UI  - 21441837
PMID- 11557783
DA  - 20010914
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  - University of Arkansas for Medical SciencesLittle Rock, Arkansas.
AU  - Bayer-Garner IB
AU  - Korourian S
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Mod Pathol
JC  - PTH
JID - 8806605
SB  - IM
EDAT- 2001/09/15 10:00
MHDA- 2001/09/15 10:00
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  - 21421121
PMID- 11529866
DA  - 20010831
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.
AU  - Holen I
AU  - Drury NL
AU  - Hargreaves PG
AU  - Croucher PI
LA  - eng
PT  - Journal Article
CY  - England
TA  - Br J Haematol
JC  - AXC
JID - 0372544
SB  - IM
EDAT- 2001/09/01 10:00
MHDA- 2001/09/01 10:00
AID - bjh2963 [pii]
PST - ppublish
SO  - Br J Haematol 2001 Aug;114(2):414-21.




UI  - 21418177
PMID- 11527150
DA  - 20010830
IS  - 0730-2312
VI  - 82
IP  - 2
DP  - 2001
TI  - Cloning and characterization of human syndecan-3.
PG  - 246-59
AB  - Syndecans are cell-surface heparan sulfate proteoglycans, which perform a
      variety of functions in the cell. Most important, they are co-receptors
      for growth factors and mediate cell-cell and cell-matrix interactions.
      Four syndecans (syndecan 1-4) have been described in different species.
      The aim of this work was the cloning and characterization of human
      syndecan-3. The human syndecan-3 sequence has high homology to the rat and
      mouse sequences, with the exception of the 5'-region. Syndecan-3 mRNA is
      mostly expressed in the nervous system, the adrenal gland, and the spleen.
      When different cell lines were transiently transfected with full-length
      syndecan-3 cDNA, it was localized to the membrane and induced the
      formation of long filopodia-like structures, microspikes, and
      varicosities. Consequently, the actin cytoskeleton was re-organized, since
      actin staining was mostly found in the cellular extensions and at the cell
      periphery, co-localizing with the syndecan-3 staining. The development of
      the phenotype depended on the presence of sugar chains, as transfected
      glycosaminoglycan-deficient Chinese hamster ovary (CHO) 745 cells did not
      show these structural changes, nor did transfected CHO K1 cells in the
      presence of heparin. The similarity of the cloned DNA sequence with that
      of other mammalian species and the high expression in the nervous system
      led us to the assumption that human syndecan-3 could perform comparable
      functions to those described for syndecan-3 in rat and mouse.
      Additionally, transient transfection experiments suggest a role of human
      syndecan-3 in the organization of cell shape by affecting the actin
      cytoskeleton, possibly by transferring signals from the cell surface in a
      sugar-dependent mechanism.
AD  - Department of Cell Biology, University of Barcelona, Spain.
AU  - Berndt C
AU  - Casaroli-Marano RP
AU  - Vilaro S
AU  - Reina M
LA  - eng
SI  - GENBANK/AF248634
PT  - Journal Article
CY  - United States
TA  - J Cell Biochem
JC  - HNF
JID - 8205768
SB  - IM
EDAT- 2001/08/31 10:00
MHDA- 2001/08/31 10:00
PST - ppublish
SO  - J Cell Biochem 2001;82(2):246-59.




UI  - 21413623
PMID- 11522680
DA  - 20010827
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.
AU  - Olsson U
AU  - Egnell AC
AU  - Lee MR
AU  - Lunden GO
AU  - Lorentzon M
AU  - Salmivirta M
AU  - Bondjers G
AU  - Camejo G
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Diabetes
JC  - E8X
JID - 0372763
SB  - AIM
SB  - IM
EDAT- 2001/08/28 10:00
MHDA- 2001/08/28 10:00
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
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
AU  - Heimann H
AU  - Coupland SE
AU  - Gochman R
AU  - Hellmich M
AU  - Foerster MH
LA  - eng
PT  - Journal Article
CY  - Germany
TA  - Graefes Arch Clin Exp Ophthalmol
JC  - FPR
JID - 8205248
SB  - IM
EDAT- 2001/08/28 10:00
MHDA- 2001/08/28 10:00
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.
AU  - De Vos J
AU  - Couderc G
AU  - Tarte K
AU  - Jourdan M
AU  - Requirand G
AU  - Delteil MC
AU  - Rossi JF
AU  - Mechti N
AU  - Klein B
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Blood
JC  - A8G
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
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
AU  - Reizes O
AU  - Lincecum J
AU  - Wang Z
AU  - Goldberger O
AU  - Huang L
AU  - Kaksonen M
AU  - Ahima R
AU  - Hinkes MT
AU  - Barsh GS
AU  - Rauvala H
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
JC  - CQ4
JID - 0413066
RN  - 0 (Blood Glucose)
RN  - 0 (Fibroblast Growth Factor, Basic)
RN  - 0 (Leptin)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, Fibroblast Growth Factor)
RN  - 0 (fibroblast growth factor-2)
RN  - 0 (syndecan)
RN  - 0 (syndecan 3)
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, Basic/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
AU  - Natkunam Y
AU  - Warnke RA
AU  - Montgomery K
AU  - Falini B
AU  - van De Rijn M
LA  - eng
ID  - CA34233/CA/NCI
PT  - Journal Article
CY  - United States
TA  - Mod Pathol
JC  - PTH
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.
AU  - Matsuda K
AU  - Maruyama H
AU  - Guo F
AU  - Kleeff J
AU  - Itakura J
AU  - Matsumoto Y
AU  - Lander AD
AU  - Korc M
LA  - eng
ID  - CA-40162/CA/NCI
ID  - NS-26862/NS/NINDS
PT  - Journal Article
CY  - United States
TA  - Cancer Res
JC  - CNF
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
AU  - Strauss E
LA  - eng
PT  - News
CY  - United States
TA  - Science
JC  - UJ7
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
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. Copyright
      2001 Wiley-Liss, Inc.
AD  - Department of Cell and Molecular Biology-Genetics, Goteborg University, SE
      405 30 Gothenburg, Sweden.
AU  - Karlsson A
AU  - Helou K
AU  - Walentinsson A
AU  - Hedrich HJ
AU  - Szpirer C
AU  - Levan G
LA  - eng
SI  - GENBANK/AF222732
SI  - GENBANK/AF222733
PT  - Journal Article
CY  - United States
TA  - Genes Chromosomes Cancer
JC  - AYV
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
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 &mgr;g/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  - Departments of Medicine, Microbiology and Immunology, and Pediatrics, and
      the Graduate Program in Microbiology and Immunology, University of
      Rochester School of Medicine and Dentistry, Rochester, NY 14642, USA.
AU  - Kuzin II
AU  - Snyder JE
AU  - Ugine GD
AU  - Wu D
AU  - Lee S
AU  - Bushnell T Jr
AU  - Insel RA
AU  - Young FM
AU  - Bottaro A
LA  - eng
PT  - Journal Article
CY  - England
TA  - Int Immunol
JC  - AY5
JID - 8916182
SB  - IM
EDAT- 2001/06/30 10:00
MHDA- 2001/06/30 10:00
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
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.
AU  - Wu X
AU  - Kan M
AU  - Wang F
AU  - Jin C
AU  - Yu C
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
JC  - CNF
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 Factor)
RN  - 9005-49-6 (Heparin)
RN  - EC 2.7.1.- (bek protein)
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 Factor/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.
AU  - Purcell MK
AU  - Mu JL
AU  - Higgins DC
AU  - Elango R
AU  - Whitmore H
AU  - Harris S
AU  - Paigen B
LA  - eng
ID  - HL32087/HL/NHLBI
PT  - Journal Article
CY  - United States
TA  - Mamm Genome
JC  - BES
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
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.
AU  - Yu KC
AU  - Chen W
AU  - Cooper AD
LA  - eng
ID  - DK38318/DK/NIDDK
ID  - DK38707/DK/NIDDK
PT  - Journal Article
CY  - United States
TA  - J Clin Invest
JC  - HS7
JID - 7802877
RN  - 0 (Asialoglycoproteins)
RN  - 0 (Chylomicrons)
RN  - 0 (Fibroblast Growth Factor, Basic)
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  - 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, Basic/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.
AU  - Anttonen A
AU  - Heikkila P
AU  - Kajanti M
AU  - Jalkanen M
AU  - Joensuu H
LA  - eng
PT  - Journal Article
CY  - Ireland
TA  - Lung Cancer
JC  - B3U
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.
AU  - Ueno M
AU  - Yamada S
AU  - Zako M
AU  - Bernfield M
AU  - Sugahara K
LA  - eng
ID  - CA28734/CA/NCI
ID  - HD06763/HD/NICHD
PT  - Journal Article
CY  - United States
TA  - J Biol Chem
JC  - HIV
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
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.
AU  - Clayton A
AU  - Thomas J
AU  - Thomas GJ
AU  - Davies M
AU  - Steadman R
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Kidney Int
JC  - KVB
JID - 0323470
RN  - 0 (Fibroblast Growth Factor, Basic)
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 (fibroblast growth factor-2)
RN  - 0 (syndecan)
RN  - 0 (syndecan 3)
RN  - 0 (syndecan-4)
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, Basic/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  - 21264348
PMID- 11371363
DA  - 20010523
DCOM- 20010719
IS  - 1074-7613
VI  - 14
IP  - 5
DP  - 2001 May
TI  - Marginal zone and B1 B cells unite in the early response against
      T-independent blood-borne particulate antigens.
PG  - 617-29
AB  - The rate of pathogen elimination determines the extent and consequences of
      an infection. In this context, the spleen with its highly specialized
      lymphoid compartments plays a central role in clearing blood-borne
      pathogens. Splenic marginal zone B cells (MZ), by virtue of their
      preactivated state and topographical location, join B1 B cells to generate
      a massive wave of IgM producing plasmablasts in the initial 3 days of a
      primary response to particulate bacterial antigens. Because of the
      intensity and rapidity of this response, combined with the types of
      antibodies produced, splenic MZ and B1 B cells endowed with a "natural
      memory" provide a bridge between the very early innate and the later
      appearing adaptive immune response.
AD  - Division of Developmental and Clinical Immunology, Department of
      Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294,
      USA.
AU  - Martin F
AU  - Oliver AM
AU  - Kearney JF
LA  - eng
ID  - AI07051/AI/NIAID
ID  - AI14782/AI/NIAID
ID  - CA13148/CA/NCI
PT  - Journal Article
CY  - United States
TA  - Immunity
JC  - CCF
JID - 9432918
RN  - 0 (Antigens, Bacterial)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, Complement 3d)
RN  - 0 (syndecan)
SB  - IM
MH  - Animal
MH  - Antigens, Bacterial/*immunology
MH  - B-Lymphocytes/*immunology
MH  - Cells, Cultured
MH  - Immunophenotyping
MH  - Lipopolysaccharides/immunology
MH  - Membrane Glycoproteins/biosynthesis
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Inbred C57BL
MH  - Mice, Transgenic
MH  - Proteoglycans/biosynthesis
MH  - Receptors, Complement 3d/*immunology
MH  - Spleen/cytology/*immunology
MH  - Streptococcus pneumoniae/*immunology
MH  - Support, U.S. Gov't, P.H.S.
MH  - T-Lymphocytes/*immunology
EDAT- 2001/05/24 10:00
MHDA- 2001/07/20 10:01
AID - S1074761301001297 [pii]
PST - ppublish
SO  - Immunity 2001 May;14(5):617-29.




UI  - 21267033
PMID- 11356864
DA  - 20010524
DCOM- 20010621
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
AU  - Hsueh YP
AU  - Roberts AM
AU  - Volta M
AU  - Sheng M
AU  - Roberts RG
LA  - eng
PT  - Journal Article
CY  - United States
TA  - J Neurosci
JC  - JDF
JID - 8102140
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Macromolecular Systems)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (neurofibromatosis type 1 protein)
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  - 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  - 21232702
PMID- 11333985
DA  - 20010503
DCOM- 20010614
IS  - 0028-0836
VI  - 411
IP  - 6833
DP  - 2001 May 3
TI  - Exploitation of syndecan-1 shedding by Pseudomonas aeruginosa enhances
      virulence.
PG  - 98-102
AB  - Cell-surface heparan sulphate proteoglycans (HSPGs) are ubiquitous and
      abundant receptors/co-receptors of extracellular ligands, including many
      microbes. Their role in microbial infections is poorly defined, however,
      because no cell-surface HSPG has been clearly connected to the
      pathogenesis of a particular microbe. We have previously shown that
      Pseudomonas aeruginosa, through its virulence factor LasA, enhances the in
      vitro shedding of syndecan-1-the predominant cell-surface HSPG of
      epithelia. Here we show that shedding of syndecan-1 is also activated by
      P. aeruginosa in vivo, and that the resulting syndecan-1 ectodomains
      enhance bacterial virulence in newborn mice. Newborn mice deficient in
      syndecan-1 resist P. aeruginosa lung infection but become susceptible when
      given purified syndecan-1 ectodomains or heparin, but not when given
      ectodomain core protein, indicating that the ectodomain's heparan sulphate
      chains are the effectors. In wild-type newborn mice, inhibition of
      syndecan-1 shedding or inactivation of the shed ectodomain's heparan
      sulphate chains prevents lung infection. Our findings uncover a
      pathogenetic mechanism in which a host response to tissue
      injury-syndecan-1 shedding-is exploited to enhance microbial virulence
      apparently by modulating host defences.
AD  - Division of Newborn Medicine, Department of Pediatrics, Children's
      Hospital, Harvard Medical School, Boston, MA 02115, USA.
      pwpark@bcm.tmc.edu
AU  - Park PW
AU  - Pier GB
AU  - Hinkes MT
AU  - Bernfield M
LA  - eng
PT  - Journal Article
CY  - England
TA  - Nature
JC  - NSC
JID - 0410462
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 9005-49-6 (Heparin)
RN  - 9050-30-0 (Heparitin Sulfate)
SB  - IM
MH  - Animal
MH  - Animals, Newborn
MH  - Bacterial Adhesion
MH  - Disease Models, Animal
MH  - Heparin/pharmacology
MH  - Heparitin Sulfate/metabolism
MH  - Lung/metabolism/microbiology
MH  - Lung Diseases/metabolism/microbiology
MH  - Membrane Glycoproteins/chemistry/*physiology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Protein Structure, Tertiary
MH  - Proteoglycans/chemistry/*physiology
MH  - Pseudomonas Infections/immunology/microbiology
MH  - Pseudomonas aeruginosa/metabolism/*pathogenicity
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
MH  - Virulence
EDAT- 2001/05/03 10:00
MHDA- 2001/06/15 10:01
AID - 10.1038/35075100 [doi]
AID - 35075100 [pii]
PST - ppublish
SO  - Nature 2001 May 3;411(6833):98-102.




UI  - 21224578
PMID- 11326638
DA  - 20010430
DCOM- 20010524
IS  - 0250-7005
VI  - 20
IP  - 6D
DP  - 2000 Nov-Dec
TI  - A prognostic value of syndecan-1 in gastric cancer.
PG  - 4905-7
AB  - BACKGROUND: Syndecan-1, a cell surface heparan sulphate proteoglycan, has
      a role in cell adhesion, maturation and proliferation. Syndecan-1 has been
      reported to be a promising prognostic marker in various cancer forms.
      MATERIALS AND METHODS: We analysed tumour specimens from 296 gastric
      cancer patients. Syndecan-1 expression was studied by
      immunohistochemistry. RESULTS: Syndecan-1 immunoreactivity was observed in
      234 (79%) patients. The expression of syndecan-1 did not correlate
      significantly with the presence of lymph node metastases, distant
      metastases, peritoneal spreading, penetration depth, tumour size, tumour
      location, Borrmann's classification, Lauren's classification, age or
      gender. Syndecan-1 immunoreactivity correlated significantly with survival
      in the whole patient series (p = 0.0499) and also in the subgroup of
      patients with stage I cancer (p = 0.0417), but not in patients with stage
      II, III or IV disease. In multivariate survival analysis, stage of disease
      and tumour size emerged as the only independent prognostic factors.
      CONCLUSIONS: In conclusion, immunohistochemical expression of syndecan-1
      is a potential prognostic factor in gastric cancer, especially in patients
      with stage I disease.
AD  - Department of Surgery, Helsinki University Central Hospital, Finland.
AU  - Wiksten JP
AU  - Lundin J
AU  - Nordling S
AU  - Kokkola A
AU  - Haglund C
LA  - eng
PT  - Journal Article
CY  - Greece
TA  - Anticancer Res
JC  - 59L
JID - 8102988
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  - Female
MH  - Human
MH  - Male
MH  - Membrane Glycoproteins/*analysis
MH  - Middle Age
MH  - Prognosis
MH  - Proteoglycans/*analysis
MH  - Stomach Neoplasms/*diagnosis/metabolism/mortality
MH  - Support, Non-U.S. Gov't
MH  - Survival Rate
MH  - Tumor Markers, Biological/*analysis
EDAT- 2001/05/01 10:00
MHDA- 2001/05/26 10:01
PST - ppublish
SO  - Anticancer Res 2000 Nov-Dec;20(6D):4905-7.




UI  - 21220712
PMID- 11320057
DA  - 20010426
DCOM- 20010712
IS  - 0959-6658
VI  - 11
IP  - 3
DP  - 2001 Mar
TI  - Anticoagulant heparan sulfate proteoglycans expression in the rat ovary
      peaks in preovulatory granulosa cells.
PG  - 183-94
AB  - Ovarian granulosa cells synthesize anticoagulant heparan sulfate
      proteoglycans (aHSPGs), which bind and activate antithrombin III. To
      determine if aHSPGs could contribute to the control of proteolytic
      activities involved in follicular development and ovulation, we studied
      the pattern of expression of these proteoglycans during the ovarian cycle.
      aHSPGs were localized on cells and tissues by (125)I-labeled antithrombin
      III binding followed by microscopic autoradiography. Localization of
      aHSPGs has shown that cultured granulosa cells, hormonally stimulated by
      gonadotropins to differentiate in vitro, up-regulate their synthesis and
      release of aHSPGS: In vivo, during gonadotropin-stimulated cycle, aHSPGs
      are present on granulosa cells of antral follicles and are strongly
      labeled in preovulatory follicles. These data demonstrate that aHSPG
      expression in the ovarian follicle is hormonally induced to culminate in
      preovulatory follicles. Moreover, we have shown that five heparan sulfate
      core proteins mRNA (perlecan; syndecan-1, -2, and -4; and glypican-1) are
      synthesized by granulosa cells, providing attachment for anticoagulant
      heparan sulfate chains on the cell surface and in the extracellular
      matrix. These core proteins are constantly expressed during the cycle,
      indicating that modulations of aHSPG levels observed in the ovary are
      likely controlled at the level of the biosynthesis of anticoagulant
      heparan sulfate glycosaminoglycan chains. This expression pattern enables
      aHSPGs to focus serine protease inhibitors in the developing follicle to
      control proteolysis and fibrin formation at ovulation.
AD  - Infertility Clinic, Department of Gynaecology and Obstetrics, Geneva
      University Hospital, 1211 Geneva 14, Switzerland.
AU  - Princivalle M
AU  - Hasan S
AU  - Hosseini G
AU  - de Agostini AI
LA  - eng
PT  - Journal Article
CY  - England
TA  - Glycobiology
JC  - BEL
JID - 9104124
RN  - 0 (Anticoagulants)
RN  - 0 (DNA Primers)
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Iodine Radioisotopes)
RN  - 0 (RNA, Messenger)
SB  - IM
MH  - Animal
MH  - Anticoagulants/*metabolism
MH  - Autoradiography
MH  - Base Sequence
MH  - DNA Primers
MH  - Female
MH  - *Follicular Phase
MH  - Granulosa Cells/*metabolism
MH  - Heparan Sulfate Proteoglycan/genetics/*metabolism
MH  - Iodine Radioisotopes
MH  - RNA, Messenger/genetics/metabolism
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Support, Non-U.S. Gov't
EDAT- 2001/04/26 10:00
MHDA- 2001/07/13 10:01
URLF- http://glycob.oupjournals.org/cgi/content/full/11/3/183
URLS- http://glycob.oupjournals.org/cgi/content/abstract/11/3/183
PST - ppublish
SO  - Glycobiology 2001 Mar;11(3):183-94.




UI  - 21203689
PMID- 11306594
DA  - 20010418
DCOM- 20010607
IS  - 0021-9738
VI  - 107
IP  - 8
DP  - 2001 Apr
TI  - Syndecans: transmembrane modulators of adhesion and matrix assembly.
PG  - 935-41
AD  - Department of Cell Biology, University of Alabama at Birmingham, Volker
      Hall 203A, 1530 3rd Avenue S., Birmingham, AL 35294-0019, USA.
      awoods@cellbio.bhs.uab.edu
AU  - Woods A
LA  - eng
ID  - DK-54605/DK/NIDDK
PT  - Journal Article
CY  - United States
TA  - J Clin Invest
JC  - HS7
JID - 7802877
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - AIM
SB  - IM
MH  - Animal
MH  - Cell Adhesion/physiology
MH  - Extracellular Matrix/metabolism/physiology
MH  - Heparan Sulfate Proteoglycan/metabolism/*physiology
MH  - Membrane Glycoproteins/metabolism/*physiology
MH  - Proteoglycans/metabolism/*physiology
MH  - Support, U.S. Gov't, P.H.S.
EDAT- 2001/04/18 10:00
MHDA- 2001/06/08 10:01
URLF- http://www.jci.org/cgi/content/full/107/8/935
PST - ppublish
SO  - J Clin Invest 2001 Apr;107(8):935-41.




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
AU  - Hoffman MP
AU  - Engbring JA
AU  - Nielsen PK
AU  - Vargas J
AU  - Steinberg Z
AU  - Karmand AJ
AU  - Nomizu M
AU  - Yamada Y
AU  - Kleinman HK
LA  - eng
PT  - Journal Article
CY  - United States
TA  - J Biol Chem
JC  - HIV
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.




UI  - 21196779
PMID- 11302427
DA  - 20010413
DCOM- 20010802
IS  - 1031-3613
VI  - 12
IP  - 3-4
DP  - 2000
TI  - Localization and quantitation of hyaluronan and sulfated
      glycosaminoglycans in the tissues and intraluminal fluid of the pig
      oviduct.
PG  - 173-82
AB  - Glycosaminoglycans (GAGs), hyaluronan (HA) and heparan sulfate (HS) were
      localized in the pre- and post-ovulatory oviducts of inseminated and
      control (non-inseminated) sows using biotinylated HA-binding protein
      (HABP) and anti-syndecan antibodies respectively. In addition, the
      concentrations of HA and total sulfated GAGs (S-GAGs) were measured in
      fluid collected in vivo from either a selected tubal segment (isthmus or
      ampulla) or from the contralateral whole oviduct (WO) of non-inseminated
      sows during proestrus-metoestrus. HA was localized in the lamina propria
      of the entire oviduct, but epithelial HA-labelling was only present in the
      sperm reservoir (uterotubal junction adjacent isthmus) in control and
      inseminated sows. In contrast, immunolabelling for HS proteoglycans
      (HSPGs, syndecans) was present on the entire epithelial lining, both pre
      and post ovulation and in both sow groups. Both HA and S-GAGs could be
      detected in the intraluminal fluid. Concentrations varied among sows and
      segments; those of the S-GAGs being higher (P<0.05) than that of HA. Mean
      levels of S-GAGs and HA tended to increase in the fluid collected from
      isthmus and ampulla during standing oestrus. Fluid levels from the WO,
      however, fluctuated less during the collection period. Major statistical
      differences were not present, owing to the large variation seen between
      animals. The results confirm, however, that GAGs are present in the pig
      oviduct. The conspicuous localization in the sperm reservoir and the
      tendency to higher levels in the fluid during pre-ovulatory oestrus
      support the hypothesis that GAGs play a role in modulating sperm viability
      and capacitation during sperm transport in the pig oviduct.
AD  - Department of Anatomy and Histology, Faculty of Veterinary Medicine,
      Swedish University of Agricultural Sciences, Uppsala.
AU  - Tienthai P
AU  - Kjellen L
AU  - Pertoft H
AU  - Suzuki K
AU  - Rodriguez-Martinez H
LA  - eng
PT  - Journal Article
CY  - Australia
TA  - Reprod Fertil Dev
JC  - RAI
JID - 8907465
RN  - 0 (Glycosaminoglycans)
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 64082-61-7 (A73025)
RN  - 9004-61-9 (Hyaluronic Acid)
RN  - 9050-30-0 (Heparitin Sulfate)
SB  - IM
MH  - Animal
MH  - Body Fluids/metabolism
MH  - Cell Survival
MH  - Fallopian Tubes/*metabolism
MH  - Female
MH  - Glycosaminoglycans/analysis/*metabolism
MH  - Heparan Sulfate Proteoglycan/metabolism
MH  - Heparitin Sulfate/metabolism
MH  - Histocytochemistry
MH  - Hyaluronic Acid/analysis/*metabolism
MH  - Male
MH  - Membrane Glycoproteins/metabolism
MH  - Proteoglycans/metabolism
MH  - Sperm Capacitation
MH  - Spermatozoa/cytology
MH  - Support, Non-U.S. Gov't
MH  - Swine
EDAT- 2001/04/17 10:00
MHDA- 2001/08/03 10:01
PST - ppublish
SO  - Reprod Fertil Dev 2000;12(3-4):173-82.




UI  - 21194302
PMID- 11299835
DA  - 20010412
DCOM- 20010510
IS  - 0250-7005
VI  - 21
IP  - 1B
DP  - 2001 Jan-Feb
TI  - Syndecan-1 expression in different soft tissue tumours.
PG  - 733-7
AB  - BACKGROUND: In vitro studies have suggested that expression of syndecan-1
      (CD138) is correlated with morphologic phenotype (epithelioid or spindle)
      of cultured tumour cells. MATERIALS AND METHODS: Fifty-seven different
      soft tissue tumours were selected to analyse their syndecan-1 (CD138)
      reactivity. Immunohistochemical staining of paraffin sections, following a
      high temperature unmasking technique, was performed. The intensity and the
      pattern of staining was studied. RESULTS: Cell membrane positivity was
      observed in epithelioid sarcomas and epithelial elements of synovial
      sarcomas. GISTs, some malignant epithelioid schwannoma and some
      fibromatosis showed intracytoplasmatic reaction, while pyogenic granuloma,
      Kaposi's sarcoma, fibrosarcoma and dermatofibrosarcoma protuberans were
      negative. CONCLUSION: At first it seemed that the cell membrane positivity
      of syndecan-1 accompanied true epithelial differentiation in soft tissue
      sarcomas, but the results further highlighted the non specific nature of
      this expression. Therefore the heterogeneity in the appearance of
      syndecan-1 in various soft tissue tumours is not simply associated with
      the phenotype, suggesting more complex functions.
AD  - Department of Human and Experimental Tumour Pathology, National Institute
      of Oncology, H-1122 Budapest, Rath Gyorgy u. 7-9, Hungary. zso@oncol.hu
AU  - Orosz Z
AU  - Kopper L
LA  - eng
PT  - Journal Article
CY  - Greece
TA  - Anticancer Res
JC  - 59L
JID - 8102988
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - IM
MH  - Comparative Study
MH  - Dermatofibrosarcoma/chemistry/pathology
MH  - Epithelial Cells/chemistry
MH  - Fibrosarcoma/chemistry/pathology
MH  - Gastrointestinal Neoplasms/chemistry/pathology
MH  - Granuloma, Pyogenic/metabolism/pathology
MH  - Human
MH  - Leiomyosarcoma/chemistry/pathology
MH  - Membrane Glycoproteins/*analysis
MH  - Neoplasm Proteins/*analysis
MH  - Neurilemmoma/chemistry/pathology
MH  - Phenotype
MH  - Proteoglycans/*analysis
MH  - Sarcoma/*chemistry/pathology
MH  - Sarcoma, Kaposi/chemistry/pathology
MH  - Sarcoma, Synovial/chemistry/pathology
MH  - Soft Tissue Neoplasms/*chemistry/pathology
MH  - Specimen Handling/methods
EDAT- 2001/04/13 10:00
MHDA- 2001/05/22 10:01
PST - ppublish
SO  - Anticancer Res 2001 Jan-Feb;21(1B):733-7.




UI  - 21189515
PMID- 11292376
DA  - 20010409
DCOM- 20010621
IS  - 1084-9521
VI  - 12
IP  - 2
DP  - 2001 Apr
TI  - Molecular interactions of syndecans during development.
PG  - 107-16
AB  - The syndecans, cell surface heparan sulfate proteoglycans (HSPGs), bind
      numerous ligands via their HS glycosaminoglycan chains. The response to
      this binding is flavored by the identity of the core protein that bears
      the HS chains. Each of the syndecan core proteins has a short cytoplasmic
      domain that binds cytosolic regulatory factors. The syndecans also contain
      highly conserved transmembrane domain and extracellular domains for which
      important activities are slowly emerging. These protein domains, which
      will be the focus of this review, localize the syndecan to sites at the
      cell surface during development where they collaborate with other
      receptors to regulate signaling and cytoskeletal organization. Copyright
      2001 Academic Press.
AD  - Department of Pathology and Laboratory Medicine, University of
      Wisconsin-Madison, 1300 University Avenue, Madison, WI 53706, USA.
      acraprae@facstaff.wisc.edu
AU  - Rapraeger AC
LA  - eng
ID  - GM48850/GM/NIGMS
ID  - HD21881/HD/NICHD
PT  - Journal Article
PT  - Review
PT  - Review, Tutorial
CY  - England
TA  - Semin Cell Dev Biol
JC  - C2B
JID - 9607332
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animal
MH  - Cell Differentiation/*physiology
MH  - Human
MH  - Membrane Glycoproteins/*chemistry/*physiology
MH  - Molecular Sequence Data
MH  - Proteoglycans/*chemistry/*physiology
MH  - Support, U.S. Gov't, P.H.S.
RF  - 64
EDAT- 2001/04/09 10:00
MHDA- 2001/06/22 10:01
AID - 10.1006/scdb.2000.0239 [doi]
AID - scdb.2000.0239 [pii]
PST - ppublish
SO  - Semin Cell Dev Biol 2001 Apr;12(2):107-16.




UI  - 21175565
PMID- 11279653
DA  - 20010330
DCOM- 20010426
IS  - 0361-8609
VI  - 67
IP  - 1
DP  - 2001 May
TI  - Proximal promoter of the murine syndecan-1 gene is not sufficient for the
      developmental pattern of syndecan expression in B lineage cells.
PG  - 20-6
AB  - Syndecan-1 (CD138) is a cell membrane proteoglycan that binds
      extracellular matrix components and various growth factors. The role of
      syndecan-1 in the control of cell growth and morphology has been
      illustrated by its altered expression in hematological malignancies such
      as multiple myeloma as well as some solid tumors. It has been reported
      that the expression of syndecan-1 in cells of the B lineage is
      developmentally regulated such that pre-B cells and plasma cells express
      syndecan-1 while mature B cells do not. Thus, we investigated whether the
      proximal promoter region of the murine syndecan-1 promoter was able to
      confer the observed on-off-on expression of syndecan-1 in cells of the B
      lineage as they develop from pre-B cells to plasma cells. Experiments
      carried out using deletion mutants of the proximal promoter cloned
      upstream of the CAT reporter gene transfected into murine cell lines,
      representing the above stages of B-cell development, such as BA/F3 (pro-B
      cell), 70Z/3 (pre-B cell), 2PK3 (late mature B cell), and MPC-11 (plasma
      cell), showed detectable levels of CAT expression. The WEHI-231 (mature B
      cell) cell lines did not show detectable levels of CAT reporter activity.
      The strong levels of expression were observed with a fragment of the
      proximal promoter spanning the region from -365 to -95 (from the
      translation start point). However, Northern analysis of RNA obtained from
      the five murine B-cell lines, representing various stages of B-cell
      development, showed that the 70Z/3, MPC-11 but not BA/F3, and 2PK3 cells
      expressed detectable levels of syndecan-1 mRNA. By FACS analysis, using a
      rat anti mouse syndecan-1 antibody, syndecan-1 expression on the cell
      surface was found to correlate with the observed mRNA expression patterns
      in these cell lines. Our results indicate that the proximal promoter of
      the murine syndecan-1 promoter is not sufficient for the observed
      developmental pattern of syndecan expression in B cells. Copyright 2001
      Wiley-Liss, Inc.
AD  - Center for Biotechnology, Department of Biosciences, Karolinska Institute,
      NOVUM, Huddinge, Sweden.
AU  - Volpe CP
AU  - Lundgren A
AU  - Aints A
AU  - Mohamed AJ
AU  - Jaakkola P
AU  - Christensson B
AU  - Gahrton G
AU  - Jalkanen M
AU  - Smith CI
AU  - Dilber MS
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Am J Hematol
JC  - 3H4
JID - 7610369
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Transcription Factor, Sp1)
RN  - 0 (syndecan)
RN  - 63231-63-0 (RNA)
SB  - IM
MH  - Animal
MH  - B-Lymphocytes/*metabolism/physiology
MH  - Binding Sites
MH  - Blotting, Northern
MH  - Cell Line
MH  - Cell Lineage/genetics
MH  - Flow Cytometry
MH  - Gene Expression Regulation, Developmental/*genetics
MH  - Genes, Reporter
MH  - Membrane Glycoproteins/*genetics/*metabolism
MH  - Mice
MH  - Mutation
MH  - Plasma Cells/metabolism/physiology
MH  - *Promoter Regions (Genetics)
MH  - Proteoglycans/*genetics/*metabolism
MH  - RNA/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Transcription Factor, Sp1/metabolism
MH  - Transfection
EDAT- 2001/04/03 10:00
MHDA- 2001/05/01 10:01
PST - ppublish
SO  - Am J Hematol 2001 May;67(1):20-6.




UI  - 21162758
PMID- 11262187
DA  - 20010323
DCOM- 20010607
IS  - 0014-4827
VI  - 264
IP  - 2
DP  - 2001 Apr 1
TI  - Testosterone-induced growth of S115 mouse mammary tumor cells is dependent
      on heparan sulfate.
PG  - 307-14
AB  - The androgen-induced proliferation of S115 mouse mammary tumor cells has
      been suggested to involve autocrinic fibroblast growth factor signaling.
      Heparan sulfate proteoglycans are required for fibroblast growth factor
      signaling, presumably due to their ability to alter binding of fibroblast
      growth factors to their receptors. We have investigated the role of
      heparan sulfate proteoglycans in the testosterone-induced proliferation of
      S115 cells. We demonstrate that when the cells are treated with sodium
      chlorate, which inhibits the sulfation of endogenous heparan sulfate
      proteoglycans, cell growth becomes dependent on exogenous heparin. The
      shortest heparin oligosaccharides supporting cell growth were
      octasaccharides, whereas dodecasaccharides were almost as effective as
      native heparin. The N-, 2-O-, and 6-O-sulfate groups of heparin were all
      required for full testosterone response. Treatment of S115 cells with
      chlorate or testosterone did not alter the expression of fibroblast growth
      factor receptors 1 or 3, whereas the expression of fibroblast growth
      factor receptor 2 was down-regulated. We have previously shown that
      overexpression of syndecan-1 heparan sulfate proteoglycan renders S115
      cells insensitive to testosterone and now demonstrate that this effect can
      be overcome by sodium chlorate treatment in combination with exogenous
      heparin. Our results suggest that heparin-like molecules are intimately
      involved in the androgen-mediated proliferation of S115 cells. Copyright
      2001 Academic Press.
AD  - Turku Centre for Biotechnology, University of Turku and Abo Akademi
      University, Turku, FIN-20520, Finland. mhieta@btk.utu.fi
AU  - Borgenstrom M
AU  - Tienhaara A
AU  - Spillmann D
AU  - Salmivirta M
AU  - Jalkanen M
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Exp Cell Res
JC  - EPB
JID - 0373226
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, Fibroblast Growth Factor)
RN  - 0 (fibroblast growth factor receptor 1)
RN  - 0 (fibroblast growth factor receptor 3)
RN  - 0 (syndecan)
RN  - 57-85-2 (Testosterone)
RN  - 9005-49-6 (Heparin)
RN  - EC 2.7.1.- (bek protein)
RN  - EC 2.7.11.- (Receptor Protein-Tyrosine Kinases)
SB  - IM
MH  - Animal
MH  - *Cell Division
MH  - Gene Expression
MH  - Heparan Sulfate Proteoglycan/*metabolism/physiology
MH  - Heparin/metabolism
MH  - Mammary Neoplasms
MH  - Membrane Glycoproteins/biosynthesis/genetics
MH  - Mice
MH  - Proteoglycans/biosynthesis/genetics
MH  - Receptor Protein-Tyrosine Kinases/genetics
MH  - Receptors, Fibroblast Growth Factor/genetics
MH  - Structure-Activity Relationship
MH  - Support, Non-U.S. Gov't
MH  - Testosterone/*metabolism/pharmacology
MH  - Tumor Cells, Cultured
EDAT- 2001/03/23 10:00
MHDA- 2001/06/08 10:01
AID - 10.1006/excr.2000.5126 [doi]
AID - excr.2000.5126 [pii]
PST - ppublish
SO  - Exp Cell Res 2001 Apr 1;264(2):307-14.




UI  - 21158880
PMID- 11261330
DA  - 20010322
DCOM- 20010426
IS  - 0939-5555
VI  - 80
IP  - 2
DP  - 2001 Feb
TI  - Immunomagnetic enrichment of CD138 positive cells from weakly infiltrated
      myeloma patients samples enables the determination of the tumor clone
      specific IgH rearrangement.
PG  - 83-9
AB  - In multiple myeloma, the polymerase chain reaction (PCR) of the Ig heavy
      chain with allele-specific oligonucleotide (ASO) primers is a common and
      well-described method of identifying the tumor clone in peripheral blood
      (PB), bone marrow (BM) or leukapheresis products (LA). A factor which is
      crucial to the detection of clonal Ig rearrangements lies in the 'purity'
      of the tumor tissue used for the consensus PCR. We describe the
      application of a method to enrich CD138 positive myeloma cells derived
      from weakly infiltrated PB-, BM- and LA-samples. These are subjected to
      immunomagnetic enrichment with the MACS system, using an CD138 antibody
      directly conjugated to magnetic beads to obtain an enriched tumor cell
      population and the subsequent amplification of tumor specific IgH
      rearrangements. We investigated 29 samples (ten PB, ten BM, nine LA) with
      a median myeloma cell content of 0.5%. The approach led to a median
      enrichment factor of 118. Tumor-specific rearrangements could be amplified
      reproducibly from samples containing less than 0.1% myeloma cells.
AD  - Department of Internal Medicine I, University of Cologne, 50924 Cologne,
      Germany. Andreas.Draube@uni-koeln.de
AU  - Draube A
AU  - Pfister R
AU  - Vockerodt M
AU  - Schuster S
AU  - Kube D
AU  - Diehl V
AU  - Tesch H
LA  - eng
PT  - Journal Article
CY  - Germany
TA  - Ann Hematol
JC  - A2P
JID - 9107334
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - IM
MH  - Consensus Sequence
MH  - Gene Rearrangement, B-Lymphocyte, Light Chain
MH  - Human
MH  - Immunomagnetic Separation
MH  - Membrane Glycoproteins/*analysis
MH  - Multiple Myeloma/*immunology/*pathology
MH  - Polymerase Chain Reaction
MH  - Proteoglycans/*analysis
MH  - Sequence Analysis
MH  - Support, Non-U.S. Gov't
EDAT- 2001/03/23 10:00
MHDA- 2001/05/01 10:01
PST - ppublish
SO  - Ann Hematol 2001 Feb;80(2):83-9.




UI  - 21157397
PMID- 11257118
DA  - 20010321
DCOM- 20010426
IS  - 0021-9525
VI  - 152
IP  - 6
DP  - 2001 Mar 19
TI  - A role for syndecan-1 in coupling fascin spike formation by
      thrombospondin-1.
PG  - 1169-82
AB  - An important role of cell matrix adhesion receptors is to mediate
      transmembrane coupling between extracellular matrix attachment, actin
      reorganization, and cell spreading. Thrombospondin (TSP)-1 is a modulatory
      component of matrix expressed during development, immune response, or
      wound repair. Cell adhesion to TSP-1 involves formation of biochemically
      distinct matrix contacts based on stable fascin spikes. The cell surface
      adhesion receptors required have not been identified. We report here that
      antibody clustering of syndecan-1 proteoglycan specifically transduces
      organization of cortical actin and fascin bundles in several cell types.
      Transfection of COS-7 cells with syndecan-1 is sufficient to stimulate
      cell spreading, fascin spike assembly, and extensive protrusive lateral
      ruffling on TSP-1 or on syndecan-1 antibody. The underlying molecular
      mechanism depends on glycosaminoglycan (GAG) modification of the
      syndecan-1 core protein at residues S45 or S47 for cell membrane spreading
      and on the VC2 region of the cytoplasmic domain for spreading and fascin
      spike formation. Expression of the VC2 deletion mutant or GAG-negative
      syndecan-1 showed that syndecan-1 is necessary in spreading and fascin
      spike formation by C2C12 cells on TSP-1. These results establish a novel
      role for syndecan-1 protein in coupling a physiological matrix ligand to
      formation of a specific matrix contact structure.
AD  - Medical Research Council Laboratory for Molecular Cell Biology and
      Department of Biochemistry and Molecular Biology, University College
      London, London WC1E 6BT, United Kingdom. dmcbjca@ucl.ac.uk
AU  - Adams JC
AU  - Kureishy N
AU  - Taylor AL
LA  - eng
PT  - Journal Article
CY  - United States
TA  - J Cell Biol
JC  - HMV
JID - 0375356
RN  - 0 (Actins)
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, CD36)
RN  - 0 (Carrier Proteins)
RN  - 0 (Chelating Agents)
RN  - 0 (Culture Media, Serum-Free)
RN  - 0 (Glycosaminoglycans)
RN  - 0 (Integrins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Microfilament Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Thrombospondin 1)
RN  - 0 (integrin-associated protein p50)
RN  - 0 (syndecan)
RN  - 125361-02-6 (Vinculin)
RN  - 146808-54-0 (fascin)
RN  - 60-00-4 (Edetic Acid)
SB  - IM
MH  - Actins/metabolism
MH  - Animal
MH  - Antigens, CD/immunology
MH  - Antigens, CD36/metabolism
MH  - Carrier Proteins/immunology/*metabolism
MH  - Cell Adhesion/*physiology
MH  - Cell Line
MH  - Cell Membrane/physiology/ultrastructure
MH  - Cell Movement/*physiology
MH  - Cell Separation
MH  - Cell Surface Extensions/*metabolism
MH  - Cells, Cultured
MH  - Chelating Agents/pharmacology
MH  - Culture Media, Serum-Free
MH  - Cytoskeleton/*metabolism
MH  - Edetic Acid/pharmacology
MH  - Flow Cytometry
MH  - Glycosaminoglycans/chemistry/metabolism
MH  - Human
MH  - Immunoblotting
MH  - Integrins/immunology
MH  - Membrane Glycoproteins/chemistry/genetics/immunology/*metabolism
MH  - Mice
MH  - Microfilament Proteins/*metabolism
MH  - Microscopy, Fluorescence
MH  - Proteoglycans/chemistry/genetics/immunology/*metabolism
MH  - Recombinant Fusion Proteins/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Thrombospondin 1/*metabolism
MH  - Transfection
MH  - Vinculin/metabolism
EDAT- 2001/03/21 10:00
MHDA- 2001/05/01 10:01
URLF- http://www.jcb.org/cgi/content/full/152/6/1169
URLS- http://www.jcb.org/cgi/content/abstract/152/6/1169
PST - ppublish
SO  - J Cell Biol 2001 Mar 19;152(6):1169-82.




UI  - 21149694
PMID- 11251555
DA  - 20010319
DCOM- 20010503
IS  - 0007-0963
VI  - 144
IP  - 2
DP  - 2001 Feb
TI  - Immunohistochemical studies on proteoglycan expression in normal skin and
      chronic ulcers.
PG  - 254-9
AB  - BACKGROUND: Proteoglycans (PGs) represent a large family of complex
      molecules. They are found either as integral membrane components or
      constituents of the extracellular matrix. Their protein backbones are
      linked to different glycosaminoglycans, such as dermatan-, chondroitin-,
      keratan- or heparan sulphate. The molecules have specific functions during
      developmental processes as well as in diseases, such as cancer and
      inflammation. OBJECTIVES: The expression patterns of various
      cell-associated heparan and chondroitin/dermatan-sulphate PGs in human
      skin and chronic venous ulcers were investigated. METHODS: Tissue sections
      from 11 patients with chronic venous ulcers were used in this study.
      Monoclonal antibodies were used for detection of the proteoglycans
      syndecan-1, -2 and -4, glypican, CD44 and perlecan. RESULTS: The different
      PGs exhibited individual staining patterns. Syndecan-1 and -4 and glypican
      expression in chronic ulcers differed from the staining in normal skin.
      Whereas the expression of syndecan-4 and glypican in intact skin was
      mostly in the pericellular regions of keratinocytes, the epidermal cells
      from the wound edge contained mostly intracellular PGs. In the wound edge,
      syndecan-4 was predominantly expressed by epidermal basal layer cells.
      Syndecan-1 was less expressed at the epidermal wound margins. PGs bind
      growth factors, regulate proteolytic activity and act as matrix receptors.
      CONCLUSIONS: The altered expression patterns of glypican and syndecan-1
      and -4 in chronic ulcers reflect their possible roles during inflammation
      and cell proliferation. Hence, analysis of PG expression should be of
      interest in future studies on normal as well as defective wound healing.
AD  - Department of Dermatology, Biomedical Center, B14, Lund University,
      Tornavagen S-221 85 Lund, Sweden.
AU  - Lundqvist K
AU  - Schmidtchen A
LA  - eng
PT  - Journal Article
CY  - England
TA  - Br J Dermatol
JC  - AW0
JID - 0004041
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, CD44)
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 143972-95-6 (perlecan)
SB  - IM
MH  - Aged
MH  - Aged, 80 and over
MH  - Antibodies, Monoclonal
MH  - Antigens, CD44/metabolism
MH  - Chronic Disease
MH  - Heparan Sulfate Proteoglycan/metabolism
MH  - Human
MH  - Immunoenzyme Techniques
MH  - Keratinocytes/metabolism
MH  - Membrane Glycoproteins/metabolism
MH  - Proteoglycans/*metabolism
MH  - Skin/*metabolism
MH  - Support, Non-U.S. Gov't
MH  - Varicose Ulcer/*metabolism
EDAT- 2001/03/17 10:00
MHDA- 2001/05/05 10:01
AID - bjd4009 [pii]
PST - ppublish
SO  - Br J Dermatol 2001 Feb;144(2):254-9.




UI  - 21143585
PMID- 11246001
DA  - 20010314
DCOM- 20010621
IS  - 0945-053X
VI  - 20
IP  - 1
DP  - 2001 Feb
TI  - Proteoglycans in the nervous system--the quest for functional roles in
      vivo.
PG  - 23-35
AB  - Large numbers of different proteoglycans are expressed in tightly
      regulated spatio-temporal patterns by both the nerve cells (neurons) and
      the supporting glial cells of the nervous system. Several of these
      proteoglycans have been shown by studies in vitro to affect the migration
      of neural precursor cells, the elongation and pathfinding of neurites and
      the formation and stabilization of synapses. Such processes are important
      for the accurate wiring of the nervous system, and so it has been
      postulated that proteoglycans play an essential role during neural
      development. However, with few exceptions, the phenotypes of null
      mutations in mice and some human genetic diseases have provided little
      support for this view. Here we will review recent data from both in vitro
      and in vivo studies analyzing the function of proteoglycans in the nervous
      system in order to provide possible explanations for their apparent lack
      of function.
AD  - Institute for Biochemistry, Medical Faculty, University of Cologne,
      Cologne, Germany. ursula.hartmann@uni-koeln.de
AU  - Hartmann U
AU  - Maurer P
LA  - eng
PT  - Journal Article
PT  - Review
PT  - Review, Tutorial
CY  - Germany
TA  - Matrix Biol
JC  - B0T
JID - 9432592
RN  - 0 (Amyloid beta-Protein Precursor)
RN  - 0 (Antigens)
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (NG2 antigen)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 0 (testican)
RN  - 143972-95-6 (perlecan)
RN  - 9007-34-5 (Collagen)
SB  - IM
MH  - Amyloid beta-Protein Precursor/physiology
MH  - Animal
MH  - Antigens/physiology
MH  - Collagen/physiology
MH  - Heparan Sulfate Proteoglycan/physiology
MH  - Human
MH  - Membrane Glycoproteins/physiology
MH  - Mice
MH  - *Nervous System
MH  - Proteoglycans/*physiology
MH  - Support, Non-U.S. Gov't
RF  - 86
EDAT- 2001/03/14 10:00
MHDA- 2001/06/22 10:01
AID - S0945053X00001372 [pii]
PST - ppublish
SO  - Matrix Biol 2001 Feb;20(1):23-35.




UI  - 21135770
PMID- 11241302
DA  - 20010312
DCOM- 20010412
IS  - 0020-7136
VI  - 95
IP  - 1
DP  - 2001 Jan 20
TI  - Epithelial and stromal syndecan-1 expression as predictor of outcome in
      patients with gastric cancer.
PG  - 1-6
AB  - The prognostic value of the immunohistochemical expression of epithelial
      and stromal syndecan-1 was evaluated in 296 patients with gastric
      carcinoma. Formalin-fixed, paraffin-embedded specimens of gastric
      adenocarcinomas were stained with mouse monoclonal antibody B-B4 against
      human syndecan-1. Loss of immunoreactivity (syndecan-1 immunoreactivity
      correlated with a higher stage of disease (stages II-IV), tumour location
      in the upper third of the stomach, nodal metastases (N1 or N2), positive
      stromal syndecan-1 staining, deep tumour penetration (to subserosa or
      deeper = T2-T4), larger tumour size (> or = 5 cm) and intestinal type of
      cancer. No correlation between epithelial syndecan-1 immunoreactivity and
      age, gender, distant metastases, grade of differentiation or Borrmann
      classification was observed. Positive stromal syndecan-1 immunoreactivity
      correlated with decreased epithelial syndecan-1 expression, intestinal
      type of cancer and Borrmann type I. Patients with low epithelial
      syndecan-1 expression in cancer cells had worse overall survival than
      patients with strong epithelial syndecan-1 staining (p = 0.0012). Stromal
      syndecan-1-positive patients had a worse outcome than patients with
      syndecan-1-negative stroma (p = 0.0193). In Cox multivariate analysis,
      stromal syndecan-1 immunoreactivity was a prognostic factor independent of
      TNM stage, surgery for cure and tumour size. Thus, the immunohistochemical
      expression of syndecan-1 might be a predictor of outcome in patients with
      gastric adenocarcinoma. Copyright 2001 Wiley-Liss, Inc.
AD  - Department of Surgery, University of Helsinki, Helsinki, Finland.
AU  - Wiksten JP
AU  - Lundin J
AU  - Nordling S
AU  - Lundin M
AU  - Kokkola A
AU  - von Boguslawski K
AU  - Haglund C
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Int J Cancer
JC  - GQU
JID - 0042124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - IM
MH  - Adenocarcinoma/diagnosis/metabolism/mortality
MH  - Adult
MH  - Age Factors
MH  - Aged
MH  - Aged, 80 and over
MH  - Animal
MH  - Antibodies, Monoclonal/metabolism
MH  - Disease Progression
MH  - Epithelium/*metabolism
MH  - Female
MH  - Human
MH  - Immunohistochemistry
MH  - Lymphatic Metastasis
MH  - Male
MH  - Membrane Glycoproteins/*biosynthesis
MH  - Mice
MH  - Middle Age
MH  - Multivariate Analysis
MH  - Prognosis
MH  - Proteoglycans/*biosynthesis
MH  - Sex Factors
MH  - Stomach Neoplasms/*metabolism/mortality/*therapy
MH  - Stromal Cells/*metabolism
MH  - Support, Non-U.S. Gov't
MH  - Time Factors
MH  - Treatment Outcome
EDAT- 2001/03/10 10:00
MHDA- 2001/04/17 10:01
AID - 10.1002/1097-0215(20010120)95:1<1::AID-IJC1000>3.0.CO;2-5 [pii]
PST - ppublish
SO  - Int J Cancer 2001 Jan 20;95(1):1-6.




UI  - 21125951
PMID- 11228212
DA  - 20010306
DCOM- 20010503
IS  - 0268-1161
VI  - 16
IP  - 3
DP  - 2001 Mar
TI  - Increased adhesiveness and internalization of Neisseria gonorrhoeae and
      changes in the expression of epithelial gonococcal receptors in the
      Fallopian tube of copper T and Norplant users.
PG  - 463-8
AB  - Interaction of Neisseria gonorrhoeae with the oviductal epithelium in
      vitro was examined in 2 cm length segments obtained after surgical
      sterilization from users of copper T intrauterine device (IUD) or Norplant
      and control women. Segments perfused with N.gonorrhoeae suspensions were
      incubated from 30 min up to 4 h, fixed, frozen and cut in 6--10 microm
      sections. Bacteria were detected immunohistochemically with rabbit
      anti-gonococcal serum followed by light and confocal microscopy. Adhesion
      and internalization of gonococci by epithelial cells were observed at all
      incubation times, and both were higher in explants from users of copper T
      IUD or Norplant implants than controls. The epithelium of controls
      expressed CD66 and syndecan-1; but CD46 was found in only one out of six
      cases. The epithelium of copper T IUD users expressed CD66 but not
      syndecan-1 or CD46. Users of Norplant exhibited expression of CD46, CD66
      and syndecan-1. Label was always found along the luminal border of the
      epithelium. There were more intraepithelial lymphocytes in users of
      contraceptive methods than in controls. Results indicate that (i)
      N.gonorrhoeae invade the oviductal epithelium from the first minutes of
      exposure, (ii) the epithelium is constitutively endowed with two known
      receptors for the gonococcus, CD66 and syndecan-1, (iii) copper T IUD and
      Norplant users exhibit higher rates of attachment and internalization of
      the gonococcus into the oviductal epithelium associated with changes in
      expression of gonococcal receptors.
AD  - Universidad de Santiago de Chile, Facultad de Quimica y Biologia, Casilla
      40 Correo 33, Estacion Central, Santiago, Chile.
AU  - Fernandez R
AU  - Nelson P
AU  - Delgado J
AU  - Aguilera J
AU  - Massai R
AU  - Velasquez L
AU  - Imarai M
AU  - Croxatto HB
AU  - Cardenas H
LA  - eng
PT  - Journal Article
CY  - England
TA  - Hum Reprod
JC  - HRP
JID - 8701199
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, Differentiation)
RN  - 0 (CD66 antigen)
RN  - 0 (Contraceptive Agents, Female)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (membrane cofactor protein)
RN  - 0 (syndecan)
RN  - 7440-50-8 (Copper)
RN  - 797-63-7 (Levonorgestrel)
SB  - IM
MH  - Adult
MH  - Animal
MH  - Antigens, CD/metabolism
MH  - Antigens, Differentiation/metabolism
MH  - Bacterial Adhesion/*drug effects
MH  - Contraceptive Agents, Female/*pharmacology
MH  - *Copper
MH  - Epithelium/metabolism/microbiology/pathology
MH  - Fallopian Tubes/*metabolism/*microbiology/pathology
MH  - Female
MH  - Gonorrhea/metabolism/microbiology/pathology
MH  - Human
MH  - *Intrauterine Devices
MH  - Levonorgestrel/*pharmacology
MH  - Lymphocytes/pathology
MH  - Membrane Glycoproteins/metabolism
MH  - Neisseria gonorrhoeae/*physiology
MH  - Proteoglycans/metabolism
MH  - Rabbits
MH  - Support, Non-U.S. Gov't
EDAT- 2001/03/03 10:00
MHDA- 2001/05/05 10:01
URLF- http://humrep.oupjournals.org/cgi/content/full/16/3/463
URLS- http://humrep.oupjournals.org/cgi/content/abstract/16/3/463
PST - ppublish
SO  - Hum Reprod 2001 Mar;16(3):463-8.




UI  - 21117953
PMID- 11225246
DA  - 20010227
IS  - 0253-2727
VI  - 21
IP  - 11
DP  - 2000 Nov
TI  - [The expression, secretion and regulation of membrane-soluble syndecan-1
      in human multiple myeloma cells]
PG  - 572-6
AB  - OBJECTIVE: To analyze the expression, secretion and regulation of
      membrane-soluble syndecan-1 in human multiple myeloma cells, and to
      explore the relationship between syndecan-1 and the development of human
      multiple myeloma. METHODS: Syndecan-1 expression on the surface of
      malignant plasma cells was analyzed by immuno-staining, the levels of
      soluble syndecan-1 in the supernatant of cultured tumor cells by ELISA.
      RESULTS: 1. Human multiple myeloma cells expressed high levels of
      syndecan-1. The density of syndecan-1 varied from 170,000 to 800,000
      molecules per cell. The expression of syndecan-1 lost rapidly as the cells
      underwent apoptosis. 2. Most myeloma cells produced soluble syndecan-1,
      the rate of production did not correlate with the density of membrane
      syndecan-1. Moreover, the production of soluble syndecan-1 did not require
      serum. 3. The protein synthesis inhibitor cycloheximide inhibited the
      production of syndecan-1. The serine protease inhibitor antipain did not
      affect the secretion of syndecan-1. CONCLUSION: As a receptor of many
      growth factors, cytokines and heparin-like growth factors, syndecan-1
      might play an important role in tumor cell growth and homing in multiple
      myeloma development.
AD  - Department of Immunology, Suzhou University, Suzhou 215007, China.
AU  - Li X
AU  - Lu Z
AU  - Klein B
LA  - chi
PT  - Journal Article
CY  - China
TA  - Zhonghua Xue Ye Xue Za Zhi
JC  - CNL
JID - 8212398
SB  - IM
EDAT- 2001/02/28 10:00
MHDA- 2001/02/28 10:00
PST - ppublish
SO  - Zhonghua Xue Ye Xue Za Zhi 2000 Nov;21(11):572-6.




UI  - 21117275
PMID- 11207564
DA  - 20010227
DCOM- 20010329
IS  - 1462-5814
VI  - 2
IP  - 1
DP  - 2000 Feb
TI  - Syndecan-1 and syndecan-4 can mediate the invasion of OpaHSPG-expressing
      Neisseria gonorrhoeae into epithelial cells.
PG  - 69-82
AB  - Neisseria gonorrhoeae (Ngo) expressing the outer membrane protein OpaHSPG
      can adhere to and invade epithelial cells via binding to heparan sulphate
      proteoglycan (HSPG) receptors. In this study, we have investigated the
      role of syndecan-1 and syndecan-4, two members of the HSPG family, in the
      uptake of Ngo by epithelial cells. When overexpressed in HeLa cells, both
      syndecans co-localize with adherent Ngo on the host cell surface. This
      overexpression of syndecan-1 and syndecan-4 leads to a three- and
      sevenfold increase in Ngo invasion respectively. In contrast, transfection
      with the syndecan-1 and syndecan-4 mutant constructs lacking the
      intracellular domain results in an abrogation of the invasion process,
      characteristic of a dominant-negative mode of action. A concomitant loss
      of the capacity to mediate Ngo uptake was also observed with syndecan-4
      mutant constructs carrying lesions in the dimerization motif necessary for
      the binding of protein kinase C (PKC) and phosphatidylinositol
      4,5-bisphosphate (PIP2), and mutants that are deficient in a C-terminal
      EFYA amino acid motif responsible for binding to syntenin or CASK. We
      conclude that syndecan-1 and syndecan-4 can both mediate Ngo uptake into
      epithelial cells, and that their intracellular domains play a crucial role
      in this process, perhaps by mediating signal transduction or anchorage to
      the cytoskeleton.
AD  - Max-Planck-Institut fur Biologie, Abteilung Infektionsbiologie, Tubingen,
      Germany.
AU  - Freissler E
AU  - Meyer auf der Heyde A
AU  - David G
AU  - Meyer TF
AU  - Dehio C
LA  - eng
PT  - Journal Article
CY  - England
TA  - Cell Microbiol
JC  - DW3
JID - 100883691
RN  - 0 (Bacterial Outer Membrane Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 0 (syndecan-4)
RN  - EC 2.7.1.- (Protein Kinase C)
SB  - IM
MH  - Amino Acid Sequence
MH  - *Bacterial Adhesion
MH  - Bacterial Outer Membrane Proteins/*physiology
MH  - Epithelial Cells/metabolism/*microbiology
MH  - Gene Expression
MH  - Hela Cells
MH  - Human
MH  - Membrane Glycoproteins/genetics/metabolism/*physiology
MH  - Molecular Sequence Data
MH  - Neisseria gonorrhoeae/*pathogenicity
MH  - Protein Kinase C/antagonists & inhibitors
MH  - Protein Structure, Tertiary
MH  - Proteoglycans/genetics/metabolism/*physiology
MH  - Sequence Deletion
MH  - Support, Non-U.S. Gov't
MH  - Transfection
MH  - Tumor Cells, Cultured
EDAT- 2001/02/24 11:00
MHDA- 2001/04/03 10:01
AID - cmi36 [pii]
PST - ppublish
SO  - Cell Microbiol 2000 Feb;2(1):69-82.




UI  - 21095799
PMID- 11179419
DA  - 20010222
DCOM- 20010628
IS  - 1059-1524
VI  - 12
IP  - 2
DP  - 2001 Feb
TI  - Characterization of syntenin, a syndecan-binding PDZ protein, as a
      component of cell adhesion sites and microfilaments.
PG  - 339-50
AB  - Syntenin is a PDZ protein that binds the cytoplasmic C-terminal FYA motif
      of the syndecans. Syntenin is widely expressed. In cell fractionation
      experiments, syntenin partitions between the cytosol and microsomes.
      Immunofluorescence microscopy localizes endogenous and epitope-tagged
      syntenin to cell adhesion sites, microfilaments, and the nucleus. Syntenin
      is composed of at least three domains. Both PDZ domains of syntenin are
      necessary to target reporter tags to the plasma membrane. The addition of
      a segment of 10 amino acids from the N-terminal domain of syntenin to
      these PDZ domains increases the localization of the tags to stress fibers
      and induces the formation of long, branching plasma membrane extensions.
      The addition of the complete N-terminal region, in contrast, reduces the
      localization of the tags to plasma membrane/adhesion sites and stress
      fibers, and reduces the morphotypical effects. Recombinant domains of
      syntenin with the highest plasma membrane localization display the lowest
      nuclear localization. Syndecan-1, E-cadherin, beta-catenin, and
      alpha-catenin colocalize with syntenin at cell-cell contacts in epithelial
      cells, and coimmunoprecipitate with syntenin from extracts of these cells.
      These results suggest a role for syntenin in the composition of adherens
      junctions and the regulation of plasma membrane dynamics, and imply a
      potential role for syntenin in nuclear processes.
AD  - Laboratory for Glycobiology and Developmental Genetics, Center for Human
      Genetics, University of Leuven, Leuven, B-3000 Belgium.
AU  - Zimmermann P
AU  - Tomatis D
AU  - Rosas M
AU  - Grootjans J
AU  - Leenaerts I
AU  - Degeest G
AU  - Reekmans G
AU  - Coomans C
AU  - David G
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Mol Biol Cell
JC  - BAU
JID - 9201390
RN  - 0 (Cadherins)
RN  - 0 (Carrier Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 0 (syntenin)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animal
MH  - Cadherins/metabolism
MH  - Carrier Proteins/genetics/*metabolism
MH  - Cell Adhesion/physiology
MH  - Cell Communication
MH  - Cell Membrane/metabolism
MH  - Cell Nucleus/metabolism
MH  - Cells, Cultured
MH  - Conserved Sequence
MH  - Cytosol/metabolism
MH  - Epithelial Cells/metabolism
MH  - Human
MH  - Mammals
MH  - Membrane Glycoproteins/*metabolism
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Microfilaments/*metabolism
MH  - Microsomes/metabolism
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Proteoglycans/*metabolism
MH  - Rabbits
MH  - Sequence Homology, Amino Acid
MH  - Support, Non-U.S. Gov't
EDAT- 2001/02/17 11:00
MHDA- 2001/07/04 10:01
URLF- http://www.molbiolcell.org/cgi/content/full/12/2/339
URLS- http://www.molbiolcell.org/cgi/content/abstract/12/2/339
PST - ppublish
SO  - Mol Biol Cell 2001 Feb;12(2):339-50.




UI  - 21092153
PMID- 11175653
DA  - 20010222
DCOM- 20010329
IS  - 0003-9985
VI  - 125
IP  - 2
DP  - 2001 Feb
TI  - Plasmablastic lymphoma of the lung: report of a unique case and review of
      the literature.
PG  - 282-5
AB  - Non-Hodgkin lymphomas associated with acquired immunodeficiency syndrome
      are heterogeneous. Recently, a novel subtype of non-Hodgkin lymphoma
      occurring mostly in patients with acquired immunodeficiency syndrome has
      been described and designated as plasmablastic lymphoma. The
      histomorphologic and immunophenotypic findings of this distinct subtype of
      non-Hodgkin lymphoma have been characterized previously. Most patients
      present with oral cavity involvement. We report a case of plasmablastic
      lymphoma presenting as a lung tumor. To our knowledge, this is the first
      case report of this unusual subtype of diffuse large B-cell lymphoma in
      this location.
AD  - Department of Pathology, University of Iowa College of Medicine, Iowa
      City, USA.
AU  - Lin Y
AU  - Rodrigues GD
AU  - Turner JF
AU  - Vasef MA
LA  - eng
PT  - Journal Article
PT  - Review
PT  - Review of Reported Cases
CY  - United States
TA  - Arch Pathol Lab Med
JC  - 79Z
JID - 7607091
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (DNA, Viral)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (monoclonal antibody VS38)
RN  - 0 (syndecan)
SB  - AIM
SB  - IM
MH  - Acquired Immunodeficiency Syndrome/complications
MH  - Antibodies, Monoclonal
MH  - Case Report
MH  - DNA, Viral/analysis
MH  - Herpesvirus 4, Human/genetics
MH  - Human
MH  - Immunohistochemistry
MH  - Immunophenotyping
MH  - In Situ Hybridization
MH  - Lung Neoplasms/*diagnosis/immunology/pathology/virology
MH  - Lymphoma, AIDS-Related/*diagnosis/immunology/pathology/virology
MH  - Lymphoma, B-Cell/*diagnosis/pathology
MH  - Lymphoma, Large-Cell, Diffuse/*diagnosis/pathology
MH  - Male
MH  - Membrane Glycoproteins/analysis
MH  - Middle Age
MH  - Plasma Cells/pathology
MH  - Proteoglycans/analysis
RF  - 13
EDAT- 2001/02/15 11:00
MHDA- 2001/04/03 10:01
PST - ppublish
SO  - Arch Pathol Lab Med 2001 Feb;125(2):282-5.




