGs) play a crucial role in growth
      regulation by assembling signaling complexes and presenting growth factors
      to their cognate receptors. Within the immune system, expression of the
      HSPG syndecan-1 (CD138) is characteristic of terminally differentiated B
      cells, ie, plasma cells, and their malignant counterpart, multiple myeloma
      (MM). This study explored the hypothesis that syndecan-1 might promote
      growth factor signaling and tumor growth in MM. For this purpose, the
      interaction was studied between syndecan-1 and hepatocyte growth factor
      (HGF), a putative paracrine and autocrine regulator of MM growth. The
      study demonstrates that syndecan-1 is capable of binding HGF and that this
      growth factor is indeed a potent stimulator of MM survival and
      proliferation. Importantly, the interaction of HGF with heparan sulfate
      moieties on syndecan-1 strongly promotes HGF-mediated signaling, resulting
      in enhanced activation of Met, the receptor tyrosine kinase for HGF.
      Moreover, HGF binding to syndecan-1 promotes activation of the
      phosphatidylinositol 3-kinase/protein kinase B and RAS/mitogen-activated
      protein kinase pathways, signaling routes that have been implicated in the
      regulation of cell survival and proliferation, respectively. These results
      identify syndecan-1 as a functional coreceptor for HGF that promotes
      HGF/Met signaling in MM cells, thus suggesting a novel function for
      syndecan-1 in MM tumorigenesis. (Blood. 2002;99:1405-1410)
AD  - Department of Pathology and the Department of Hematology, Academic Medical
      Center, University of Amsterdam, The Netherlands.
FAU - Derksen, Patrick W B
AU  - Derksen PW
FAU - Keehnen, Robert M J
AU  - Keehnen RM
FAU - Evers, Ludo M
AU  - Evers LM
FAU - van Oers, Marinus H J
AU  - van Oers MH
FAU - Spaargaren, Marcel
AU  - Spaargaren M
FAU - Pals, Steven T
AU  - Pals ST
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Blood
JID - 7603509
SB  - AIM
SB  - IM
EDAT- 2002/02/07 10:00
MHDA- 2002/02/07 10:00
URLF- http://www.bloodjournal.org/cgi/content/full/99/4/1405
URLS- http://www.bloodjournal.org/cgi/content/abstract/99/4/1405
PST - ppublish
SO  - Blood 2002 Feb 15;99(4):1405-10.




UI  - 21655489
PMID- 11796840
DA  - 20020117
DCOM- 20020228
IS  - 0893-3952
VI  - 15
IP  - 1
DP  - 2002 Jan
TI  - The level of syndecan-1 expression is a distinguishing feature in behavior
      between keratoacanthoma and invasive cutaneous squamous cell carcinoma.
PG  - 45-9
AB  - Keratoacanthoma (KA) resolves spontaneously but is regarded by some as a
      variant of squamous cell carcinoma (SCC). However, others consider KA a
      totally benign entity. Syndecan-1 is one of the heparan sulfate
      proteoglycans that mediates intercellular and cell to matrix adhesion. Its
      expression appears to be inversely correlated with tumor aggressiveness
      and invasiveness. Previous studies have shown decreased levels of
      syndecan-1 expression in invasive cutaneous SCC, correlating with tumor
      de-differentiation. However, a similar study has never been done on KA. To
      investigate syndecan-1 expression in classic KA and compare the results
      with those of classic invasive SCC, 24 KAs were immunostained for
      syndecan-1 (CD 138) using the monoclonal antibody B-B4 on formalin-fixed
      paraffin-embedded tissue. Results were semi-quantitatively scored as
      either negative or positive (mild, moderate, or strong) and compared with
      those previously obtained on 23 invasive SCC and in situ lesions. All 24
      KAs were positive for syndecan-1 expression. Staining intensity of 18
      cases was comparable with that of SCC in situ or adjacent normal
      epidermis. By comparison, invasive SCC showed significantly diminished
      staining. Reduced staining in focal areas of cytologic atypia at the base
      was present in three KAs. Syndecan-1 expression in KA mirrors that of SCC
      in situ and normal epidermis, providing a molecular basis that
      biologically KA may be closely related to SCC in situ but distinctively
      different from invasive SCC.
AD  - Department of Pathology, University of Arkansas for Medical Sciences, 4301
      W. Markham, Little Rock, AR 72205, USA. mukunyadziperkins@uams.edu
FAU - Mukunyadzi, Perkins
AU  - Mukunyadzi P
FAU - Sanderson, Ralph D
AU  - Sanderson RD
FAU - Fan, Chun-Yang
AU  - Fan CY
FAU - Smoller, Bruce R
AU  - Smoller BR
LA  - eng
ID  - CA 68494/CA/NCI
PT  - Journal Article
CY  - United States
TA  - Mod Pathol
JID - 8806605
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - IM
MH  - Carcinoma in Situ/*metabolism/pathology
MH  - Carcinoma, Squamous Cell/*metabolism/pathology
MH  - Diagnosis, Differential
MH  - Human
MH  - Immunoenzyme Techniques
MH  - Keratoacanthoma/*metabolism/pathology
MH  - Membrane Glycoproteins/*biosynthesis
MH  - Neoplasm Invasiveness
MH  - Proteoglycans/*biosynthesis
MH  - Skin Neoplasms/*metabolism/pathology
MH  - Stromal Cells/metabolism/pathology
MH  - Support, U.S. Gov't, P.H.S.
EDAT- 2002/01/18 10:00
MHDA- 2002/03/01 10:01
URLF- http://modpath.uscapjournals.org/cgi/content/full/15/1/45
URLS- http://modpath.uscapjournals.org/cgi/content/abstract/15/1/45
PST - ppublish
SO  - Mod Pathol 2002 Jan;15(1):45-9.




UI  - 21646943
PMID- 11786733
DA  - 20020111
DCOM- 20020204
IS  - 1010-4283
VI  - 22
IP  - 6
DP  - 2001 Nov-Dec
TI  - Expression of oncofetal fibronectin and syndecan-1 mRNA in 18 human lung
      cancer cell lines.
PG  - 390-6
AB  - It has been suggested that fibronectin (FN) and syndecan play an important
      role in many aspects of cell-substrate interactions including cell
      adhesion. We hypothesized that oncofetal FN (onfFN) and syndecan play an
      important role in the process of adhesion of several human lung cancer
      cell lines. To test this, levels of onfFN in the culture supernatant were
      measured by an enzyme-linked immunosorbent assay in 18 human lung cancer
      cell lines. In addition, expressions of onfFN and syndecan-1 mRNA were
      analyzed by reverse transcriptase-polymerase chain reaction (RT-PCR). Of
      18 lung cancer cell lines, 3 cell lines (all adenocarcinoma) released a
      significant amount of onfFN in culture supernatants. Of the 18 cell lines
      tested, 6 cell lines expressed a significant amount of mRNA for onfFN and
      4 expressed a significant amount of mRNA for syndecan-1. Levels of onfFN
      and expressions of mRNA for onfFN and syndecan-1 were consistently higher
      in non-small cell lung cancer cell lines than in small cell lung cancer
      cell lines. In addition, cell lines that expressed mRNA for onfFN and
      syndecan-1 tended to adhere to culture dishes. Syndecan-1 expression was
      significantly higher in attached cells compared with nonattached cells
      within the same cell line. Differences in onfFN and syndecan synthesis may
      explain some in vitro and in vivo characteristics of lung cancer.
CI  - Copyright 2001 S. Karger AG, Basel
AD  - First Department of Internal Medicine, Kagawa Medical University, Kagawa,
      Japan.
FAU - Nanki, N
AU  - Nanki N
FAU - Fujita, J
AU  - Fujita J
FAU - Yang, Y
AU  - Yang Y
FAU - Hojo, S
AU  - Hojo S
FAU - Bandoh, S
AU  - Bandoh S
FAU - Yamaji, Y
AU  - Yamaji Y
FAU - Ishida, T
AU  - Ishida T
LA  - eng
PT  - Journal Article
CY  - Switzerland
TA  - Tumour Biol
JID - 8409922
RN  - 0 (Fibronectins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (oncofetal fibronectin)
RN  - 0 (syndecan)
SB  - IM
MH  - Cell Adhesion
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Fibronectins/*biosynthesis/genetics
MH  - Gene Expression Regulation, Neoplastic
MH  - Human
MH  - Lung Neoplasms/*metabolism/pathology
MH  - Membrane Glycoproteins/*biosynthesis/genetics
MH  - Polymerase Chain Reaction
MH  - Proteoglycans/*biosynthesis/genetics
MH  - RNA, Messenger/biosynthesis/genetics
MH  - Tumor Cells, Cultured
EDAT- 2002/01/12 10:00
MHDA- 2002/02/05 10:01
AID - tbi22390 [pii]
URLF- http://www.online.karger.com/library/karger/renderer/dataset.exe?jcode=TBI
      &action=render&rendertype=fulltext&uid=TBI.tbi22390
URLS- http://www.karger.com/journals/tbi/tbi_jh.htm
PST - ppublish
SO  - Tumour Biol 2001 Nov-Dec;22(6):390-6.




UI  - 21645767
PMID- 11786412
DA  - 20020111
IS  - 0002-9440
VI  - 160
IP  - 1
DP  - 2002 Jan
TI  - Heparan sulfate proteoglycans as regulators of fibroblast growth factor-2
      receptor binding in breast carcinomas.
PG  - 185-94
AB  - Binding of fibroblast growth factors (FGFs) to their tyrosine
      kinase-signaling receptors (FGFRs) requires heparan sulfate (HS). HS
      proteoglycans (HSPGs) determine mitogenic responses of breast carcinoma
      cells to FGF-2 in vitro. For this study, we examined the role of HSPGs as
      modulators of FGF-2 binding to FGFR-1 in situ and in vitro. During
      stepwise reconstitution of the FGF-2/HSPG/FGFR-1 complex in situ, we
      identified an elevated ability of breast carcinoma cell HSPGs to promote
      receptor complex formation compared to normal breast epithelium. HSPGs
      isolated from the MCF-7 breast-carcinoma cell line were then fractionated
      according to their ability to assemble the FGF-2 receptor complex. All
      MCF-7 HSPGs are decorated with HS chains similarly capable of promoting
      FGF-2 receptor complex formation. In this in vitro model, syndecan-1 and
      syndecan-4 are the cell surface HSPGs contributing most to the complex
      formation. Relative expression levels of these syndecans in human breast
      carcinoma tissues correlate well with receptor complex formation in situ,
      indicating that in breast carcinomas, core protein levels determine FGF-2
      receptor complex formation. However, variances in syndecan expression
      levels do not explain the difference in FGF-2 receptor complex formation
      between normal and malignant epithelial cells, suggesting that alterations
      in HS structure occur during malignant transformation.
AD  - Department of Pathology and Laboratory Medicine, University of
      Wisconsin-Madison, Madison, Wisconsin.
FAU - Mundhenke, Christoph
AU  - Mundhenke C
FAU - Meyer, Kristy
AU  - Meyer K
FAU - Drew, Sally
AU  - Drew S
FAU - Friedl, Andreas
AU  - Friedl A
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Am J Pathol
JID - 0370502
SB  - AIM
SB  - IM
EDAT- 2002/01/12 10:00
MHDA- 2002/01/12 10:00
URLF- http://ajp.amjpathol.org/cgi/content/full/160/1/185
URLS- http://ajp.amjpathol.org/cgi/content/abstract/160/1/185
PST - ppublish
SO  - Am J Pathol 2002 Jan;160(1):185-94.




UI  - 21643866
PMID- 11784020
DA  - 20020110
DCOM- 20020128
IS  - 0012-1606
VI  - 239
IP  - 1
DP  - 2001 Nov 1
TI  - Syndecan-3 and syndecan-4 specifically mark skeletal muscle satellite
      cells and are implicated in satellite cell maintenance and muscle
      regeneration.
PG  - 79-94
AB  - Myogenesis in the embryo and the adult mammal consists of a highly
      organized and regulated sequence of cellular processes to form or repair
      muscle tissue that include cell proliferation, migration, and
      differentiation. Data from cell culture and in vivo experiments implicate
      both FGFs and HGF as critical regulators of these processes. Both factors
      require heparan sulfate glycosaminoglycans for signaling from their
      respective receptors. Since syndecans, a family of cell-surface
      transmembrane heparan sulfate proteoglycans (HSPGs) are implicated in FGF
      signaling and skeletal muscle differentiation, we examined the expression
      of syndecans 1-4 in embryonic, fetal, postnatal, and adult muscle tissue,
      as well as on primary adult muscle fiber cultures. We show that
      syndecan-1, -3, and -4 are expressed in developing skeletal muscle tissue
      and that syndecan-3 and -4 expression is highly restricted in adult
      skeletal muscle to cells retaining myogenic capacity. These two HSPGs
      appear to be expressed exclusively and universally on quiescent adult
      satellite cells in adult skeletal muscle tissue, suggesting a role for
      HSPGs in satellite cell maintenance or activation. Once activated, all
      satellite cells maintain expression of syndecan-3 and syndecan-4 for at
      least 96 h, also implicating these HSPGs in muscle regeneration.
      Inhibition of HSPG sulfation by treatment of intact myofibers with
      chlorate results in delayed proliferation and altered MyoD expression,
      demonstrating that heparan sulfate is required for proper progression of
      the early satellite cell myogenic program. These data suggest that, in
      addition to providing potentially useful new markers for satellite cells,
      syndecan-3 and syndecan-4 may play important regulatory roles in satellite
      cell maintenance, activation, proliferation, and differentiation during
      skeletal muscle regeneration.
CI  - Copyright 2001 Academic Press.
AD  - Department of Molecular, Cellular and Developmental Biology, University of
      Colorado, Boulder, Colorado 80309, USA.
FAU - Cornelison, D D
AU  - Cornelison DD
FAU - Filla, M S
AU  - Filla MS
FAU - Stanley, H M
AU  - Stanley HM
FAU - Rapraeger, A C
AU  - Rapraeger AC
FAU - Olwin, B B
AU  - Olwin BB
LA  - eng
ID  - AR39467/AR/NIAMS
ID  - GM48850/GM/NIGMS
ID  - HD21881/HD/NICHD
ID  - HL07851/HL/NHLBI
PT  - Journal Article
CY  - United States
TA  - Dev Biol
JID - 0372762
RN  - 0 (Biological Markers)
RN  - 0 (Chlorates)
RN  - 0 (Laminin)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (MyoD Protein)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, Fibroblast Growth Factor)
RN  - 0 (fibroblast growth factor receptor 1)
RN  - 0 (syndecan 3)
RN  - 0 (syndecan-4)
RN  - 9050-30-0 (Heparitin Sulfate)
RN  - EC 2.7.11.- (Proto-Oncogene Protein c-met)
RN  - EC 2.7.11.- (Receptor Protein-Tyrosine Kinases)
SB  - IM
MH  - Aging/metabolism
MH  - Animal
MH  - Animals, Newborn
MH  - Biological Markers/analysis
MH  - Cell Differentiation/drug effects
MH  - Cell Division/drug effects
MH  - Cell Movement/drug effects
MH  - Cells, Cultured
MH  - Chlorates/pharmacology
MH  - Embryo/cytology/drug effects/embryology/metabolism
MH  - Forelimb
MH  - Gene Expression Regulation, Developmental/drug effects
MH  - Heparitin Sulfate/pharmacology
MH  - Laminin/analysis
MH  - Membrane Glycoproteins/*metabolism
MH  - Mice
MH  - *Muscle Development/drug effects
MH  - Muscle Fibers/cytology/metabolism
MH  - Muscle, Skeletal/*cytology/embryology/growth & development/*metabolism
MH  - MyoD Protein/analysis
MH  - Proteoglycans/*metabolism
MH  - Proto-Oncogene Protein c-met/analysis
MH  - Receptor Protein-Tyrosine Kinases/analysis
MH  - Receptors, Fibroblast Growth Factor/analysis
MH  - *Regeneration/drug effects
MH  - Signal Transduction/drug effects
MH  - Support, U.S. Gov't, P.H.S.
EDAT- 2002/01/11 10:00
MHDA- 2002/01/29 10:01
AID - 10.1006/dbio.2001.0416 [doi]
AID - dbio.2001.0416 [pii]
PST - ppublish
SO  - Dev Biol 2001 Nov 1;239(1):79-94.




UI  - 21640541
PMID- 11781374
DA  - 20020108
DCOM- 20020131
IS  - 0022-1007
VI  - 195
IP  - 1
DP  - 2002 Jan 7
TI  - Fc gamma receptors and cross-presentation in dendritic cells.
PG  - F1-3
AD  - INSERM U520, Institut Curie, 75005 Paris, France. sebas@curie.fr
FAU - Amigorena, Sebastian
AU  - Amigorena S
LA  - eng
PT  - Comment
PT  - Journal Article
CY  - United States
TA  - J Exp Med
JID - 2985109R
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (MAGE-3 antigen)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (NY-ESO-1 protein)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, IgG)
RN  - 0 (syndecan)
SB  - IM
CON - J Exp Med. 2002 Jan 7;195(1):125-33. PMID: 11781371
MH  - Antibodies, Neoplasm/*immunology
MH  - *Antigen Presentation
MH  - Antigens, Neoplasm/*immunology
MH  - Autoimmunity
MH  - Dendritic Cells/*immunology
MH  - Immune Tolerance
MH  - Membrane Glycoproteins/immunology
MH  - Neoplasm Proteins/immunology
MH  - Proteins/immunology
MH  - Proteoglycans/immunology
MH  - Receptors, IgG/*metabolism
MH  - T-Lymphocytes, Cytotoxic/immunology
EDAT- 2002/01/10 10:00
MHDA- 2002/02/01 10:01
URLF- http://www.jem.org/cgi/content/full/195/1/F1
PST - ppublish
SO  - J Exp Med 2002 Jan 7;195(1):F1-3.




UI  - 21640538
PMID- 11781371
DA  - 20020108
DCOM- 20020131
IS  - 0022-1007
VI  - 195
IP  - 1
DP  - 2002 Jan 7
TI  - Antitumor monoclonal antibodies enhance cross-presentation ofcCellular
      antigens and the generation of myeloma-specific killer T cells by
      dendritic cells.
PG  - 125-33
AB  - The mechanism of antitumor effect of monoclonal antibodies (mAbs) is not
      fully understood. Here we show that coating myeloma cells with
      anti-syndecan-1 antibody promotes cross-presentation of cellular antigens
      by dendritic cells (DCs) to autologous T cells from healthy donors. The
      tumor cells treated with anti-syndecan-1 or isotype-matched control
      antibody were fed to HLA-mismatched monocyte-derived immature DCs. Tumor
      cell-loaded mature DCs induced a strong CD8(+) T cell response that was
      specific for the cancer-testis (C-T) antigens expressed in the tumor. The
      CD8(+) T cells killed peptide-pulsed targets, as well as myeloma tumor
      cells. Importantly, mAbs-coated tumor-loaded DCs were consistently
      superior to DCs loaded with peptides or dying cells for eliciting
      tumor-specific killer T cells. This enhanced cross-presentation was not
      due to enhanced tumor cell uptake or to DC maturation. When mixtures of
      NY-Eso-1-positive and -negative myeloma cells were captured by DCs, the
      anti-syndecan-1 antibody had to be on the NY-Eso-1-positive cells to
      elicit NY-Eso-1-specific response. Cross-presentation was inhibited by
      pretreatment of DCs with Fc gamma receptor blocking antibodies. Targeting
      of mAb-coated tumors to DCs may contribute to the efficacy of
      tumor-reactive mAb and offers a new strategy for immunotherapy.
AD  - Laboratory of Tumor Immunology and Immunotherapy, The Rockefeller
      University, New York, NY 10021, USA.
FAU - Dhodapkar, Kavita M
AU  - Dhodapkar KM
FAU - Krasovsky, Joseph
AU  - Krasovsky J
FAU - Williamson, Barbara
AU  - Williamson B
FAU - Dhodapkar, Madhav V
AU  - Dhodapkar MV
LA  - eng
ID  - CA81138/CA/NCI
ID  - M0-RR00102/RR/NCRR
PT  - Journal Article
CY  - United States
TA  - J Exp Med
JID - 2985109R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (MAGE-3 antigen)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (NY-ESO-1 protein)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, IgG)
RN  - 0 (syndecan)
RN  - 82115-62-6 (Interferon Type II)
SB  - IM
CIN - J Exp Med. 2002 Jan 7;195(1):F1-3. PMID: 11781374
MH  - Antibodies, Monoclonal/immunology/pharmacology
MH  - Antibodies, Neoplasm/*immunology/pharmacology
MH  - *Antigen Presentation
MH  - Antigens, Neoplasm/*immunology
MH  - Apoptosis
MH  - Dendritic Cells/*immunology
MH  - Human
MH  - Immunotherapy
MH  - Interferon Type II/secretion
MH  - Killer Cells/*immunology
MH  - Male
MH  - Membrane Glycoproteins/immunology
MH  - Multiple Myeloma/*therapy
MH  - Neoplasm Proteins/immunology
MH  - Proteins/immunology
MH  - Proteoglycans/immunology
MH  - Receptors, IgG/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
MH  - T-Lymphocytes/*immunology
MH  - Testicular Neoplasms/immunology
EDAT- 2002/01/10 10:00
MHDA- 2002/02/01 10:01
URLF- http://www.jem.org/cgi/content/full/195/1/125
URLS- http://www.jem.org/cgi/content/abstract/195/1/125
PST - ppublish
SO  - J Exp Med 2002 Jan 7;195(1):125-33.




UI  - 21637968
PMID- 11779146
DA  - 20020107
DCOM- 20020225
IS  - 0006-291X
VI  - 290
IP  - 1
DP  - 2002 Jan 11
TI  - Expression and characterization of minican, a recombinant syndecan-1 with
      extensively truncated core protein.
PG  - 146-52
AB  - Syndecan-1 is an integral membrane heparan sulfate/chondroitin sulfate
      proteoglycan, involved in the control of cell growth and differentiation.
      The biological activities of syndecan-1 involve interactions with a
      variety of extracellular ligands, such as growth factors and matrix
      components, that are mainly mediated by the heparan sulfate moieties. The
      expression of syndecan-1 is downregulated in various malignant tumors, and
      low levels of expression appear to correlate with poor prognosis of some
      cancer types. On the other hand, the extracellular portion of syndecan-1
      (ectodomain) has been demonstrated to inhibit the proliferation of various
      cancer cells in culture, suggesting that proteoglycan-like molecules
      should be studied further with regard to their antitumor activities. We
      have expressed, in CHO cells, a truncated syndecan-1 ectodomain
      ("minican") harboring domains for glycosaminoglycan attachment and
      antibody recognition. Analysis of recombinant minican indicates that it
      shares some of the biochemical and biological characteristics attributed
      to syndecan-1 ectodomain. Minican was thus substituted with heparan
      sulfate chains and bound to extracellular matrix proteins as well as
      fibroblast growth factors. Notably, minican inhibited the proliferation of
      S115 mouse mammary carcinoma cells and the effect seemed to involve
      inhibition of the Ras/Erk signaling pathway. Our data suggest that
      recombinant syndecan-1 with a minimal protein component is biologically
      active. This information may provide useful in further design of
      proteoglycan-like antitumor molecules.
CI  - (c)2002 Elsevier Science.
AD  - Turku Centre for Biotechnology, University of Turku and Abo Akademi
      University, Tykistokatu 6, BioCity, FIN-20520, Turku, Finland.
FAU - Viklund, Leif
AU  - Viklund L
FAU - Loo, Britt-Marie
AU  - Loo BM
FAU - Hermonen, Jorma
AU  - Hermonen J
FAU - El-Darwish, Kamel
AU  - El-Darwish K
FAU - Jalkanen, Markku
AU  - Jalkanen M
FAU - Salmivirta, Markku
AU  - Salmivirta M
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Biochem Biophys Res Commun
JID - 0372516
RN  - 0 (Culture Media, Serum-Free)
RN  - 0 (DNA, Complementary)
RN  - 0 (Disaccharides)
RN  - 0 (Glycosaminoglycans)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Proteoglycans)
RN  - 0 (Recombinant Proteins)
RN  - 0 (minican)
RN  - 0 (syndecan)
RN  - 57-85-2 (Testosterone)
RN  - 62031-54-3 (Fibroblast Growth Factors)
RN  - 9050-30-0 (Heparitin Sulfate)
RN  - EC 2.7.1.- (Mitogen-Activated Protein Kinases)
RN  - EC 3.6.1.- (ras Proteins)
RN  - EC 4.2.2. (Polysaccharide-Lyases)
RN  - EC 4.2.2.4 (Chondroitin ABC Lyase)
RN  - EC 4.2.2.8 (heparitinsulfate lyase)
SB  - IM
MH  - Animal
MH  - Blotting, Northern
MH  - Blotting, Western
MH  - CHO Cells
MH  - Cell Division/drug effects
MH  - Chondroitin ABC Lyase/metabolism
MH  - Cloning, Molecular
MH  - Culture Media, Serum-Free/pharmacology
MH  - DNA, Complementary/metabolism
MH  - Disaccharides/chemistry
MH  - Dose-Response Relationship, Drug
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Extracellular Matrix/metabolism
MH  - Fibroblast Growth Factors/metabolism
MH  - Glycosaminoglycans/chemistry
MH  - Hamsters
MH  - Heparitin Sulfate/chemistry
MH  - Membrane Glycoproteins/*biosynthesis/*chemistry
MH  - Mice
MH  - Mitogen-Activated Protein Kinases/metabolism
MH  - Peptide Fragments/*biosynthesis/*chemistry
MH  - Phosphorylation
MH  - Polysaccharide-Lyases/metabolism
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Proteoglycans/*biosynthesis/*chemistry
MH  - Recombinant Proteins/*biosynthesis/*chemistry
MH  - Signal Transduction
MH  - Support, Non-U.S. Gov't
MH  - Testosterone/pharmacology
MH  - Time Factors
MH  - Transfection
MH  - Tumor Cells, Cultured
MH  - ras Proteins/metabolism
EDAT- 2002/01/10 10:00
MHDA- 2002/02/28 10:01
AID - 10.1006/bbrc.2001.6187 [doi]
AID - bbrc.2001.6187 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun 2002 Jan 11;290(1):146-52.




UI  - 21604411
PMID- 11761938
DA  - 20011213
DCOM- 20020201
IS  - 0047-1852
VI  - 59 Suppl 6
DP  - 2001 Oct
TI  - [Syndecan-1]
PG  - 184-8
AD  - Third Department of Internal Medicine, Asahikawa Medical College.
FAU - Fujimoto, Y
AU  - Fujimoto Y
FAU - Kohgo, Y
AU  - Kohgo Y
LA  - jpn
PT  - Journal Article
PT  - Review
PT  - Review, Tutorial
CY  - Japan
TA  - Nippon Rinsho
JID - 0420546
RN  - 0 (Glycosaminoglycans)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - IM
MH  - Animal
MH  - Carcinoma, Hepatocellular/*pathology
MH  - Extracellular Matrix/metabolism
MH  - Glycosaminoglycans/metabolism
MH  - Human
MH  - Liver/metabolism
MH  - Liver Neoplasms/*pathology
MH  - Membrane Glycoproteins/genetics/metabolism/*physiology
MH  - Neoplasm Invasiveness
MH  - *Neoplasm Metastasis
MH  - Proteoglycans/genetics/metabolism/*physiology
MH  - Signal Transduction
RF  - 14
EDAT- 2002/01/05 10:00
MHDA- 2002/02/02 10:01
PST - ppublish
SO  - Nippon Rinsho 2001 Oct;59 Suppl 6:184-8.




UI  - 21607909
PMID- 11743640
DA  - 20011214
DCOM- 20020213
IS  - 1019-6439
VI  - 20
IP  - 1
DP  - 2002 Jan
TI  - Syndecan-1 expression in cancer of the uterine cervix: association with
      lymph node metastasis.
PG  - 39-43
AB  - The development of carcinoma is associated with alterations in the
      expression of many cell adhesion molecules. Syndecan-1 is a cell surface
      proteoglycan that binds cells to the extracellular matrix and changes its
      expression following malignant transformation in some tumors. Our purpose
      was to examine the pattern of syndecan-1 expression in cancer of the
      uterine cervix and assess the clinicopathological significance of
      syndecan-1 expression. A total of 106 tissue specimens (6 normal, 19
      cervical intraepithelial neoplasia (CIN) and 81 invasive cancer) were
      analyzed immunohistochemically. In addition, the corresponding expression
      of mRNA in tumor tissues was evaluated by reverse transcription-polymerase
      chain reaction (RT/PCR) in comparison with normal counterparts. Syndecan-1
      was positive in normal squamous cells except the basal cell layer. The
      intensity of syndecan-1 staining was the strongest in normal epithelium,
      followed by CIN, and invasive squamous cell carcinoma. Syndecan-1
      expression in cancer tissue tended to be higher in keratinizing type than
      non-keratinizing type and not found in adenocarcinoma. Syndecan-1
      expression was markedly decreased at the mRNA level in invasive squamous
      cell carcinoma as compared with that of normal uterine cervix.
      Interestingy, there was an inverse correlation between the expression of
      syndecan-1 in the primary site and lymph node metastasis, although there
      was no significant correlation between syndecan-1 expression and the
      prognosis. The results of the present study suggest that syndecan-1
      expression is associated with squamous tissues and plays a key role in the
      progression of the cancer of the uterine cervix especially in the
      metastatic process.
AD  - Department of Obstetrics and Gynecology, Yamaguchi University School of
      Medicine, Yamaguchi 755-8505, Japan. fnuma@po.cc.yamaguchi-u.ac.jp
FAU - Numa, Fumitaka
AU  - Numa F
FAU - Hirabayashi, Kei
AU  - Hirabayashi K
FAU - Kawasaki, Keiko
AU  - Kawasaki K
FAU - Sakaguchi, Yuko
AU  - Sakaguchi Y
FAU - Sugino, Norihiro
AU  - Sugino N
FAU - Suehiro, Yutaka
AU  - Suehiro Y
FAU - Suminami, Yoshinori
AU  - Suminami Y
FAU - Hirakawa, Hiroshi
AU  - Hirakawa H
FAU - Umayahara, Kenji
AU  - Umayahara K
FAU - Nawata, Shugo
AU  - Nawata S
FAU - Ogata, Hidenobu
AU  - Ogata H
FAU - Kato, Hiroshi
AU  - Kato H
LA  - eng
PT  - Journal Article
CY  - Greece
TA  - Int J Oncol
JID - 9306042
RN  - 0 (DNA Primers)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (syndecan)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Carcinoma, Adenosquamous/*metabolism/secondary
MH  - Cervical Intraepithelial Neoplasia/*metabolism/secondary
MH  - Cervix Neoplasms/*metabolism/secondary
MH  - Cervix Uteri/metabolism
MH  - DNA Primers/chemistry
MH  - Female
MH  - Human
MH  - Immunoenzyme Techniques
MH  - Leiomyoma/metabolism
MH  - Lymphatic Metastasis
MH  - Membrane Glycoproteins/*biosynthesis/genetics
MH  - Middle Age
MH  - Neoplasm Proteins/*biosynthesis/genetics
MH  - Proteoglycans/*biosynthesis/genetics
MH  - RNA, Messenger/biosynthesis
MH  - Reverse Transcriptase Polymerase Chain Reaction
EDAT- 2001/12/18 10:00
MHDA- 2002/02/14 10:01
PST - ppublish
SO  - Int J Oncol 2002 Jan;20(1):39-43.




UI  - 21600290
PMID- 11738054
DA  - 20011212
DCOM- 20020219
IS  - 0008-6363
VI  - 52
IP  - 3
DP  - 2001 Dec
TI  - Adhesion receptors of vascular smooth muscle cells and their functions.
PG  - 372-86
AB  - Vascular smooth muscle cells (SMCs) are present in several phenotypic
      states in blood vessels. They show a high degree of plasticity, undergoing
      rapid and reversible phenotypic changes in response to environmental
      stresses and vascular injury. Thereby, SMCs play an important role in
      development of atherosclerosis and restenosis after angioplasty and
      coronary bypass grafting. Many functions of SMCs, such as adhesion,
      migration, proliferation, contraction, differentiation and apoptosis are
      determined by surface adhesion receptors involved in cell-cell binding and
      interactions between cells and extracellular matrix (ECM) proteins. Some
      cell adhesion receptors are involved in intracellular signalling and
      participate in cellular response to different stimuli. The adhesion
      receptors of vascular SMCs discussed here include the ECM adhesion
      receptors integrins, alpha-dystroglycan and syndecans, as well as the
      cell-cell adhesion receptors cadherins and cell adhesion molecules. This
      review is intended to provide a generalised overview of the receptors
      expressed in vascular SMCs in relation to their functions and implications
      for vascular pathology.
AD  - Division of Cardiology, Department of Medicine, University of Leicester,
      Clinical Sciences Wing, Glenfield General Hospital, LE3 9QP, Leicester,
      UK. em9@le.ac.uk
FAU - Moiseeva, E P
AU  - Moiseeva EP
LA  - eng
PT  - Journal Article
PT  - Review
PT  - Review, Academic
CY  - Netherlands
TA  - Cardiovasc Res
JID - 0077427
RN  - 0 (Cadherins)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (Integrins)
RN  - 0 (Laminin)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (syndecan)
RN  - 146888-27-9 (43-156K dystrophin-associated glycoprotein)
SB  - IM
MH  - Cadherins/metabolism
MH  - Cardiovascular Diseases/metabolism
MH  - Cell Adhesion/physiology
MH  - Cell Adhesion Molecules/metabolism
MH  - Cytoskeletal Proteins/metabolism
MH  - Extracellular Matrix/metabolism
MH  - Human
MH  - Integrins/metabolism
MH  - Laminin/metabolism
MH  - Membrane Glycoproteins/metabolism
MH  - Muscle, Smooth, Vascular/*metabolism
MH  - Proteoglycans/metabolism
MH  - Receptors, Cell Surface/*metabolism
MH  - Support, Non-U.S. Gov't
RF  - 203
EDAT- 2001/12/12 10:00
MHDA- 2002/02/20 10:01
AID - S0008636301003996 [pii]
PST - ppublish
SO  - Cardiovasc Res 2001 Dec;52(3):372-86.




UI  - 21587766
PMID- 11731446
DA  - 20011203
DCOM- 20020103
IS  - 0008-5472
VI  - 61
IP  - 23
DP  - 2001 Dec 1
TI  - Interference of tenascin-C with syndecan-4 binding to fibronectin blocks
      cell adhesion and stimulates tumor cell proliferation.
PG  - 8586-94
AB  - Tenascin-C is an adhesion-modulatory extracellular matrix molecule that is
      highly expressed in tumors. To investigate the effect of tenascin-C on
      tumor cells, we analyzed its antiadhesive nature and effect on tumor cell
      proliferation in a fibronectin context. Glioblastoma and breast carcinoma
      cell adhesion was compromised by a mixed fibronectin/tenascin-C
      substratum, which concomitantly caused increased tumor-cell proliferation.
      We identified the antiadhesive mechanism as a specific interference of
      tenascin-C with cell binding to the HepII/syndecan-4 site in fibronectin
      through direct binding of tenascin-C to the 13th fibronectin type III
      repeat (FNIII13). Cell adhesion and proliferation levels were restored by
      the addition of FNIII13. Overexpression of syndecan-4, but not syndecan-1
      or -2, reverted the cell adhesion defect of tenascin-C. We characterized
      FNIII13 as the binding site for syndecan-4. Thus we describe a novel
      mechanism by which tenascin-C impairs the adhesive function of fibronectin
      through binding to FNIII13, thereby inhibiting the coreceptor function of
      syndecan-4 in fibronectin-induced integrin signaling.
AD  - Friedrich Miescher Institute for Biomedical Research, 4058 Basel,
      Switzerland.
FAU - Huang, W
AU  - Huang W
FAU - Chiquet-Ehrismann, R
AU  - Chiquet-Ehrismann R
FAU - Moyano, J V
AU  - Moyano JV
FAU - Garcia-Pardo, A
AU  - Garcia-Pardo A
FAU - Orend, G
AU  - Orend G
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Cancer Res
JID - 2984705R
RN  - 0 (Fibronectins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, Fibronectin)
RN  - 0 (Tenascin)
RN  - 0 (syndecan-4)
SB  - IM
MH  - Animal
MH  - Binding Sites
MH  - CHO Cells
MH  - Cell Adhesion/drug effects/physiology
MH  - Cell Division/drug effects/physiology
MH  - Cell Movement/drug effects/physiology
MH  - Chickens
MH  - Fibronectins/*metabolism
MH  - Hamsters
MH  - Human
MH  - Membrane Glycoproteins/*metabolism
MH  - Peptide Fragments/metabolism
MH  - Proteoglycans/*metabolism
MH  - Receptors, Fibronectin/biosynthesis
MH  - Support, Non-U.S. Gov't
MH  - Tenascin/*pharmacology
MH  - Tumor Cells, Cultured
EDAT- 2001/12/04 10:00
MHDA- 2002/01/05 10:01
URLF- http://cancerres.aacrjournals.org/cgi/content/full/61/23/8586
URLS- http://cancerres.aacrjournals.org/cgi/content/abstract/61/23/8586
PST - ppublish
SO  - Cancer Res 2001 Dec 1;61(23):8586-94.




UI  - 21581905
PMID- 11724824
DA  - 20011128
DCOM- 20020108
IS  - 0021-9525
VI  - 155
IP  - 5
DP  - 2001 Nov 26
TI  - Role of heparan sulfate as a tissue-specific regulator of FGF-4 and FGF
      receptor recognition.
PG  - 845-58
AB  - FGF signaling uses receptor tyrosine kinases that form high-affinity
      complexes with FGFs and heparan sulfate (HS) proteoglycans at the cell
      surface. It is hypothesized that assembly of these complexes requires
      simultaneous recognition of distinct sulfation patterns within the HS
      chain by FGF and the FGF receptor (FR), suggesting that tissue-specific HS
      synthesis may regulate FGF signaling. To address this, FGF-2 and FGF-4,
      and extracellular domain constructs of FR1-IIIc (FR1c) and FR2-IIIc
      (FR2c), were used to probe for tissue-specific HS in embryonic day 18
      mouse embryos. Whereas FGF-2 binds HS ubiquitously, FGF-4 exhibits a
      restricted pattern, failing to bind HS in the heart and blood vessels and
      failing to activate signaling in mouse aortic endothelial cells. This
      suggests that FGF-4 seeks a specific HS sulfation pattern, distinct from
      that of FGF-2, which is not expressed in most vascular tissues.
      Additionally, whereas FR2c binds all FGF-4-HS complexes, FR1c fails to
      bind FGF-4-HS in most tissues, as well as in Raji-S1 cells expressing
      syndecan-1. Proliferation assays using BaF3 cells expressing either FR1c
      or FR2c support these results. This suggests that FGF and FR recognition
      of specific HS sulfation patterns is critical for the activation of FGF
      signaling, and that synthesis of these patterns is regulated during
      embryonic development.
AD  - Department of Pathology and Laboratory Medicine, University of
      Wisconsin-Madison, Madison, WI 53706, USA.
FAU - Allen, B L
AU  - Allen BL
FAU - Filla, M S
AU  - Filla MS
FAU - Rapraeger, A C
AU  - Rapraeger AC
LA  - eng
ID  - R01-GM48850/GM/NIGMS
PT  - Journal Article
CY  - United States
TA  - J Cell Biol
JID - 0375356
RN  - 0 (Isoenzymes)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (Receptors, Fibroblast Growth Factor)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (carcinoplacental isoenzymes)
RN  - 0 (fibroblast growth factor receptor 1)
RN  - 0 (fibroblast growth factor-4)
RN  - 103107-01-3 (Fibroblast Growth Factor 2)
RN  - 62031-54-3 (Fibroblast Growth Factors)
RN  - 9005-49-6 (Heparin)
RN  - 9050-30-0 (Heparitin Sulfate)
RN  - EC 2.7.1.- (fibroblast growth factor receptor 2)
RN  - EC 2.7.11.- (Receptor Protein-Tyrosine Kinases)
SB  - IM
MH  - Animal
MH  - Brain/blood supply/embryology
MH  - Cells, Cultured
MH  - Embryo/metabolism
MH  - Endothelium, Vascular/cytology/metabolism
MH  - Fibroblast Growth Factor 2/chemistry/metabolism
MH  - Fibroblast Growth Factors/*metabolism
MH  - Heparin/pharmacology
MH  - Heparitin Sulfate/chemistry/*metabolism
MH  - Immunohistochemistry
MH  - Isoenzymes/genetics/metabolism
MH  - Kidney/cytology/embryology/metabolism
MH  - Liver/cytology/embryology/metabolism
MH  - Lung/cytology/embryology/metabolism
MH  - Mice
MH  - Molecular Structure
MH  - Myocardium/chemistry/metabolism
MH  - Protein Binding
MH  - Proto-Oncogene Proteins/*metabolism
MH  - Receptor Protein-Tyrosine Kinases/metabolism
MH  - Receptors, Fibroblast Growth Factor/*metabolism
MH  - Recombinant Fusion Proteins/metabolism
MH  - Signal Transduction/physiology
MH  - Skin/chemistry/cytology/embryology
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
EDAT- 2001/11/29 10:00
MHDA- 2002/01/10 10:01
PHST- 2001/Nov/26 [aheadofprint]
AID - 10.1083/jcb.200106075 [doi]
AID - jcb.200106075 [pii]
URLF- http://www.jcb.org/cgi/content/full/155/5/845
URLS- http://www.jcb.org/cgi/content/abstract/155/5/845
PST - ppublish
SO  - J Cell Biol 2001 Nov 26;155(5):845-58.




UI  - 21534862
PMID- 11676858
DA  - 20011025
DCOM- 20020111
IS  - 0910-5050
VI  - 92
IP  - 10
DP  - 2001 Oct
TI  - Reduced expression of syndecan-1 affects metastatic potential and clinical
      outcome in patients with colorectal cancer.
PG  - 1074-81
AB  - Syndecan-1 is a transmembrane heparansulfate proteoglycan which regulates
      cell-to-cell or cell-to-extracellular matrix interactions and may
      influence malignant cell behavior. We investigated the alterations of
      syndecan-1 expressions in colorectal cancers and analyzed the relationship
      between histological and clinical characteristics. Syndecan-1 protein
      expression in colorectal cancer tissues was investigated with
      immunohistochemical staining of resected specimens. In situ hybridization
      was performed using syndecan-1 riboprobe to confirm the transcriptional
      signals. Syndecan-1 mRNA expression in cancer cell lines cultured with or
      without methylation inhibitor was also analyzed by quantitative PCR. Out
      of 105 specimens tested, less than 25% of tumor cells were stained with
      anti-syndecan-1 monoclonal antibody in 36 (34.3%). In situ hybridization
      showed a similar staining profile to that of immunohistochemistry.
      Syndecan-1 mRNA expression was increased by the methylation inhibitor
      5-aza-2'-deoxycytidine, suggesting that the hypermethylation is involved
      in the suppression of syndecan-1 expression. Clinically, the incidence of
      metastasis to lymphnode or liver in patients with syndecan-1-negative
      tumors was significantly high. Among T1 colorectal cancers displaying a
      primary invasive phase, lymphnode metastasis, undifferentiated characters
      and 'budding' of cancer cells were more common in syndecan-1-negative
      tumors. The survival rate in patients with syndecan-1-negative tumors was
      decreased significantly in a stage-independent manner. These results
      suggest that the reduction of syndecan-1 expression in colorectal cancer
      cells, which is supposed to be regulated at the transcription level, is
      closely related to invasive character. The evaluation of syndecan-1
      expression in colorectal cancer may allow prediction of patients' survival
      after surgery.
AD  - Third Department of Internal Medicine, Asahikawa Medical College,
      Asahikawa 078-8510.
FAU - Fujiya, M
AU  - Fujiya M
FAU - Watari, J
AU  - Watari J
FAU - Ashida, T
AU  - Ashida T
FAU - Honda, M
AU  - Honda M
FAU - Tanabe, H
AU  - Tanabe H
FAU - Fujiki, T
AU  - Fujiki T
FAU - Saitoh, Y
AU  - Saitoh Y
FAU - Kohgo, Y
AU  - Kohgo Y
LA  - eng
PT  - Journal Article
CY  - Japan
TA  - Jpn J Cancer Res
JID - 8509412
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (RNA, Neoplasm)
RN  - 0 (syndecan)
RN  - 2353-33-5 (5-aza-2'-deoxycytidine)
RN  - 320-67-2 (Azacitidine)
SB  - IM
MH  - Adenocarcinoma/diagnosis/genetics/metabolism/pathology
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Azacitidine/*analogs & derivatives/pharmacology
MH  - Chi-Square Distribution
MH  - Colorectal Neoplasms/diagnosis/genetics/*metabolism/*pathology
MH  - Female
MH  - Human
MH  - Immunohistochemistry
MH  - In Situ Hybridization
MH  - Intestinal Mucosa/chemistry/metabolism
MH  - Lymphatic Metastasis
MH  - Male
MH  - Membrane Glycoproteins/analysis/genetics/immunology/*metabolism
MH  - Methylation/drug effects
MH  - Middle Age
MH  - *Neoplasm Metastasis
MH  - Neoplasm Staging
MH  - Prognosis
MH  - Proteoglycans/analysis/genetics/immunology/*metabolism
MH  - RNA, Messenger/genetics/metabolism
MH  - RNA, Neoplasm/genetics/metabolism
MH  - Survival Analysis
MH  - Tumor Cells, Cultured
EDAT- 2001/10/26 10:00
MHDA- 2002/01/12 10:01
PST - ppublish
SO  - Jpn J Cancer Res 2001 Oct;92(10):1074-81.




UI  - 21534861
PMID- 11676857
DA  - 20011025
DCOM- 20020111
IS  - 0910-5050
VI  - 92
IP  - 10
DP  - 2001 Oct
TI  - Loss of syndecan-1 and increased expression of heparanase in invasive
      esophageal carcinomas.
PG  - 1062-73
AB  - Heparan sulfate proteoglycans play important biological roles in cell-cell
      and cell-matrix adhesion, and are closely associated with growth factor
      actions. Loss of syndecan-1, a cell surface-bound heparan sulfate
      proteoglycan, has been reported for advanced head and neck carcinomas, and
      expression of endoglycosidic heparanase, which cleaves heparan sulfate
      glycosaminoglycans (HS-GAGs), is associated with invasion and metastatic
      potential of malignant tumors. Paraffin sections of 103 primary esophageal
      squamous cell carcinomas were immunohistochemically examined for the
      expression of syndecan-1 core protein, HS-GAGs and heparanase protein, and
      the results were compared with various clinicopathological parameters,
      such as invasion depth. For 16 cases, fresh tumor samples were
      quantitatively analyzed for heparanase and syndecan-1 mRNA expression by
      real-time RT-PCR in addition to the immunohistochemical studies.
      Syndecan-1 core protein and HS-GAGs expression was significantly decreased
      in pT2 and pT3 cases compared with their pTis and pT1 counterparts.
      Decreased expression of core protein and HS-GAGs was correlated with the
      incidence of lymphatic invasion, and venous involvement. Furthermore,
      decreased expression of HS-GAGs was correlated positively with the
      incidence of nodal metastasis and distant organ metastasis, and negatively
      with the grade of tumor cell differentiation. The percentage of
      cytoplasmic heparanase protein-positive cases increased significantly in
      pT2 and pT3 cases compared to that in pTis and pT1 cases, and this was
      associated with lymphatic invasion, and venous and lymph nodal
      involvement. The level of heparanase mRNA was inversely correlated with
      the degree of HS-GAGs expression rather than core protein. In conclusion,
      loss of syndecan-1 and heparanase overexpression in esophageal squamous
      cell carcinomas are closely associated with malignant potential. Regarding
      the mechanism of loss of HS-GAGs, heparanase upregulation appears to play
      an important role.
AD  - Department of Human Pathology, Tokyo Medical and Dental University,
      Bunkyo-ku, Tokyo 113-8519. mikami-s@sc.itc.keio.ac.jp
FAU - Mikami, S
AU  - Mikami S
FAU - Ohashi, K
AU  - Ohashi K
FAU - Usui, Y
AU  - Usui Y
FAU - Nemoto, T
AU  - Nemoto T
FAU - Katsube, K
AU  - Katsube K
FAU - Yanagishita, M
AU  - Yanagishita M
FAU - Nakajima, M
AU  - Nakajima M
FAU - Nakamura, K
AU  - Nakamura K
FAU - Koike, M
AU  - Koike M
LA  - eng
PT  - Journal Article
CY  - Japan
TA  - Jpn J Cancer Res
JID - 8509412
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Neoplasm)
RN  - 0 (syndecan)
RN  - EC 3.2.1.- (heparanase)
RN  - EC 3.2.1.31 (Glucuronidase)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Carcinoma, Squamous Cell/chemistry/enzymology/genetics/pathology
MH  - Esophageal Neoplasms/*chemistry/enzymology/genetics/*pathology
MH  - Esophagus/chemistry/cytology
MH  - Female
MH  - Glucuronidase/genetics/immunology/*metabolism
MH  - Heparan Sulfate Proteoglycan/metabolism
MH  - Human
MH  - Immunohistochemistry
MH  - Male
MH  - Membrane Glycoproteins/analysis/genetics/immunology/*metabolism
MH  - Middle Age
MH  - *Neoplasm Invasiveness
MH  - Proteoglycans/analysis/genetics/immunology/*metabolism
MH  - RNA, Neoplasm/genetics/metabolism
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Tumor Cells, Cultured
EDAT- 2001/10/26 10:00
MHDA- 2002/01/12 10:01
PST - ppublish
SO  - Jpn J Cancer Res 2001 Oct;92(10):1062-73.




UI  - 21530815
PMID- 11676398
DA  - 20011024
DCOM- 20011101
IS  - 0340-7004
VI  - 50
IP  - 7
DP  - 2001 Sep
TI  - Multiple myeloma cells are killed by syndecan-1-directed
      superantigen-activated T cells.
PG  - 382-90
AB  - Multiple myeloma (MM) is an incurable plasma cell/plasmablast malignancy
      with a great need for innovative treatment strategies. Since experimental
      immunotherapy with targeted superantigens (SAg) proved to be effective in
      other haematopoietic tumours, we investigated whether this would also hold
      true for MM. We used the bacterial SAg Staphylococcus enterotoxin A (SEA),
      a potent activator of T cell cytotoxicity by means of its binding to
      particular T cell receptor Vbeta sequences on effector cells and MHC class
      II molecules on target cells. To eliminate potentially unspecific binding
      via MHC class II, SEA was point mutated (SEAm). In a second step SEAm was
      genetically fused to protein A (PA), resulting in a fusion protein
      (PA-SEAm). This fusion protein was used together with four different
      plasma-cell-specific/associated mAbs to direct T cells towards 10 MM
      target cell lines. Three of these mAbs were directed against
      syndecan-1/CD138, known to be highly expressed on MM and plasma cells, but
      absent on other haematopoietic cells. All MM cell lines proved to be
      sensitive to SAg-activated T cell killing (15-50% lysis), as measured in a
      51Cr-release assay. This effect was clearly mediated via the
      plasma-cell-reactive antibodies, as control antibodies only conferred a
      low background lysis. MM therapy based on targeted SAgs could in theory be
      hampered by dysfunctional T cells in MM patients. However, we show that T
      cells from MM patients and healthy controls responded equally well to
      activation by SAg.
AD  - Clinical Immunology Division, Rudbeck Laboratory, Uppsala University,
      Sweden.
FAU - Ragnarsson, L
AU  - Ragnarsson L
FAU - Stromberg, T
AU  - Stromberg T
FAU - Wijdenes, J
AU  - Wijdenes J
FAU - Totterman, T H
AU  - Totterman TH
FAU - Weigelt, C
AU  - Weigelt C
LA  - eng
PT  - Journal Article
CY  - Germany
TA  - Cancer Immunol Immunother
JID - 8605732
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Enterotoxins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Superantigens)
RN  - 0 (syndecan)
RN  - 37337-57-8 (enterotoxin A, Staphylococcal)
SB  - IM
MH  - Antibodies, Monoclonal/immunology
MH  - Cell Line
MH  - Cytotoxicity, Immunologic
MH  - Enterotoxins/*immunology
MH  - Human
MH  - Immunotherapy
MH  - Lymphocyte Transformation
MH  - Membrane Glycoproteins/analysis/*immunology
MH  - Multiple Myeloma/immunology/*therapy
MH  - Proteoglycans/analysis/*immunology
MH  - Superantigens/*immunology
MH  - Support, Non-U.S. Gov't
MH  - T-Lymphocytes/*immunology
EDAT- 2001/10/26 10:00
MHDA- 2001/11/03 10:01
PST - ppublish
SO  - Cancer Immunol Immunother 2001 Sep;50(7):382-90.




UI  - 21525649
PMID- 11669479
DA  - 20011023
DCOM- 20011205
IS  - 0022-0345
VI  - 80
IP  - 8
DP  - 2001 Aug
TI  - Cell-surface proteoglycan expression by lymphocytes from peripheral blood
      and gingiva in health and periodontal disease.
PG  - 1704-10
AB  - Cell-surface proteoglycans are involved in lymphocyte migration and
      activation. This study investigated the expression of syndecan-1,
      syndecan-4, and glypican in peripheral blood lymphocytes and by
      lymphocytes in variously inflamed periodontal tissues. Gingival specimens
      from healthy, gingivitis, or chronic periodontitis sites were stained by
      means of antibodies against B- and T-lymphocytes and also syndecan-1,
      syndecan-4, and glypican. Syndecan-1 expression by peripheral blood
      mononuclear cells (PBMC) from healthy, gingivitis, and chronic
      periodontitis subjects was assessed by flow cytometry. Syndecan-1 was
      expressed by B-cells/plasma cells but not T-cells in both gingivitis and
      chronic periodontitis lesions. Both B-cells/plasma cells and T-cells in
      gingivitis and chronic periodontitis expressed syndecan-4. Glypican was
      expressed only by macrophages. Stimulation of PBMC with mitogens and
      growth factors modulated syndecan-1 expression in both the T- and B-cells.
      Thus, cell-surface proteoglycan expression by lymphocytes in periodontal
      inflammation is cell-type-specific and may be modulated by inflammation.
AD  - School of Dentistry, The University of Queensland, Brisbane, Australia.
FAU - Manakil, J F
AU  - Manakil JF
FAU - Sugerman, P B
AU  - Sugerman PB
FAU - Li, H
AU  - Li H
FAU - Seymour, G J
AU  - Seymour GJ
FAU - Bartold, P M
AU  - Bartold PM
LA  - eng
PT  - Journal Article
CY  - United States
TA  - J Dent Res
JID - 0354343
RN  - 0 (Growth Substances)
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Mitogens)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 0 (syndecan-4)
SB  - D
SB  - IM
MH  - Adult
MH  - Aged
MH  - Alveolar Bone Loss/metabolism/pathology
MH  - Analysis of Variance
MH  - B-Lymphocytes/metabolism/pathology
MH  - Chronic Disease
MH  - Female
MH  - Flow Cytometry
MH  - Gingiva/metabolism/*pathology
MH  - Gingival Hemorrhage/metabolism/pathology
MH  - Gingivitis/blood/metabolism/*pathology
MH  - Growth Substances/pharmacology
MH  - Heparan Sulfate Proteoglycan/*analysis
MH  - Human
MH  - Lymphocytes/metabolism/*pathology
MH  - Macrophages/metabolism/pathology
MH  - Male
MH  - Membrane Glycoproteins/*analysis
MH  - Middle Age
MH  - Mitogens/pharmacology
MH  - Periodontal Attachment Loss/metabolism/pathology
MH  - Periodontal Pocket/metabolism/pathology
MH  - Periodontitis/blood/metabolism/*pathology
MH  - Plasma Cells/metabolism/pathology
MH  - Proteoglycans/*analysis
MH  - Regression Analysis
MH  - Statistics
MH  - Support, Non-U.S. Gov't
MH  - T-Lymphocytes/metabolism/pathology
MH  - Tooth Cervix/pathology
EDAT- 2001/10/24 10:00
MHDA- 2002/01/05 10:01
PST - ppublish
SO  - J Dent Res 2001 Aug;80(8):1704-10.




UI  - 21482060
PMID- 11598898
DA  - 20011012
DCOM- 20011025
LR  - 20011102
IS  - 0021-9541
VI  - 189
IP  - 2
DP  - 2001 Nov
TI  - PR-39 coordinates changes in vascular smooth muscle cell adhesive strength
      and locomotion by modulating cell surface heparan sulfate-matrix
      interactions.
PG  - 133-43
AB  - PR-39 is proline-rich peptide produced at sites of tissue injury. While
      the functional properties of this peptide have not been fully defined,
      PR-39 may be an important regulator of processes related to cell-matrix
      adhesion since it reportedly upregulates syndecan-4, which is a critical
      determinant of focal adhesion formation. The ability of PR-39 to modulate
      the adhesion and chemokinetic migration behavior of arterial smooth muscle
      cells (SMCs) in a fashion coordinated with syndecan-4 expression was
      investigated. Treatment of SMCs with PR-39 did not alter syndecan-1 mRNA,
      but did induce a two-fold increase in syndecan-4 mRNA (P < 0.0001) and
      significantly enhanced cell surface expression of both syndecan-4 (P <
      0.01) and heparan sulfate (HS) (P < 0.05). These observations were
      consistent with an observed increase in cell-matrix adhesive strength (P <
      0.05) and a reduction in cell speed (P < 0.01) on fibronectin-coated
      substrates. Incubation of PR-39 treated cells with a soluble fibronectin
      derived heparin-binding peptide, as a competitive inhibitor of heparan
      sulfate/matrix interactions, abolished these effects. These data suggest
      that PR-39 mediated alterations of cell adhesion and motility may be
      related, in part, to the increased expression of heparan sulfate
      glycosaminoglycans (GAGs) that accompany the upregulation of cell surface
      syndecan-4. Furthermore, this investigation supports the notion that
      factors which control syndecan-4 expression may play an important role in
      regulating adhesion related cell processes.
CI  - Copyright 2001 Wiley-Liss, Inc.
AD  - School of Chemical Engineering, Georgia Institute of Technology, Atlanta,
      Georgia, USA.
FAU - Chon, J H
AU  - Chon JH
FAU - Houston, M M
AU  - Houston MM
FAU - Xu, C
AU  - Xu C
FAU - Chaikof, E L
AU  - Chaikof EL
LA  - eng
ID  - HL60963/HL/NHLBI
PT  - Journal Article
CY  - United States
TA  - J Cell Physiol
JID - 0050222
RN  - 0 (Antimicrobial Cationic Peptides)
RN  - 0 (Fibronectins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (syndecan-4)
RN  - 139637-11-9 (PR 39)
RN  - 9050-30-0 (Heparitin Sulfate)
SB  - IM
MH  - Animal
MH  - Antimicrobial Cationic Peptides/*pharmacology
MH  - *Cell Adhesion/drug effects
MH  - Cell Membrane/metabolism
MH  - *Cell Movement/drug effects
MH  - Dose-Response Relationship, Drug
MH  - Extracellular Matrix/*metabolism/physiology
MH  - Fibronectins/metabolism
MH  - Heparitin Sulfate/*metabolism/physiology
MH  - Membrane Glycoproteins/biosynthesis/genetics
MH  - Muscle, Smooth, Vascular/drug effects/*physiology
MH  - Proteoglycans/biosynthesis/genetics
MH  - RNA, Messenger/biosynthesis
MH  - Rats
MH  - Support, U.S. Gov't, P.H.S.
MH  - Tumor Cells, Cultured
MH  - Up-Regulation
EDAT- 2001/10/13 10:00
MHDA- 2001/10/26 10:01
AID - 10.1002/jcp.1050 [pii]
PST - ppublish
SO  - J Cell Physiol 2001 Nov;189(2):133-43.




UI  - 21482521
PMID- 11598177
DA  - 20011012
DCOM- 20011204
IS  - 0893-3952
VI  - 14
IP  - 10
DP  - 2001 Oct
TI  - Syndecan-1 (CD138) immunoreactivity in bone marrow biopsies of multiple
      myeloma: shed syndecan-1 accumulates in fibrotic regions.
PG  - 1052-8
AB  - Syndecan-1 (CD138) mediates myeloma cell adhesion, and loss of syndecan-1
      from the cell surface may contribute to myeloma proliferation and
      dissemination. Flow cytometry analysis of myeloma cells in bone marrow
      specimens shows heterogeneity in cell surface syndecan-1 expression. It is
      not known whether weaker expression correlates with more aggressive
      disease. However, recent reports suggest that variations in syndecan-1
      staining intensity on myeloma cells may be an artifact of specimen
      handling. In this study, we evaluate syndecan-1 expression in bone marrow
      biopsy sections from 28 multiple myeloma patients, to elucidate the
      heterogeneity of syndecan-1 expression in situ. Immunoreactivity for
      syndecan-1, using the antibody B-B4 (CD138), was found in more than 95% of
      multiple myeloma cells in 27 of 28 biopsies. However, one biopsy had more
      than 50% CD138-negative cells and cells with weak CD138 expression were
      identified in the majority of cases. Loss of syndecan-1 did not appear to
      relate to myeloma cell differentiation. In addition, syndecan-1 was
      detected on intravascular and intrasinusoidal myeloma cells suggesting
      that loss of syndecan-1 may not be required for extramedullary
      dissemination. Bone marrow biopsies from nine additional patients, with
      variable CD138 staining intensity on myeloma cells as determined by flow
      cytometry, were studied by immunohistochemistry. The heterogeneous CD138
      expression was confirmed in situ, with weakly positive cells concentrated
      in areas of reticulin fibrosis. These cells had a disrupted pattern of
      membrane staining in contrast to the strong linear membrane staining seen
      in the other multiple myeloma cells. In addition, the fibrotic stroma
      stained intensely for syndecan-1. Accumulation of syndecan-1 within the
      extracellular matrix of the marrow likely is derived by shedding of the
      molecule from the surface of myeloma cells. Because syndecan-1 can act to
      regulate the activity of heparan-binding growth factors, these reservoirs
      of syndecan-1 may play a critical role in promoting myeloma pathogenesis,
      or in regeneration of the tumor after chemotherapy.
AD  - Department of Pathology, University of Arkansas for Medical Sciences,
      Little Rock, Arkansas 72205, USA. bayerileneb@uams.edu
FAU - Bayer-Garner, I B
AU  - Bayer-Garner IB
FAU - Sanderson, R D
AU  - Sanderson RD
FAU - Dhodapkar, M V
AU  - Dhodapkar MV
FAU - Owens, R B
AU  - Owens RB
FAU - Wilson, C S
AU  - Wilson CS
LA  - eng
ID  - CA55819/CA/NCI
ID  - CA68494/CA/NCI
PT  - Journal Article
CY  - United States
TA  - Mod Pathol
JID - 8806605
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - IM
MH  - Biopsy
MH  - Bone Marrow/chemistry/*pathology
MH  - Fibrosis/metabolism/pathology
MH  - Flow Cytometry
MH  - Human
MH  - Immunohistochemistry
MH  - Membrane Glycoproteins/*analysis
MH  - Multiple Myeloma/metabolism/*pathology
MH  - Proteoglycans/*analysis
MH  - Support, U.S. Gov't, P.H.S.
EDAT- 2001/10/13 10:00
MHDA- 2002/01/05 10:01
URLF- http://modpath.uscapjournals.org/cgi/content/full/14/10/1052
URLS- http://modpath.uscapjournals.org/cgi/content/abstract/14/10/1052
PST - ppublish
SO  - Mod Pathol 2001 Oct;14(10):1052-8.




UI  - 21452799
PMID- 11568003
DA  - 20010924
DCOM- 20011204
IS  - 0006-4971
VI  - 98
IP  - 7
DP  - 2001 Oct 1
TI  - Sperm protein 17 is expressed on normal and malignant lymphocytes and
      promotes heparan sulfate-mediated cell-cell adhesion.
PG  - 2160-5
AB  - Sperm protein 17 (Sp17) is a highly conserved mammalian protein present on
      acrosome-reacted sperm that is thought to promote fertilization by binding
      sulfated carbohydrates of the oocyte zona pellucida. Although Sp17 was
      originally described as a testis-specific antigen, emerging evidence
      indicates that it may be more ubiquitously expressed than was previously
      thought. With the use of a specific antiserum, Sp17 was found to be
      present on the surface of malignant lymphoid cells, including B- and
      T-lymphoid cell lines, and on the surface of primary cells isolated from 2
      patients having B-lymphoid tumors. Surprisingly, circulating B lymphocytes
      isolated from healthy volunteers also expressed Sp17, while circulating T
      lymphocytes exhibited only very weak expression. The role of Sp17 in
      promoting lymphoid cell adhesion was addressed with the use of recombinant
      Sp17 (rSp17). The rSp17 binds to the surface of myeloma cells but not to
      cells pretreated with heparitinase, an enzyme that removes heparan sulfate
      from the cell surface. Moreover, rSp17 promotes extensive aggregation of
      cells that express the syndecan-1 heparan sulfate proteoglycan, but in
      contrast, cells lacking syndecan-1 expression fail to aggregate in the
      presence of rSp17. These findings suggest that Sp17 promotes heparan
      sulfate-mediated cell aggregation and thereby plays a role in regulating
      adhesion and migration of normal and malignant lymphocytes.
AD  - Arkansas Cancer Research Center, Departments of Pathology and Anatomy,
      University of Arkansas for Medical Sciences, Little Rock, AR 72205, USA.
FAU - Lacy, H M
AU  - Lacy HM
FAU - Sanderson, R D
AU  - Sanderson RD
LA  - eng
ID  - CA55819/CA/NCI
ID  - CA68494/CA/NCI
PT  - Journal Article
CY  - United States
TA  - Blood
JID - 7603509
RN  - 0 (Carrier Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (zona pellucida-binding protein Sp17)
RN  - 9050-30-0 (Heparitin Sulfate)
SB  - AIM
SB  - IM
MH  - Carrier Proteins/genetics/*metabolism/*pharmacology
MH  - Cell Adhesion/drug effects
MH  - Cell Movement/drug effects
MH  - Fluorescent Antibody Technique, Indirect
MH  - Heparitin Sulfate/*pharmacology
MH  - Human
MH  - Lymphocytes/*chemistry/cytology
MH  - Multiple Myeloma/pathology
MH  - RNA, Messenger/analysis
MH  - Support, U.S. Gov't, P.H.S.
MH  - Tumor Cells, Cultured
EDAT- 2001/09/25 10:00
MHDA- 2002/01/05 10:01
URLF- http://www.bloodjournal.org/cgi/content/full/98/7/2160
URLS- http://www.bloodjournal.org/cgi/content/abstract/98/7/2160
PST - ppublish
SO  - Blood 2001 Oct 1;98(7):2160-5.




UI  - 21441837
PMID- 11557783
DA  - 20010914
DCOM- 20011011
IS  - 0893-3952
VI  - 14
IP  - 9
DP  - 2001 Sep
TI  - Plasma cells in chronic endometritis are easily identified when stained
      with syndecan-1.
PG  - 877-9
AB  - BACKGROUND: Chronic endometritis has been observed in 3-10% of women with
      irregular uterine bleeding who undergo endometrial biopsy. The diagnosis
      of chronic endometritis rests on the recognition of plasma cells in
      endometrial tissue that may show a prominent spindle cell stromal
      component, and is frequently difficult to date. Syndecan-1 is a
      cell-surface proteoglycan that is expressed on the cell surface of plasma
      cells. DESIGN: Eighteen endometrial curettage cases with the diagnosis of
      chronic endometritis and 25 endometrial curettage cases of dysfunctional
      uterine bleeding, in females under the age of thirty-five in whom no other
      histopathologic changes were noted, were reviewed for the presence of
      plasma cells. Sections were then stained with syndecan-1. RESULTS: All of
      the chronic endometritis cases showed easily visible syndecan-1 staining
      of plasma cell membranes. None of the cases of dysfunctional uterine
      bleeding showed presence of plasma cells in either the hematoxylin and
      eosin stained or syndecan-1 stained sections. CONCLUSIONS: In cases of
      suspected chronic endometritis in which no plasma cells can be found on
      hematoxylin and eosin stained slides, syndecan-1 may be an effective
      adjunct in the identification of plasma cells and thus aid in the
      diagnosis of chronic endometritis.
AD  - Department of Pathology, University of Arkansas for Medical Sciences,
      Little Rock, Arkansas 72205, USA.
FAU - Bayer-Garner, I B
AU  - Bayer-Garner IB
FAU - Korourian, S
AU  - Korourian S
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Mod Pathol
JID - 8806605
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - IM
MH  - Chronic Disease
MH  - Endometritis/*metabolism/pathology
MH  - Female
MH  - Human
MH  - Immunohistochemistry
MH  - Membrane Glycoproteins/*analysis
MH  - Plasma Cells/*chemistry/pathology
MH  - Proteoglycans/*analysis
MH  - Staining and Labeling
EDAT- 2001/09/15 10:00
MHDA- 2001/10/12 10:01
URLF- http://modpath.uscapjournals.org/cgi/content/full/14/9/877
URLS- http://modpath.uscapjournals.org/cgi/content/abstract/14/9/877
PST - ppublish
SO  - Mod Pathol 2001 Sep;14(9):877-9.




UI  - 21424503
PMID- 11533182
DA  - 20010904
DCOM- 20011011
IS  - 0022-538X
VI  - 75
IP  - 19
DP  - 2001 Oct
TI  - Syndecans serve as attachment receptors for human immunodeficiency virus
      type 1 on macrophages.
PG  - 9187-200
AB  - Macrophages are thought to represent one of the first cell types in the
      body to be infected during the early stage of human immunodeficiency virus
      type 1 (HIV-1) transmission and represent a potential viral reservoir in
      vivo. Thus, an understanding of HIV-1 attachment to these cells is
      fundamental to the development of novel anti-HIV-1 therapies. Although one
      of the major targets of HIV-1 in vivo--CD4(+) T lymphocytes--express high
      CD4 levels, other major targets such as macrophages do not. We asked in
      this study whether this low CD4 level on macrophages is sufficient to
      support HIV-1 attachment to these cells or whether cell surface proteins
      other than CD4 are required for this process. We show that CD4 alone is
      not sufficient to support the initial adsorption of HIV-1 to macrophages.
      Importantly, we find that heparan sulfate proteoglycans (HSPGs) serve as
      the main class of attachment receptors for HIV-1 on macrophages. Most
      importantly, we demonstrate that a single family of HSPGs, the syndecans,
      efficiently mediates HIV-1 attachment and represents an abundant class of
      attachment receptors on macrophages.
AD  - Department of Immunology, The Scripps Research Institute, La Jolla,
      California 92037, USA.
FAU - Saphire, A C
AU  - Saphire AC
FAU - Bobardt, M D
AU  - Bobardt MD
FAU - Zhang, Z
AU  - Zhang Z
FAU - David, G
AU  - David G
FAU - Gallay, P A
AU  - Gallay PA
LA  - eng
PT  - Journal Article
CY  - United States
TA  - J Virol
JID - 0113724
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, HIV)
RN  - 0 (syndecan)
SB  - IM
MH  - HIV Infections/metabolism/*virology
MH  - HIV-1/*physiology
MH  - Hela Cells
MH  - Human
MH  - Macrophages/metabolism/*virology
MH  - Membrane Glycoproteins/*physiology
MH  - Proteoglycans/*physiology
MH  - Receptors, HIV/*physiology
MH  - Support, Non-U.S. Gov't
MH  - Virus Replication
EDAT- 2001/09/05 10:00
MHDA- 2001/10/12 10:01
AID - 10.1128/JVI.75.19.9187-9200.2001 [doi]
URLF- http://jvi.asm.org/cgi/content/full/75/19/9187
URLS- http://jvi.asm.org/cgi/content/abstract/75/19/9187
PST - ppublish
SO  - J Virol 2001 Oct;75(19):9187-200.




UI  - 21421121
PMID- 11529866
DA  - 20010831
DCOM- 20010927
IS  - 0007-1048
VI  - 114
IP  - 2
DP  - 2001 Aug
TI  - Evidence of a role for a non-matrix-type metalloproteinase activity in the
      shedding of syndecan-1 from human myeloma cells.
PG  - 414-21
AB  - Syndecan-1 is a cell surface proteoglycan that is expressed on human
      myeloma cells and is thought to act as a co-receptor for certain
      extracellular matrix proteins and growth factors. The ectodomain of
      syndecan-1 is thought to be shed from the surface of myeloma cells,
      although the exact mechanism of release remains unclear. In this study, we
      used a panel of inhibitors to identify the class of proteinase responsible
      for shedding the soluble syndecan-1 ectodomain from human myeloma cells.
      Using enzyme-linked immunosorbent assay, flow cytometry and
      immunocytochemistry, we demonstrated that myeloma cell lines expressed
      syndecan-1 on their surface and that this was shed constitutively, but to
      a varying extent. In addition, phorbol 12-myristate 13-acetate (PMA), an
      activator of protein kinase C, stimulated a marked loss of cell surface
      syndecan-1 from each of the cell lines and this was associated with a
      corresponding increase in soluble syndecan-1. Inhibitors of serine and
      cysteine proteinases, and matrix-type metalloproteinases, did not inhibit
      constitutive or PMA-stimulated syndecan-1 shedding from JJN3 and RPMI 8226
      cells. However, BB-94, a hydroxamate-based, broad-spectrum,
      metalloproteinase inhibitor, substantially suppressed constitutive and
      PMA-stimulated syndecan-1 loss from myeloma cells. These data indicate
      that a non-matrix-type metalloproteinase is responsible for syndecan-1
      shedding from the surface of myeloma cells.
AD  - Division of Genomic Medicine, University of Sheffield Medical School,
      Sheffield, UK.
FAU - Holen, I
AU  - Holen I
FAU - Drury, N L
AU  - Drury NL
FAU - Hargreaves, P G
AU  - Hargreaves PG
FAU - Croucher, P I
AU  - Croucher PI
LA  - eng
PT  - Journal Article
CY  - England
TA  - Br J Haematol
JID - 0372544
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Isothiocyanates)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 16561-29-8 (Tetradecanoylphorbol Acetate)
RN  - 2321-07-5 (Fluorescein)
RN  - 3129-90-6 (isothiocyanic acid)
RN  - EC 2.7.1.- (Protein Kinase C)
RN  - EC 3.4.24 (Metalloendopeptidases)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Cell Membrane/chemistry
MH  - Flow Cytometry
MH  - Fluorescein
MH  - Human
MH  - Immunohistochemistry/methods
MH  - Isothiocyanates/immunology
MH  - Membrane Glycoproteins/analysis/*metabolism/secretion
MH  - Metalloendopeptidases/*metabolism
MH  - Multiple Myeloma/*metabolism/secretion
MH  - Protein Kinase C/metabolism
MH  - Proteoglycans/analysis/*metabolism/secretion
MH  - Statistics, Nonparametric
MH  - Stimulation, Chemical
MH  - Support, Non-U.S. Gov't
MH  - Tetradecanoylphorbol Acetate/pharmacology
MH  - Tumor Cells, Cultured/metabolism
EDAT- 2001/09/01 10:00
MHDA- 2001/09/28 10:01
AID - bjh2963 [pii]
PST - ppublish
SO  - Br J Haematol 2001 Aug;114(2):414-21.




UI  - 21413623
PMID- 11522680
DA  - 20010827
DCOM- 20010920
IS  - 0012-1797
VI  - 50
IP  - 9
DP  - 2001 Sep
TI  - Changes in matrix proteoglycans induced by insulin and fatty acids in
      hepatic cells may contribute to dyslipidemia of insulin resistance.
PG  - 2126-32
AB  - Insulin resistance and type 2 diabetes are associated with elevated
      circulating levels of insulin, nonesterified fatty acids (NEFAs), and
      lipoprotein remnants. Extracellular matrix proteoglycan (PG) alterations
      are also common in macro- and microvascular complications of type 2
      diabetes. In liver, extracellular heparan sulfate (HS) PGs contribute to
      the uptake of triglyceride-rich lipoprotein remnants. We found that HepG2
      cells cultured with 10 or 50 nmol/l insulin or 300 micromol/l
      albumin-bound linoleic acid changed their PG secretion. The
      glycosaminoglycans (GAGs) of the secreted PGs from insulin-treated HepG2
      cells were enriched in chondroitin sulfate (CS) PGs. In contrast, cells
      exposed to linoleic acid secreted PGs with decreased content of CS.
      Insulin caused a moderate increase in mRNA for versican (secreted CS PG),
      whereas linoleic acid markedly decreased mRNA for versican in HepG2 cells,
      as did the peroxisomal proliferator-activated receptor-alpha agonist
      bezafibrate. The effects of insulin or linoleic acid on syndecan 1, a cell
      surface HS PG, were similar to those on versican, but less pronounced. The
      livers of obese Zucker fa/fa rats, which are insulin-resistant and have
      high levels of insulin, NEFAs, and triglyceride-rich remnants, showed
      increased expression of CS PGs when compared with lean littermates. These
      changes in PG composition decreased the affinity of remnant beta-VLDL
      particles to PGs isolated from insulin-treated HepG2 cells and obese rat
      livers. The results indicated that insulin and NEFAs modulate the
      expression of PGs in hepatic cells. We speculate that in vivo this
      exchange of CS for HS may reduce the clearance of remnant beta-VLDLs and
      contribute to the dyslipidemia of insulin resistance.
AD  - Wallenberg Laboratory for Cardiovascular Research, Goteborg University,
      Sahlgrenska University Hospital, Goteborg, Sweden.
FAU - Olsson, U
AU  - Olsson U
FAU - Egnell, A C
AU  - Egnell AC
FAU - Lee, M R
AU  - Lee MR
FAU - Lunden, G O
AU  - Lunden GO
FAU - Lorentzon, M
AU  - Lorentzon M
FAU - Salmivirta, M
AU  - Salmivirta M
FAU - Bondjers, G
AU  - Bondjers G
FAU - Camejo, G
AU  - Camejo G
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Diabetes
JID - 0372763
RN  - 0 (Fatty Acids)
RN  - 0 (Lipoproteins, VLDL)
RN  - 0 (Proteoglycans)
RN  - 11061-68-0 (Insulin)
RN  - 2197-37-7 (Linoleic Acid)
SB  - AIM
SB  - IM
MH  - Animal
MH  - Cell Line
MH  - Extracellular Matrix/metabolism
MH  - Fatty Acids/*pharmacology
MH  - Human
MH  - Hyperlipidemia/*etiology
MH  - Insulin/*pharmacology
MH  - Insulin Resistance/*physiology
MH  - Linoleic Acid/pharmacology
MH  - Lipoproteins, VLDL/blood
MH  - Liver/cytology/*metabolism
MH  - Obesity/genetics/metabolism
MH  - Proteoglycans/metabolism/*physiology
MH  - Rats
MH  - Rats, Zucker/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Thinness
EDAT- 2001/08/28 10:00
MHDA- 2001/09/21 10:01
URLF- http://diabetes.diabetes.org/cgi/content/full/50/9/2126
URLS- http://diabetes.diabetes.org/cgi/content/abstract/50/9/2126
PST - ppublish
SO  - Diabetes 2001 Sep;50(9):2126-32.




UI  - 21412462
PMID- 11521692
DA  - 20010827
DCOM- 20020114
IS  - 0721-832X
VI  - 239
IP  - 7
DP  - 2001 Jul
TI  - Alterations in expression of mucin, tenascin-c and syndecan-1 in the
      conjunctiva following retinal surgery and plaque radiotherapy.
PG  - 488-95
AB  - PURPOSE: Disturbances of the ocular tear film layer and dry eye symptoms
      are common complications following retinal surgery and ocular tumour
      therapy. Examined were the histopathological changes of the conjunctiva
      following posterior segment surgery and plaque radiotherapy. METHODS:
      Biopsy specimens of the superior bulbar conjunctiva were obtained during
      cataract surgery between 2 weeks and 7 years following vitrectomy (n=92)
      or plaque radiotherapy for uveal melanoma (n=20) and from control subjects
      without previous ocular surgery (n=29). These were examined using
      conventional histology (HE, PAS, Van Gieson) and immunochemistry [APAAP,
      using antibodies directed against MUC1, MUC5AC, syndecan-1 and tenascin-C
      (TN-C)]. The histopathological changes were graded and statistical
      analysis was performed using Wilcoxon and Kruskal-Wallis rank sum tests.
      RESULTS: Conjunctival specimens of patients following vitrectomy or plaque
      radiotherapy for uveal melanoma demonstrated increased epithelial
      stratification, a significant decrease in the number of PAS- and
      MUC5AC-positive goblet cells, and distributional changes in expression of
      MUC1, syndecan- and TN-C within conjunctival epithelium or stroma. These
      alterations - in particular the goblet cell reduction and stromal fibrosis
      - were most prominent in those patients who had undergone radiotherapy.
      CONCLUSIONS: Posterior segment surgery can lead to morphological
      alterations of the conjunctiva and distributional changes in ocular
      mucins, which may cause dry eye symptoms.
AD  - Department of Ophthalmology, University Hospital Benjamin Franklin, Free
      University, Berlin, Germany. heimann@ukbf.fu-berlin.de
FAU - Heimann, H
AU  - Heimann H
FAU - Coupland, S E
AU  - Coupland SE
FAU - Gochman, R
AU  - Gochman R
FAU - Hellmich, M
AU  - Hellmich M
FAU - Foerster, M H
AU  - Foerster MH
LA  - eng
PT  - Journal Article
CY  - Germany
TA  - Graefes Arch Clin Exp Ophthalmol
JID - 8205248
RN  - 0 (Eye Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Mucins)
RN  - 0 (Proteoglycans)
RN  - 0 (Tenascin)
RN  - 0 (syndecan)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - *Brachytherapy
MH  - Conjunctiva/*metabolism
MH  - Dry Eye Syndromes/metabolism
MH  - Eye Proteins/*metabolism
MH  - Female
MH  - Human
MH  - Immunoenzyme Techniques
MH  - Male
MH  - Melanoma/radiotherapy
MH  - Membrane Glycoproteins/*metabolism
MH  - Middle Age
MH  - Mucins/*metabolism
MH  - Proteoglycans/*metabolism
MH  - Retinal Diseases/surgery
MH  - Tenascin/*metabolism
MH  - Uveal Neoplasms/radiotherapy
MH  - *Vitrectomy
EDAT- 2001/08/28 10:00
MHDA- 2002/01/15 10:01
PST - ppublish
SO  - Graefes Arch Clin Exp Ophthalmol 2001 Jul;239(7):488-95.




UI  - 21361178
PMID- 11468178
DA  - 20010724
DCOM- 20010913
IS  - 0006-4971
VI  - 98
IP  - 3
DP  - 2001 Aug 1
TI  - Identifying intercellular signaling genes expressed in malignant plasma
      cells by using complementary DNA arrays.
PG  - 771-80
AB  - In multiple myeloma (MM), the growth of primary plasma cells depends not
      only on interleukin-6 (IL-6), but also on additional unidentified signals
      delivered by the bone marrow environment. Using Atlas complementary DNA
      (cDNA) arrays comprising 268 genes coding for intercellular signaling
      molecules, this study identified genes that are overexpressed in myeloma
      cells compared to autologous B-lymphoblastoid cell lines. These genes
      encode the oncogenic Tyro3 tyrosine kinase receptor, the heparin-binding
      epidermal growth factor-like growth factor (HB-EGF) that is an epithelial
      autocrine tumor growth factor, the thrombin receptor (TR) that is linked
      to HB-EGF and syndecan-1 processing and to cell invasion, chemokine
      receptors CCR1 and CCR2, the Wnt pathway actor Frizzled-related protein
      (FRZB), and the Notch receptor ligand Jagged 2. These data, obtained with
      the Atlas cDNA array, were confirmed by reverse transcriptase-polymerase
      chain reaction or protein analysis or both. Furthermore, Tyro3, HB-EGF,
      TR, and FRZB gene expression was documented in purified primary malignant
      plasma cells from patients with plasma cell leukemia or MM. HB-EGF and
      FRZB were poorly expressed in purified polyclonal plasma cells. Finally,
      HB-EGF was proved to be an essential autocrine growth factor for the XG-1
      myeloma cells. This study shows the potency and the biologic relevance of
      cDNA arrays used to analyze simultaneously a large panel of intercellular
      signaling genes and, by identifying several genes overexpressed in
      malignant plasma cells, opens new fields of investigation in MM biology.
      (Blood. 2001;98:771-780)
AD  - INSERM U475, Unit for Cellular Therapy, CHU Montpellier, 99 Rue Puech
      Villa, 34197 Montpellier Cedex 5, France.
FAU - De Vos, J
AU  - De Vos J
FAU - Couderc, G
AU  - Couderc G
FAU - Tarte, K
AU  - Tarte K
FAU - Jourdan, M
AU  - Jourdan M
FAU - Requirand, G
AU  - Requirand G
FAU - Delteil, M C
AU  - Delteil MC
FAU - Rossi, J F
AU  - Rossi JF
FAU - Mechti, N
AU  - Mechti N
FAU - Klein, B
AU  - Klein B
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Blood
JID - 7603509
RN  - 0 (Neoplasm Proteins)
RN  - 149176-25-0 (heparin-binding EGF-like growth factor)
RN  - 62229-50-9 (Epidermal Growth Factor)
SB  - AIM
SB  - IM
MH  - B-Lymphocytes/metabolism
MH  - Cell Division/drug effects
MH  - Epidermal Growth Factor/metabolism
MH  - Flow Cytometry
MH  - Gene Expression/genetics
MH  - Human
MH  - Multiple Myeloma/genetics/*metabolism/pathology
MH  - Neoplasm Proteins/genetics/metabolism
MH  - Oligonucleotide Array Sequence Analysis/*methods
MH  - Plasma Cells/*metabolism/pathology
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Signal Transduction/*genetics
MH  - Support, Non-U.S. Gov't
MH  - Tumor Cells, Cultured
EDAT- 2001/07/27 10:00
MHDA- 2001/09/14 10:01
URLF- http://www.bloodjournal.org/cgi/content/full/98/3/771
URLS- http://www.bloodjournal.org/cgi/content/abstract/98/3/771
PST - ppublish
SO  - Blood 2001 Aug 1;98(3):771-80.




UI  - 21354315
PMID- 11461706
DA  - 20010719
DCOM- 20010809
LR  - 20011102
IS  - 0092-8674
VI  - 106
IP  - 1
DP  - 2001 Jul 13
TI  - Transgenic expression of syndecan-1 uncovers a physiological control of
      feeding behavior by syndecan-3.
PG  - 105-16
AB  - Transgenic expression in the hypothalamus of syndecan-1, a cell surface
      heparan sulfate proteoglycan (HSPG) and modulator of ligand-receptor
      encounters, produces mice with hyperphagia and maturity-onset obesity
      resembling mice with reduced action of alpha melanocyte stimulating
      hormone (alphaMSH). Via their HS chains, syndecans potentiate the action
      of agouti-related protein and agouti signaling protein, endogenous
      inhibitors of alphaMSH. In wild-type mice, syndecan-3, the predominantly
      neural syndecan, is expressed in hypothalamic regions that control energy
      balance. Food deprivation increases hypothalamic syndecan-3 levels
      several-fold. Syndecan-3 null mice, otherwise apparently normal, respond
      to food deprivation with markedly reduced reflex hyperphagia. We propose
      that oscillation of hypothalamic syndecan-3 levels physiologically
      modulates feeding behavior.
AD  - Division of Newborn Medicine, Department of Pediatrics and Cell Biology,
      Harvard Medical School, 300 Longwood Avenue, Boston, MA 02115, USA.
      oreizes@go.com
FAU - Reizes, O
AU  - Reizes O
FAU - Lincecum, J
AU  - Lincecum J
FAU - Wang, Z
AU  - Wang Z
FAU - Goldberger, O
AU  - Goldberger O
FAU - Huang, L
AU  - Huang L
FAU - Kaksonen, M
AU  - Kaksonen M
FAU - Ahima, R
AU  - Ahima R
FAU - Hinkes, M T
AU  - Hinkes MT
FAU - Barsh, G S
AU  - Barsh GS
FAU - Rauvala, H
AU  - Rauvala H
FAU - Bernfield, M
AU  - Bernfield M
LA  - eng
ID  - DK28506/DK/NIDDK
ID  - HD06763/HD/NICHD
ID  - HD18655/HD/NICHD
PT  - Journal Article
CY  - United States
TA  - Cell
JID - 0413066
RN  - 0 (Blood Glucose)
RN  - 0 (Leptin)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, Fibroblast Growth Factor)
RN  - 0 (syndecan)
RN  - 0 (syndecan 3)
RN  - 103107-01-3 (Fibroblast Growth Factor 2)
RN  - 11061-68-0 (Insulin)
RN  - 50-22-6 (Corticosterone)
RN  - 581-05-5 (alpha-MSH)
SB  - IM
MH  - Aging/physiology
MH  - Amino Acid Sequence
MH  - Animal
MH  - Blood Glucose/metabolism
MH  - Corticosterone/blood
MH  - Feeding Behavior/*physiology
MH  - Female
MH  - Fibroblast Growth Factor 2/metabolism
MH  - Food Deprivation
MH  - Human
MH  - Hyperphagia/genetics/physiopathology
MH  - Hypothalamus/*physiology
MH  - Insulin/blood
MH  - Leptin/blood
MH  - Male
MH  - Membrane Glycoproteins/chemistry/deficiency/genetics/*physiology
MH  - Mice
MH  - Mice, Knockout
MH  - Mice, Transgenic
MH  - Molecular Sequence Data
MH  - Mutagenesis
MH  - Obesity/genetics/physiopathology
MH  - Proteoglycans/chemistry/deficiency/genetics/*physiology
MH  - Receptors, Fibroblast Growth Factor/physiology
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
MH  - alpha-MSH/metabolism
EDAT- 2001/07/20 10:00
MHDA- 2001/08/10 10:01
AID - S0092867401004159 [pii]
PST - ppublish
SO  - Cell 2001 Jul 13;106(1):105-16.




UI  - 21348456
PMID- 11455001
DA  - 20010716
DCOM- 20010830
IS  - 0893-3952
VI  - 14
IP  - 7
DP  - 2001 Jul
TI  - Analysis of MUM1/IRF4 protein expression using tissue microarrays and
      immunohistochemistry.
PG  - 686-94
AB  - The gene encoding MUM1 was characterized as a possible translocation
      partner in chromosomal abnormalities involving a significant number of
      multiple myelomas. The overexpression of the MUM1 protein as a result of
      translocation t(6;14) (p25;q32) identified MUM1 as a putative regulatory
      molecule involved in B-cell differentiation and tumorigenesis. The
      expression of MUM1 protein in multiple myelomas supports this hypothesis.
      In the current study, using tissue microarray technology, we have tested
      the expression of the MUM1 protein in 1335 human malignancies and normal
      tissues. Our data show that the MUM1 protein is expressed in a wide
      spectrum of hematolymphoid neoplasms and in malignant melanomas but is
      absent in other human tumors. In addition, in tissue microarrays as well
      as in conventional paraffin sections, MUM1 staining was found to lack
      specificity in detecting plasmacytic differentiation as compared with two
      markers, CD138/Syndecan and VS38, commonly used in paraffin
      immunohistochemistry for detection of plasma cells.
AD  - Department of Pathology, Stanford University Medical Center, Stanford,
      California 94305, USA. ynatkunam@yahoo.com
FAU - Natkunam, Y
AU  - Natkunam Y
FAU - Warnke, R A
AU  - Warnke RA
FAU - Montgomery, K
AU  - Montgomery K
FAU - Falini, B
AU  - Falini B
FAU - van De Rijn, M
AU  - van De Rijn M
LA  - eng
ID  - CA34233/CA/NCI
PT  - Journal Article
CY  - United States
TA  - Mod Pathol
JID - 8806605
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Transcription Factors)
RN  - 0 (lymphoid-specific interferon regulatory factor)
RN  - 0 (monoclonal antibody VS38)
RN  - 0 (syndecan)
SB  - IM
MH  - Antibodies, Monoclonal/analysis
MH  - DNA-Binding Proteins/*analysis/metabolism
MH  - Human
MH  - Immunohistochemistry
MH  - Lymphoma, B-Cell/metabolism/pathology
MH  - Membrane Glycoproteins/analysis
MH  - Proteoglycans/analysis
MH  - Support, U.S. Gov't, P.H.S.
MH  - Tissue Distribution
MH  - Transcription Factors/*analysis/metabolism
EDAT- 2001/07/17 10:00
MHDA- 2001/08/31 10:01
URLF- /cgi/content/full/14/7/686
URLS- /cgi/content/abstract/14/7/686
PST - ppublish
SO  - Mod Pathol 2001 Jul;14(7):686-94.




UI  - 21347237
PMID- 11454708
DA  - 20010716
DCOM- 20010802
IS  - 0008-5472
VI  - 61
IP  - 14
DP  - 2001 Jul 15
TI  - Glypican-1 is overexpressed in human breast cancer and modulates the
      mitogenic effects of multiple heparin-binding growth factors in breast
      cancer cells.
PG  - 5562-9
AB  - Glypicans are a family of glycosylphosphatidylinositol-anchored cell
      surface heparan sulfate proteoglycans implicated in the control of
      cellular growth and differentiation. Here we show that glypican-1 is
      strongly expressed in human breast cancers, whereas expression of
      glypican-1 is low in normal breast tissues. In contrast, the expression of
      glypican-3 and -4 is only slightly increased in breast cancers by
      comparison with normal breast tissues, and glypican-2 and -5 are below the
      level of detection by Northern blotting in both normal and cancer samples.
      Treatment of MDA-MB-231 and MDA-MB-468 breast cancer cells with
      phosphoinositide-specific phospholipase-C abrogated the mitogenic response
      to two heparin-binding growth factors, heparin-binding epidermal growth
      factor-like growth factor and fibroblast growth factor 2. Stable
      transfection of these cells with a glypican-1 antisense construct markedly
      decreased glypican-1 protein levels and the mitogenic response to the same
      heparin-binding growth factors, as well as that to heregulin alpha,
      heregulin beta, and hepatocyte growth factor. Syndecan-1 was also
      expressed at high levels in both breast cancer tissues and breast cancer
      cells when compared with normal breast tissues. There was a good
      correlation between glypican-1 and syndecan-1 expression in the tumors.
      However, clones expressing the glypican-1 antisense construct did not
      exhibit decreased syndecan-1 levels, indicating that loss of
      responsiveness to heparin-binding growth factors in these clones was not
      due to altered syndecan-1 expression. Furthermore, 8 of 10 tumors with
      stage 2 or 3 disease exhibited high levels of glypican-1 by Northern blot
      analysis. In contrast, low levels of glypican-1 mRNA were evident in 1 of
      10 tumors with stage 2 or 3 disease and in 9 of 10 tumors with stage 1
      disease. Taken together, these data suggest that glypican-1 may play a
      pivotal role in the ability of breast cancer cells to exhibit a mitogenic
      response to multiple heparin-binding growth factors and may contribute to
      disease progression in this malignancy.
AD  - Division of Endocrinology, Diabetes and Metabolism, Department of
      Medicine, Biological Chemistry, and Pharmacology, University of
      California, Irvine, California 92697, USA.
FAU - Matsuda, K
AU  - Matsuda K
FAU - Maruyama, H
AU  - Maruyama H
FAU - Guo, F
AU  - Guo F
FAU - Kleeff, J
AU  - Kleeff J
FAU - Itakura, J
AU  - Itakura J
FAU - Matsumoto, Y
AU  - Matsumoto Y
FAU - Lander, A D
AU  - Lander AD
FAU - Korc, M
AU  - Korc M
LA  - eng
ID  - CA-40162/CA/NCI
ID  - NS-26862/NS/NINDS
PT  - Journal Article
CY  - United States
TA  - Cancer Res
JID - 2984705R
RN  - 0 (DNA, Antisense)
RN  - 0 (Growth Substances)
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (syndecan)
RN  - EC 3.1.4.10 (1-phosphatidylinositol phosphodiesterase)
RN  - EC 3.1.4.3 (Phospholipase C)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Blotting, Northern
MH  - Breast Neoplasms/*genetics/metabolism/pathology
MH  - DNA, Antisense/genetics
MH  - Female
MH  - Gene Expression Regulation, Neoplastic
MH  - Growth Substances/*pharmacology
MH  - Heparan Sulfate Proteoglycan/analysis/*genetics
MH  - Human
MH  - Immunohistochemistry
MH  - In Situ Hybridization
MH  - Membrane Glycoproteins/analysis/genetics
MH  - Middle Age
MH  - Phospholipase C/metabolism/pharmacology
MH  - Proteoglycans/analysis/genetics
MH  - RNA, Messenger/genetics/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
MH  - Transfection
MH  - Tumor Cells, Cultured/drug effects/metabolism
EDAT- 2001/07/17 10:00
MHDA- 2001/08/03 10:01
URLF- http://cancerres.aacrjournals.org/cgi/content/full/61/14/5562
URLS- http://cancerres.aacrjournals.org/cgi/content/abstract/61/14/5562
PST - ppublish
SO  - Cancer Res 2001 Jul 15;61(14):5562-9.




UI  - 21345374
PMID- 11452090
DA  - 20010713
DCOM- 20010726
IS  - 0036-8075
VI  - 293
IP  - 5528
DP  - 2001 Jul 13
TI  - Cell biology. Fresh molecule whets appetite.
PG  - 190
FAU - Strauss, E
AU  - Strauss E
LA  - eng
PT  - News
CY  - United States
TA  - Science
JID - 0404511
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, Corticotropin)
RN  - 0 (melanocortin receptor 3)
RN  - 0 (syndecan)
RN  - 0 (syndecan 3)
SB  - IM
MH  - Animal
MH  - Appetite Regulation/*physiology
MH  - Hypothalamus/metabolism
MH  - Membrane Glycoproteins/*physiology
MH  - Mice
MH  - Proteoglycans/*physiology
MH  - Receptors, Corticotropin/metabolism
MH  - Satiation
MH  - Signal Transduction
EDAT- 2001/07/14 10:00
MHDA- 2001/07/28 10:01
AID - 10.1126/science.293.5528.190 [doi]
AID - 293/5528/190 [pii]
URLF- http://www.sciencemag.org/cgi/content/full/293/5528/190
URLS- http://www.sciencemag.org/cgi/content/summary/293/5528/190
PST - ppublish
SO  - Science 2001 Jul 13;293(5528):190.




UI  - 21325992
PMID- 11433525
DA  - 20010702
DCOM- 20010802
LR  - 20011119
IS  - 1045-2257
VI  - 31
IP  - 4
DP  - 2001 Aug
TI  - Amplification of Mycn, Ddx1, Rrm2, and Odc1 in rat uterine endometrial
      carcinomas.
PG  - 345-56
AB  - The BDII rat is genetically predisposed to estrogen-dependent endometrial
      adenocarcinoma and represents a valuable model for this type of tumor.
      Tumors arising in strain crosses involving the BDII rats had previously
      been screened for DNA copy number changes using comparative genome
      hybridization (CGH). It was found that extra copies of the proximal region
      of rat chromosome (RNO) 6 commonly could be detected in these tumors.
      Based on RH-mapping data and comparative mapping with mouse and human,
      seven cancer-related genes were predicted to be situated in RNO6q14-q16.
      Rat PACs were isolated for the N-myc proto-oncogene (Mycn), apolipoprotein
      B (Apob), the DEAD box gene 1 (Ddx1), ornithine decarboxylase 1 (Odc1),
      proopiomelanocortin (Pomc1), ribonucleotide reductase, M2 polypeptide
      (Rrm2), and syndecan 1 (Sdc1). The localization of the genes to the region
      was verified by FISH (fluorescence in situ hybridization) mapping, and the
      detailed order among them was determined by dual-color FISH. By Southern
      blot analysis, it was found that the Mycn locus was highly amplified in
      two out of 10 cell cultures derived from the tumors. In one of them
      (designated RUT30), the amplification level of Mycn was estimated at 140x.
      Two other genes were coamplified (Ddx1 and Rrm2) at much lower levels.
      Similarly, in another culture (designated RUT2), Mycn was amplified more
      than 40x, whereas three of the other genes (Ddx1, Rrm2, and Odc1) were
      coamplified at lower levels. Using FISH on metaphase chromosomes from the
      cell cultures analyzed, the amplified sequences were shown to be located
      in typical HSRs. With competitive RT-PCR, distinct overexpression of Mycn
      and Ddx1 could be demonstrated in both RUT2 and RUT30. In addition, Mycn
      was overexpressed in two other tumors not exhibiting Mycn amplification.
      Taken together, our results suggest that overexpression of Mycn plays an
      important role in the development of endometrial cancer in the BDII rat.
      In humans, Mycn amplification has been reported mainly from tumors of
      neuronal origin. To our knowledge, this is the first report of Mycn
      amplification and overexpression in hormone-dependent tumors.
CI  - Copyright 2001 Wiley-Liss, Inc.
AD  - Department of Cell and Molecular Biology-Genetics, Goteborg University, SE
      405 30 Gothenburg, Sweden.
AU  - Karlsson A
FAU - Helou, K
AU  - Helou K
FAU - Walentinsson, A
AU  - Walentinsson A
FAU - Hedrich, H J
AU  - Hedrich HJ
FAU - Szpirer, C
AU  - Szpirer C
FAU - Levan, G
AU  - Levan G
LA  - eng
SI  - GENBANK/AF222732
SI  - GENBANK/AF222733
PT  - Journal Article
CY  - United States
TA  - Genes Chromosomes Cancer
JID - 9007329
RN  - 0 (Chromatin)
RN  - 0 (Proto-Oncogene Proteins c-myc)
RN  - 0 (RNA, Messenger)
RN  - 0 (RNA, Neoplasm)
RN  - EC 1.17.4.- (ribonucleotide reductase M2)
RN  - EC 1.17.4.1 (Ribonucleoside Diphosphate Reductase)
RN  - EC 2.7.7.- (DDX1 protein)
RN  - EC 2.7.7.- (RNA Helicases)
RN  - EC 4.1.1.17 (Ornithine Decarboxylase)
SB  - IM
MH  - Animal
MH  - Chromatin/genetics
MH  - Chromosome Mapping
MH  - Endometrial Neoplasms/*enzymology/*genetics
MH  - Female
MH  - *Gene Amplification/methods
MH  - Genes, myc/*genetics
MH  - In Situ Hybridization, Fluorescence
MH  - Molecular Sequence Data
MH  - Ornithine Decarboxylase/biosynthesis/chemistry/genetics
MH  - Proto-Oncogene Proteins c-myc/chemistry/genetics/isolation & purification
MH  - RNA Helicases/chemistry/genetics/isolation & purification
MH  - RNA, Messenger/biosynthesis
MH  - RNA, Neoplasm/biosynthesis
MH  - Rats
MH  - Rats, Inbred BN
MH  - Rats, Inbred Strains
MH  - Rats, Sprague-Dawley
MH  - Ribonucleoside Diphosphate Reductase/biosynthesis/genetics
MH  - Support, Non-U.S. Gov't
MH  - Uterine Neoplasms/*enzymology/*genetics
EDAT- 2001/07/04 10:00
MHDA- 2001/08/03 10:01
PST - ppublish
SO  - Genes Chromosomes Cancer 2001 Aug;31(4):345-56.




UI  - 21324481
PMID- 11431422
DA  - 20010629
DCOM- 20011101
LR  - 20011102
IS  - 0953-8178
VI  - 13
IP  - 7
DP  - 2001 Jul
TI  - Tetracyclines inhibit activated B cell function.
PG  - 921-31
AB  - Tetracyclines have recently been shown to exert a number of pleiotropic
      anti-inflammatory and immunomodulatory activities, independent of their
      antibiotic properties. These include the ability to inhibit
      metalloproteinases (MP), a class of enzymes involved in crucial cellular
      functions such as the shedding of soluble mediators and their receptors
      from the cell surface, as well as interaction with, and remodeling of, the
      extracellular matrix. Here we report that doxycycline at therapeutic
      concentrations (1--5 microg/ml) significantly suppresses Ig secretion and
      class switching by in vitro activated murine B cells. Suppression of Ig
      secretion correlates with a decrease in levels of mRNA for the terminal B
      cell differentiation-associated genes Blimp-1 and mad-4, as well as to a
      reduction in expression of the plasma cell markers Syndecan-1 and J chain.
      Inhibition of class switching occurs at the recombination stage and is
      also induced by other MP inhibitors, including tetracycline analogs
      lacking antibiotic activity and the chemically unrelated hydroxamate
      KB8301. These novel, direct effects of MP inhibitors on B lymphocytes
      suggest an intrinsic role for MP in B cell activation and likely explain
      some of the observed in vivo immunomodulatory properties of tetracyclines.
      Moreover, these findings have significant implications for tetracycline
      therapy in Ig-mediated autoimmune or allergic diseases and raise questions
      about the use of doxycycline-inducible transgenic systems for the study of
      B cell function.
AD  - Department of Medicine, University of Rochester School of Medicine and
      Dentistry, Rochester, NY 14642, USA.
FAU - Kuzin, I I
AU  - Kuzin II
FAU - Snyder, J E
AU  - Snyder JE
FAU - Ugine, G D
AU  - Ugine GD
FAU - Wu, D
AU  - Wu D
FAU - Lee, S
AU  - Lee S
FAU - Bushnell, T Jr
AU  - Bushnell T Jr
FAU - Insel, R A
AU  - Insel RA
FAU - Young, F M
AU  - Young FM
FAU - Bottaro, A
AU  - Bottaro A
LA  - eng
ID  - AI07169/AI/NIAID
ID  - AI07285/AI/NIAID
ID  - R29CA73696/CA/NCI
ID  - RO1AI37123/AI/NIAID
ID  - RO1AI45012/AI/NIAID
ID  - RO1HD36293/HD/NICHD
PT  - Journal Article
CY  - England
TA  - Int Immunol
JID - 8916182
RN  - 0 (Antibiotics, Tetracycline)
RN  - 0 (Biological Markers)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Immunoglobulin Isotypes)
RN  - 564-25-0 (Doxycycline)
SB  - IM
MH  - Animal
MH  - Antibiotics, Tetracycline/*pharmacology
MH  - B-Lymphocytes/*drug effects/immunology
MH  - Biological Markers
MH  - Cell Differentiation
MH  - Cell Division/drug effects
MH  - Cells, Cultured
MH  - Doxycycline/*pharmacology
MH  - Gene Rearrangement, B-Lymphocyte/drug effects
MH  - Immunoglobulin Class Switching
MH  - Immunoglobulin G/biosynthesis
MH  - Immunoglobulin Isotypes
MH  - Lymphocyte Transformation/drug effects/immunology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Inbred C57BL
MH  - Spleen/cytology
MH  - Support, U.S. Gov't, P.H.S.
EDAT- 2001/06/30 10:00
MHDA- 2001/11/03 10:01
URLF- http://intimm.oupjournals.org/cgi/content/full/13/7/921
URLS- http://intimm.oupjournals.org/cgi/content/abstract/13/7/921
PST - ppublish
SO  - Int Immunol 2001 Jul;13(7):921-31.




UI  - 21324357
PMID- 11431373
DA  - 20010629
DCOM- 20010719
LR  - 20011128
IS  - 0008-5472
VI  - 61
IP  - 13
DP  - 2001 Jul 1
TI  - A rare premalignant prostate tumor epithelial cell syndecan-1 forms a
      fibroblast growth factor-binding complex with progression-promoting
      ectopic fibroblast growth factor receptor 1.
PG  - 5295-302
AB  - The abnormal appearance and age-dependent loss of resident fibroblast
      growth factor receptor-2 (FGFR2) and gain of activity of FGFR1 in
      epithelial cells is a hallmark of the slow progression to malignancy in
      some models of prostate cancer. Pericellular matrix heparan sulfate (HS)
      is an integral subunit of the FGFR tyrosine kinase complex that restricts
      activity in absence of FGF, facilitates binding of an activating FGF, and
      confers specificity for FGF isoforms. In this report, we isolated and
      purified HS proteoglycan (HSPG) from premalignant prostate tumor
      epithelial cells based on the ability of the HS chains to form a binary
      complex with immunoglobulin module II of the ectopic and
      progression-promoting FGFR1 that was competent to bind FGF. The FGFR1
      affinity-purified product exhibited a specific activity of over 600 times
      that of crude cellular HSPG enriched from cell lysates by ion exchange
      chromatography. The purified preparation exhibited a single NH(2)-terminal
      sequence with 11 of 13 residues identical to syndecan-1. The activity of
      purified recombinant glutathione S-transferase-tagged syndecan-1 expressed
      in premalignant epithelial cells confirmed that syndecan-1 bears HS chains
      that exhibit the rare motif that forms the FGF-binding complex with
      ectopic FGFR1. These results are the first to identify by affinity
      purification a specific HSPG core protein, the HS chains of which act as
      an integral subunit of the FGFR complex. The results suggest that
      syndecan-1 provides HS chains in premalignant epithelial cells to both the
      FGFR2- and FGFR1-signaling complexes that are integral to their dual roles
      in progression to malignancy.
AD  - Center for Cancer Biology and Nutrition, Institute of Biosciences and
      Technology, Texas A&M University System Health Science Center, Houston,
      Texas 77030-3303, USA.
FAU - Wu, X
AU  - Wu X
FAU - Kan, M
AU  - Kan M
FAU - Wang, F
AU  - Wang F
FAU - Jin, C
AU  - Jin C
FAU - Yu, C
AU  - Yu C
FAU - McKeehan, W L
AU  - McKeehan WL
LA  - eng
ID  - CA59971/CA/NCI
ID  - DK35310/DK/NIDDK
ID  - DK40739/DK/NIDDK
PT  - Journal Article
CY  - United States
TA  - Cancer Res
JID - 2984705R
RN  - 0 (DNA, Complementary)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (Receptors, Fibroblast Growth Factor)
RN  - 0 (Recombinant Proteins)
RN  - 0 (fibroblast growth factor receptor 1)
RN  - 0 (heparin proteoglycan)
RN  - 0 (syndecan)
RN  - 62031-54-3 (Fibroblast Growth Factors)
RN  - 9005-49-6 (Heparin)
RN  - EC 2.7.1.- (fibroblast growth factor receptor 2)
RN  - EC 2.7.11.- (Receptor Protein-Tyrosine Kinases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animal
MH  - Base Sequence
MH  - Chromatography, Affinity
MH  - DNA, Complementary/genetics
MH  - Fibroblast Growth Factors/metabolism
MH  - Heparin/analogs & derivatives/genetics/isolation & purification/metabolism
MH  - Male
MH  - Membrane Glycoproteins/genetics/isolation & purification/*metabolism
MH  - Molecular Sequence Data
MH  - Precancerous Conditions/chemistry/metabolism
MH  - Prostatic Neoplasms/chemistry/metabolism
MH  - Proteoglycans/genetics/isolation & purification/*metabolism
MH  - RNA, Messenger/genetics/metabolism
MH  - Rats
MH  - Receptor Protein-Tyrosine Kinases/*metabolism
MH  - Receptors, Fibroblast Growth Factor/*metabolism
MH  - Recombinant Proteins/metabolism
MH  - Support, U.S. Gov't, P.H.S.
EDAT- 2001/06/30 10:00
MHDA- 2001/07/20 10:01
URLF- http://cancerres.aacrjournals.org/cgi/content/full/61/13/5295
URLS- http://cancerres.aacrjournals.org/cgi/content/abstract/61/13/5295
PST - ppublish
SO  - Cancer Res 2001 Jul 1;61(13):5295-302.




UI  - 21313638
PMID- 11420610
DA  - 20010622
DCOM- 20010830
IS  - 0938-8990
VI  - 12
IP  - 7
DP  - 2001 Jul
TI  - Fine mapping of Ath6, a quantitative trait locus for atherosclerosis in
      mice.
PG  - 495-500
AB  - Ath6 is a novel quantitative trait locus associated with differences in
      susceptibility to atherosclerosis between C57BL/6J (B6) and C57BLKS/J
      (BKS) inbred mouse strains. Combining data from an intercross and a
      backcross (1593 meioses) between mice from B6 and BKS strains and from The
      Jackson Laboratory interspecific backcross panels, (C57BL/6J x Mus
      spretus) F1 x C57BL/6J and (C57BL/6J x SPRET/Ei) F1 x SPRET/Ei, we
      constructed a consensus genetic map and narrowed Ath6 to a 1.07 +/- 0.26
      cM interval between the anonymous DNA marker D12Pgn4 and the gene Nmyc1.
      This region is near the proximal end of murine Chromosome (Chr) 12, which
      is homologous to the human chromosomal region 2p24-p25. Marker order in
      the Ath6 region was concordant among the two crosses and The Jackson
      Laboratory interspecific backcross panels. This high resolution map rules
      out candidate genes encoding apolipoprotein B, syndecan 1, and Adam17. The
      two Ath6 crosses have a combined potential resolution of 0.06 cM.
AD  - The Jackson Laboratory, 600 Main Street, Bar Harbor, ME 04609, USA.
FAU - Purcell, M K
AU  - Purcell MK
FAU - Mu, J L
AU  - Mu JL
FAU - Higgins, D C
AU  - Higgins DC
FAU - Elango, R
AU  - Elango R
FAU - Whitmore, H
AU  - Whitmore H
FAU - Harris, S
AU  - Harris S
FAU - Paigen, B
AU  - Paigen B
LA  - eng
ID  - HL32087/HL/NHLBI
PT  - Journal Article
CY  - United States
TA  - Mamm Genome
JID - 9100916
RN  - 0 (DNA Primers)
RN  - 0 (Genetic Markers)
RN  - 9007-49-2 (DNA)
SB  - IM
MH  - Alleles
MH  - Animal
MH  - Aorta/pathology
MH  - Arteriosclerosis/*genetics/pathology
MH  - *Chromosome Mapping
MH  - *Crosses, Genetic
MH  - Crossing Over (Genetics)
MH  - DNA/genetics
MH  - DNA Primers/chemistry
MH  - Diet, Atherogenic
MH  - Female
MH  - Genetic Markers
MH  - Genetic Predisposition to Disease/*genetics
MH  - Linkage (Genetics)
MH  - Male
MH  - Mice
MH  - Mice, Inbred C57BL/*genetics
MH  - Polymerase Chain Reaction
MH  - *Quantitative Trait
MH  - Species Specificity
MH  - Support, U.S. Gov't, P.H.S.
EDAT- 2001/06/23 10:00
MHDA- 2001/08/31 10:01
PHST- 2000/Sep/12 [received]
PHST- 2001/Feb/22 [accepted]
PST - ppublish
SO  - Mamm Genome 2001 Jul;12(7):495-500.




UI  - 21286365
PMID- 11390420
DA  - 20010606
DCOM- 20010628
LR  - 20011102
IS  - 0021-9738
VI  - 107
IP  - 11
DP  - 2001 Jun
TI  - LDL receptor-related protein mediates cell-surface clustering and hepatic
      sequestration of chylomicron remnants in LDLR-deficient mice.
PG  - 1387-94
AB  - It has been proposed that in the liver, chylomicron remnants (lipoproteins
      carrying dietary lipid) may be sequestered before being internalized by
      hepatocytes. To study this, chylomicron remnants labeled with a
      fluorescent dye were perfused into isolated livers of LDL
      receptor-deficient (LDLR-deficient) mice (Ldlr(-/-)) and examined by
      confocal microscopy. In contrast to livers from normal mice, there was
      clustering of the chylomicron remnants on the cell surface in the space of
      DISSE: These remnant clusters colocalized with clusters of LDLR-related
      protein (LRP) and could be eliminated by low concentrations of
      receptor-associated protein, an inhibitor of LRP. When competed with
      ligands of heparan sulfate proteoglycans (HSPGs), the remnant clusters
      still appeared but were fewer in number, although syndecans (membrane
      HSPGs) colocalized with the remnant clusters. This suggests that the
      clustering of remnants is not dependent on syndecans but that the
      syndecans may modify the binding of remnants. These results establish that
      sequestration is a novel process, the clustering of remnants in the space
      of DISSE: The clustering involves remnants binding to the LRP, and this
      may be stabilized by binding with syndecans, eventually followed by
      endocytosis.
AD  - Department of Medicine, Division of Gastroenterology, Stanford University
      School of Medicine, Stanford, California, USA.
FAU - Yu, K C
AU  - Yu KC
FAU - Chen, W
AU  - Chen W
FAU - Cooper, A D
AU  - Cooper AD
LA  - eng
ID  - DK38318/DK/NIDDK
ID  - DK38707/DK/NIDDK
PT  - Journal Article
CY  - United States
TA  - J Clin Invest
JID - 7802877
RN  - 0 (Asialoglycoproteins)
RN  - 0 (Chylomicrons)
RN  - 0 (Fluorescent Dyes)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, LDL)
RN  - 0 (alpha-Fetoproteins)
RN  - 0 (asialofetuin)
RN  - 0 (chylomicron remnant)
RN  - 0 (syndecan)
RN  - 103107-01-3 (Fibroblast Growth Factor 2)
RN  - 9005-49-6 (Heparin)
SB  - AIM
SB  - IM
MH  - Animal
MH  - Asialoglycoproteins/metabolism
MH  - Chylomicrons/*metabolism
MH  - Endocytosis/drug effects/physiology
MH  - Fibroblast Growth Factor 2/metabolism
MH  - Fluorescent Dyes/metabolism
MH  - Heparin/pharmacology
MH  - Hepatocytes/*metabolism
MH  - Liver/anatomy & histology/*metabolism
MH  - Membrane Glycoproteins/metabolism
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Microscopy, Confocal
MH  - Proteoglycans/metabolism
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Receptors, LDL/*metabolism
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
MH  - alpha-Fetoproteins/metabolism
EDAT- 2001/06/08 10:00
MHDA- 2001/06/29 10:01
URLF- http://www.jci.org/cgi/content/full/107/11/1387
URLS- http://www.jci.org/cgi/content/abstract/107/11/1387
PST - ppublish
SO  - J Clin Invest 2001 Jun;107(11):1387-94.




UI  - 21286789
PMID- 11390011
DA  - 20010606
DCOM- 20010712
IS  - 0169-5002
VI  - 32
IP  - 3
DP  - 2001 Jun
TI  - High syndecan-1 expression is associated with favourable outcome in
      squamous cell lung carcinoma treated with radical surgery.
PG  - 297-305
AB  - Expression of syndecan-1 is down-regulated in many cellular transformation
      models. We studied the clinical significance of syndecan-1 expression in
      116 squamous cell lung carcinomas treated with radical surgery.
      Paraffin-embedded tissue samples were immunostained with two antibodies
      against human syndecan-1 (B-B4 and 104-9). Syndecan-1 expression was
      higher in well differentiated cancers than in moderately or poorly
      differentiated cancers with either antibody (P=0.001 for B-B4, and
      P<0.0001 for 104-9), but no significant association was found with the
      primary tumour size (T-stage) or the clinical stage. When the median
      expression (10% of cancer cells positive in B-B4 staining) was used as the
      cut-off value, cancers with high expression were associated with more
      favourable survival than those with low expression (the 2-year survival
      rate corrected for intercurrent deaths 84% vs 61%, P=0.026). However,
      syndecan-1 expression was not an independent prognostic factor in a
      multivariate survival analysis. We conclude that syndecan-1 expression
      decreases in parallel with histological dedifferentiation in squamous cell
      carcinoma of the lung, and that low syndecan-1 expression is associated
      with unfavourable outcome.
AD  - Department of Oncology, Helsinki University Central Hospital, FIN-00029
      HUS, Helsinki, Finland.
FAU - Anttonen, A
AU  - Anttonen A
FAU - Heikkila, P
AU  - Heikkila P
FAU - Kajanti, M
AU  - Kajanti M
FAU - Jalkanen, M
AU  - Jalkanen M
FAU - Joensuu, H
AU  - Joensuu H
LA  - eng
PT  - Journal Article
CY  - Ireland
TA  - Lung Cancer
JID - 8800805
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Tumor Markers, Biological)
RN  - 0 (syndecan)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Carcinoma, Squamous Cell/pathology/*surgery
MH  - Cell Differentiation
MH  - Cell Transformation, Neoplastic
MH  - Female
MH  - *Gene Expression Regulation, Neoplastic
MH  - Human
MH  - Lung Neoplasms/pathology/*surgery
MH  - Male
MH  - Membrane Glycoproteins/*biosynthesis
MH  - Middle Age
MH  - Prognosis
MH  - Proteoglycans/*biosynthesis
MH  - Support, Non-U.S. Gov't
MH  - Survival Analysis
MH  - Tumor Markers, Biological/*analysis
EDAT- 2001/06/08 10:00
MHDA- 2001/07/13 10:01
AID - S0169500200002300 [pii]
PST - ppublish
SO  - Lung Cancer 2001 Jun;32(3):297-305.




UI  - 21369939
PMID- 11384972
DA  - 20010730
DCOM- 20010913
IS  - 0021-9258
VI  - 276
IP  - 31
DP  - 2001 Aug 3
TI  - Structural characterization of heparan sulfate and chondroitin sulfate of
      syndecan-1 purified from normal murine mammary gland epithelial cells.
      Common phosphorylation of xylose and differential sulfation of galactose
      in the protein linkage region tetrasaccharide sequence.
PG  - 29134-40
AB  - Syndecan-1, present on the surfaces of normal murine mammary gland
      epithelial cells, is a transmembrane hybrid proteoglycan, which bears
      glycosaminoglycan (GAG) side chains of heparan sulfate (HS) and
      chondroitin sulfate (CS). Purified syndecan-1 ectodomains were analyzed
      for disaccharide composition and the GAG-protein linkage region after
      digestion with bacterial lyases. The HS chains contained predominantly a
      nonsulfated unit with smaller proportions of two monosulfated, two
      disulfated, and a trisulfated unit, whereas CS chains were demonstrated
      for the first time to bear GlcUA-GalNAc(4-O-sulfate) as a major component
      as well as GlcUA-GalNAc, GlcUA-GalNAc(6-O-sulfate), and an E disaccharide
      unit GlcUA-GalNAc(4,6-O-disulfate) as minor yet appreciable components.
      Two kinds of linkage region tetrasaccharides, GlcUA-Gal-Gal-Xyl and
      GlcUA-Gal-Gal-Xyl(2-O-phosphate), were found for the HS chains in a molar
      ratio of 55:45. In marked contrast, an additional sulfated
      tetrasaccharide, GlcUA-Gal(4-O-sulfate)-Gal-Xyl, was demonstrated only for
      the CS chains, and the unmodified phosphorylated and sulfated components
      were present at a molar ratio of 55:26:19. The present study thus provided
      conclusive evidence for the hypothesis that 4-O-sulfation of Gal is
      peculiar to CS chains in contrast to the phosphorylation of Xyl, which is
      common to both HS and CS chains. These modifications may be required for
      biosynthetic maturation of the linkage region tetrasaccharide sequence,
      which is a prerequisite for creating the repeating disaccharide region of
      GAG chains and/or biosynthetic selective chain assembly of CS and HS
      chains.
AD  - Department of Biochemistry, Kobe Pharmaceutical University,
      Higashinada-ku, Kobe 658-8558, Japan.
FAU - Ueno, M
AU  - Ueno M
FAU - Yamada, S
AU  - Yamada S
FAU - Zako, M
AU  - Zako M
FAU - Bernfield, M
AU  - Bernfield M
FAU - Sugahara, K
AU  - Sugahara K
LA  - eng
ID  - CA28734/CA/NCI
ID  - HD06763/HD/NICHD
PT  - Journal Article
CY  - United States
TA  - J Biol Chem
JID - 2985121R
RN  - 0 (Disaccharides)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Oligosaccharides)
RN  - 0 (Proteoglycans)
RN  - 0 (Sulfates)
RN  - 0 (Xylose)
RN  - 0 (syndecan)
RN  - 26566-61-0 (Galactose)
RN  - 9007-28-7 (Chondroitin Sulfates)
RN  - 9050-30-0 (Heparitin Sulfate)
RN  - EC 3.1.6. (Sulfatases)
RN  - EC 3.2.1.31 (Glucuronidase)
SB  - IM
MH  - Animal
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - Cell Membrane/chemistry
MH  - Chondroitin Sulfates/*chemistry/isolation & purification
MH  - Disaccharides/chemistry
MH  - Epithelial Cells/*chemistry
MH  - Female
MH  - Galactose/analysis
MH  - Glucuronidase
MH  - Heparitin Sulfate/*chemistry/isolation & purification
MH  - Mammae/*cytology
MH  - Membrane Glycoproteins/*chemistry/isolation & purification
MH  - Mice
MH  - Molecular Sequence Data
MH  - Oligosaccharides/*chemistry
MH  - Phosphorylation
MH  - Proteoglycans/*chemistry/isolation & purification
MH  - Sulfatases
MH  - Sulfates
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
MH  - Xylose/analysis
EDAT- 2001/06/01 10:00
MHDA- 2001/09/14 10:01
PHST- 2001/May/30 [aheadofprint]
AID - 10.1074/jbc.M102089200 [doi]
AID - M102089200 [pii]
URLF- http://www.jbc.org/cgi/content/full/276/31/29134
URLS- http://www.jbc.org/cgi/content/abstract/276/31/29134
PST - ppublish
SO  - J Biol Chem 2001 Aug 3;276(31):29134-40.




UI  - 21275816
PMID- 11380810
DA  - 20010530
DCOM- 20010809
LR  - 20011102
IS  - 0085-2538
VI  - 59
IP  - 6
DP  - 2001 Jun
TI  - Cell surface heparan sulfate proteoglycans control the response of renal
      interstitial fibroblasts to fibroblast growth factor-2.
PG  - 2084-94
AB  - BACKGROUND: While the progression of renal disease to end stage is
      strongly correlated with tubulointerstitial changes, the control of the
      fibrotic process within the interstitium is poorly understood. Basic
      fibroblast growth factor (FGF-2) has been implicated as a major growth
      factor involved in fibroblast activation and extracellular matrix
      synthesis. Furthermore, in many cells, the activity of FGF-2 is controlled
      by a low-affinity but high-capacity interaction with heparan sulfate (HS)
      proteoglycans (PGs), such as members of the syndecan family. These
      molecules are likely to be central to the control of interstitial
      fibrosis, but as yet, there has been no characterization of their
      synthesis by interstitial cells. METHODS: The expression of HSPG on the
      surface of NRK 49F fibroblasts was demonstrated by immunohistochemistry
      and by metabolic labeling with [(35)S]-sulfate. HSs were characterized by
      specific enzymatic digestion, size exclusion chromatography, and anion
      exchange chromatography. The mRNA for syndecan 1 through syndecan 4 in the
      fibroblasts was detected by semiquantitative reverse
      transcription-polymerase chain reaction. Fibroblast proliferation was
      measured by the MTT assay. RESULTS: Immunohistochemistry and
      [(35)S]-sulfate-labeling demonstrated that renal fibroblasts expressed
      HSPGs on their surface. Furthermore, enzymatic removal of these HS (but
      not chondroitin sulfate) glycosaminoglycan (GAG) chains, or inhibition of
      GAG sulfation, abolished the proliferative response of both NRK cells and
      primary human cortical fibroblasts to FGF-2 but not to platelet-derived
      growth factor. The addition of conditioned medium, containing HS-GAG
      fragments, restored the proliferative response to FGF-2, confirming the
      specificity of the interaction. Finally, the mRNA for all four syndecans
      was detected in the fibroblasts, and that for syndecan 1 in particular was
      up-regulated by FGF-2. CONCLUSIONS: The present study demonstrates that
      the expression of cell surface HSPG was essential for the proliferation of
      renal fibroblasts in response to FGF-2, and therefore may play a major
      role in the development and persistence of a proliferating phenotype
      during interstitial nephritis.
AD  - Institute of Nephrology, University of Wales College of Medicine, Cardiff,
      Wales, United Kingdom.
FAU - Clayton, A
AU  - Clayton A
FAU - Thomas, J
AU  - Thomas J
FAU - Thomas, G J
AU  - Thomas GJ
FAU - Davies, M
AU  - Davies M
FAU - Steadman, R
AU  - Steadman R
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Kidney Int
JID - 0323470
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (Sulfur Radioisotopes)
RN  - 0 (syndecan)
RN  - 0 (syndecan 3)
RN  - 0 (syndecan-4)
RN  - 103107-01-3 (Fibroblast Growth Factor 2)
RN  - 149769-25-5 (fibroglycan)
SB  - IM
MH  - Animal
MH  - Cell Division/drug effects/physiology
MH  - Cells, Cultured
MH  - Extracellular Matrix/metabolism
MH  - Fibroblast Growth Factor 2/metabolism/*pharmacology
MH  - Fibroblasts/drug effects/metabolism
MH  - Gene Expression/physiology
MH  - Heparan Sulfate Proteoglycan/*genetics/*metabolism
MH  - Human
MH  - Kidney/*cytology
MH  - Membrane Glycoproteins/genetics/metabolism
MH  - Membrane Proteins/genetics/metabolism
MH  - Nephritis, Interstitial/*metabolism
MH  - Proteoglycans/genetics/metabolism
MH  - RNA, Messenger/analysis
MH  - Sulfur Radioisotopes/diagnostic use
MH  - Support, Non-U.S. Gov't
EDAT- 2001/05/31 10:00
MHDA- 2001/08/10 10:01
AID - kid723 [pii]
PST - ppublish
SO  - Kidney Int 2001 Jun;59(6):2084-94.




UI  - 21267033
PMID- 11356864
DA  - 20010524
DCOM- 20010621
LR  - 20011102
IS  - 1529-2401
VI  - 21
IP  - 11
DP  - 2001 Jun 1
TI  - Bipartite interaction between neurofibromatosis type I protein
      (neurofibromin) and syndecan transmembrane heparan sulfate proteoglycans.
PG  - 3764-70
AB  - The neurofibromatosis type 1 (NF1) gene encodes a large tumor suppressor
      protein (neurofibromin). Although it is known to possess Ras
      GTPase-activating protein (GAP) activity, the cellular role of
      neurofibromin remains unclear. Here we used yeast two-hybrid screening to
      identify neurofibromin-interacting proteins. Syndecan-2, a transmembrane
      heparan sulfate proteoglycan (HSPG), was isolated as a binding partner for
      two distinct regions of the neurofibromin protein. We subsequently found
      that neurofibromin can bind all four mammalian syndecans. NF1 interaction
      requires the transmembrane domain and a membrane-proximal region of the
      cytoplasmic tail of syndecan, but not the C terminus of syndecan known to
      bind to CASK, a membrane-associated guanylate kinase (MAGUK).
      Neurofibromin, syndecans, and CASK have overlapping subcellular
      distributions in axons and synapses of neurons, as shown by biochemical
      fractionation and immunostaining. Moreover, neurofibromin exists in a
      complex with syndecan and CASK in vivo, as evidenced by their
      coimmunoprecipitation from rat brain. Our findings suggest that
      interaction with different members of the syndecan family may be a
      mechanism for localizing neurofibromin to specialized domains of the
      plasma membrane.
AD  - Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan, 115,
      Republic of China. yph@gate.sinica.edu.tw
FAU - Hsueh, Y P
AU  - Hsueh YP
FAU - Roberts, A M
AU  - Roberts AM
FAU - Volta, M
AU  - Volta M
FAU - Sheng, M
AU  - Sheng M
FAU - Roberts, R G
AU  - Roberts RG
LA  - eng
PT  - Journal Article
CY  - United States
TA  - J Neurosci
JID - 8102140
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Macromolecular Systems)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Neurofibromin 1)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 0 (syndecan 3)
RN  - 149769-25-5 (fibroglycan)
RN  - EC 2.7.4.- (CASK protein)
RN  - EC 2.7.4.4 (Nucleoside-Phosphate Kinase)
SB  - IM
MH  - Animal
MH  - Brain/metabolism
MH  - Brain Chemistry
MH  - Heparan Sulfate Proteoglycan/*metabolism
MH  - Human
MH  - Macromolecular Systems
MH  - Membrane Glycoproteins/genetics/*metabolism
MH  - Nerve Tissue Proteins/genetics/*metabolism
MH  - Neurofibromatosis 1/genetics
MH  - Neurofibromin 1
MH  - Nucleoside-Phosphate Kinase/metabolism
MH  - Precipitin Tests
MH  - Protein Binding/physiology
MH  - Protein Structure, Tertiary/physiology
MH  - Proteoglycans/genetics/*metabolism
MH  - Rats
MH  - Saccharomyces/genetics
MH  - Subcellular Fractions/chemistry/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Two-Hybrid System Techniques
EDAT- 2001/05/23 10:00
MHDA- 2001/06/22 10:01
AID - 21/11/3764 [pii]
URLF- http://www.jneurosci.org/cgi/content/full/21/11/3764
URLS- http://www.jneurosci.org/cgi/content/abstract/21/11/3764
PST - ppublish
SO  - J Neurosci 2001 Jun 1;21(11):3764-70.




UI  - 21303666
PMID- 11304538
DA  - 20010618
DCOM- 20010719
IS  - 0021-9258
VI  - 276
IP  - 25
DP  - 2001 Jun 22
TI  - Cell type-specific differences in glycosaminoglycans modulate the
      biological activity of a heparin-binding peptide (RKRLQVQLSIRT) from the G
      domain of the laminin alpha1 chain.
PG  - 22077-85
AB  - AG73 (RKRLQVQLSIRT), a peptide from the G domain of the laminin alpha1
      chain, has diverse biological activities with different cell types. The
      heparan sulfate side chains of syndecan-1 on human salivary gland cells
      were previously identified as the cell surface ligand for AG73. We used
      homologous peptides from the other laminin alpha-chains (A2G73-A5G73) to
      determine whether the bioactivity of the AG73 sequence is conserved. Human
      salivary gland cells and a mouse melanoma cell line (B16F10) both bind to
      the peptides, but cell attachment was inhibited by glycosaminoglycans,
      modified heparin, and sized heparin fragments in a cell type-specific
      manner. In other assays, AG73, but not the homologous peptides, inhibited
      branching morphogenesis of salivary glands and B16F10 network formation on
      Matrigel. We identified residues critical for AG73 bioactivity using
      peptides with amino acid substitutions and truncations. Fewer residues
      were critical for inhibiting branching morphogenesis (XKXLXVXXXIRT) than
      those required to inhibit B16F10 network formation on Matrigel (N-terminal
      XXRLQVQLSIRT). In addition, surface plasmon resonance analysis identified
      the C-terminal IRT of the sequence to be important for heparin binding.
      Structure-based sequence alignment predicts AG73 in a beta-sheet with the
      N-terminal K (Lys(2)) and the C-terminal R (Arg(10)) on the surface of the
      G domain. In conclusion, we have determined that differences in cell
      surface glycosaminoglycans and differences in the amino acids in AG73
      recognized by cells modulate the biological activity of the peptide and
      provide a mechanism to explain its cell-specific activities.
AD  - Craniofacial Developmental Biology and Regeneration Branch, NIDCR,
      National Institutes of Health, Bethesda, Maryland 20892-4370, USA.
      mhoffman@mail.nih.gov
FAU - Hoffman, M P
AU  - Hoffman MP
FAU - Engbring, J A
AU  - Engbring JA
FAU - Nielsen, P K
AU  - Nielsen PK
FAU - Vargas, J
AU  - Vargas J
FAU - Steinberg, Z
AU  - Steinberg Z
FAU - Karmand, A J
AU  - Karmand AJ
FAU - Nomizu, M
AU  - Nomizu M
FAU - Yamada, Y
AU  - Yamada Y
FAU - Kleinman, H K
AU  - Kleinman HK
LA  - eng
PT  - Journal Article
CY  - United States
TA  - J Biol Chem
JID - 2985121R
RN  - 0 (AG 73)
RN  - 0 (Glycosaminoglycans)
RN  - 0 (Laminin)
RN  - 0 (Peptide Fragments)
RN  - 58-85-5 (Biotin)
RN  - 9005-49-6 (Heparin)
SB  - IM
MH  - Amino Acid Sequence
MH  - Amino Acid Substitution
MH  - Animal
MH  - Biotin/metabolism
MH  - Cell Adhesion
MH  - Crystallography, X-Ray
MH  - Glycosaminoglycans/*metabolism
MH  - Heparin/metabolism
MH  - Laminin/*metabolism
MH  - Mice
MH  - Mice, Inbred ICR
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Peptide Fragments/*metabolism
MH  - Protein Conformation
MH  - Surface Plasmon Resonance
EDAT- 2001/04/17 10:00
MHDA- 2001/07/20 10:01
PHST- 2001/Apr/13 [aheadofprint]
AID - 10.1074/jbc.M100774200 [doi]
AID - M100774200 [pii]
URLF- http://www.jbc.org/cgi/content/full/276/25/22077
URLS- http://www.jbc.org/cgi/content/abstract/276/25/22077
PST - ppublish
SO  - J Biol Chem 2001 Jun 22;276(25):22077-85.




