The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Sdc1  -  syndecan 1

Rattus norvegicus

Synonyms: HSPG, SYND1, SYNDECA, Synd1, Syndecan, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Sdc1


High impact information on Sdc1

  • Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses [6].
  • Syndecan-1 expressed in Schwann cells causes morphological transformation and cytoskeletal reorganization and associates with actin during cell spreading [3].
  • To investigate the biological functions of transmembrane proteoglycans we have produced clonal cell lines of rat Schwann cells that express the hybrid proteoglycan syndecan-1 [3].
  • There was no apparent stable association of cell surface syndecan-1 with focal contact sites, as determined by dual staining with anti-syndecan-1 and anti-vinculin antibodies [3].
  • The syndecan-1 expressing cells exhibited significantly enhanced spreading on several different substrata, including fibronectin and laminin, and an altered morphology [3].

Chemical compound and disease context of Sdc1

  • In control rats, Adriamycin nephrosis was associated with significantly impaired GBM staining for both HSPG core protein (assessed from BL-31 staining) and HS staining (assessed from JM-403 staining) 12 weeks after disease induction [7].
  • To test this hypothesis, we studied the effects of lisinopril (5 mg/kg/24 h) on proteinuria, focal glomerulosclerosis (FGS) and glomerular heparan sulfate (HS) proteoglycan (HSPG) GBM staining in rats with established Adriamycin nephrosis [7].

Biological context of Sdc1


Anatomical context of Sdc1

  • We reported previously that syndecan-1 expression by cultured rate vascular smooth muscle cells (VSMCs) is induced by serum- or platelet-derived growth factor (PDGF) [12].
  • All four syndecan mRNAs were detected in uninjured rat carotid arteries [12].
  • Our previous studies indicated that cell surface proteoglycans were mostly heparan sulfate ones (HSPG) in 20 day-old Sertoli cells [Biochim. Biophys. Acta 1510 (2001) 474] [13].
  • Syndecan-1 and -2 mRNAs were increased 30 minutes after stimulation of quiescent rat mesangial cells (RMCs) with serum [14].
  • In polarized B lymphoid cells, syndecan-1 is targeted specifically to a discrete membrane domain termed the uropod that is located at the cell's trailing edge [15].

Associations of Sdc1 with chemical compounds

  • ARH-77 cells do not adhere to type I collagen and readily invade into collagen gels, but following expression of the transmembrane heparan sulfate proteoglycan syndecan-1, they bind collagen and fail to invade [16].
  • In contrast, syndecan-1 mRNA expression in response to serum was completely blocked in the presence of cycloheximide [12].
  • Within this functional domain, syndecan-1 promotes cell-cell adhesion and concentration of heparin binding growth factors [15].
  • Its cytoplasmic domain contains a central region unlike that of any other vertebrate or invertebrate syndecan core protein with a cationic motif that binds inositol phospholipids [17].
  • Despite distinct molecular masses of glypican and syndecan glycosaminoglycans and minor differences in disaccharide composition and sulfation pattern, the overall proportion and distribution of sulfated regions and the affinity for the Hep II domain were similar [18].

Regulatory relationships of Sdc1


Other interactions of Sdc1

  • Surprisingly, cells bearing a chimera composed of the glypican extracellular domain fused to the syndecan transmembrane and cytoplasmic domains bind to collagen but remain invasive, implying that adhesion to collagen is not by itself sufficient to inhibit invasion [16].
  • Our data indicated that the regulation of their expression specifically depends on the nature of HSPG and Sertoli cell developmental stage and evidenced a specific PKC regulation of HSPG mRNA expression [13].
  • Upon purification and deglycosylation, an antiserum to rat liver HSPGs that reacts primarily with syndecan-2 showed a strong signal corresponding to this protein and three weaker bands that may represent additional syndecans. mRNAs for syndecan-1, -2, and -4 were present in the cultures [14].
  • Syndecan-4 (syn-4), a transmembrane heparan sulfate-containing proteoglycan, is unique among the four members of the syndecan family in its specific cellular localization to complex cytoskeletal adhesion sites, i.e., focal adhesions [21].
  • Glypican-1, syndecan-1 and -4, potential bFGF coreceptors, are mainly regulated at the transcriptional level [22].

Analytical, diagnostic and therapeutic context of Sdc1


  1. Differential regulation of syndecan expression by osteosarcoma cell lines in response to cytokines but not osteotropic hormones. Birch, M.A., Skerry, T.M. Bone (1999) [Pubmed]
  2. Syndecan-1 in B lymphoid malignancies. Sanderson, R.D., Børset, M. Ann. Hematol. (2002) [Pubmed]
  3. Syndecan-1 expressed in Schwann cells causes morphological transformation and cytoskeletal reorganization and associates with actin during cell spreading. Carey, D.J., Stahl, R.C., Cizmeci-Smith, G., Asundi, V.K. J. Cell Biol. (1994) [Pubmed]
  4. Gene expression of syndecans and betaglycan in isolated rat liver cells. Weiner, O.H., Zoremba, M., Gressner, A.M. Cell Tissue Res. (1996) [Pubmed]
  5. Time-dependent increases in syndecan-1 and fibroglycan messenger RNA expression in the infarct zone after experimentally induced myocardial infarction in rats. Endo, C., Kusachi, S., Ninomiya, Y., Yamamoto, K., Murakami, M., Murakami, T., Shinji, T., Koide, N., Kondo, J., Tsuji, T. Coron. Artery Dis. (1997) [Pubmed]
  6. Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses. Hsueh, Y.P., Yang, F.C., Kharazia, V., Naisbitt, S., Cohen, A.R., Weinberg, R.J., Sheng, M. J. Cell Biol. (1998) [Pubmed]
  7. ACE inhibition preserves heparan sulfate proteoglycans in the glomerular basement membrane of rats with established adriamycin nephropathy. Wapstra, F.H., Navis, G.J., van Goor, H., van den Born, J., Berden, J.H., de Jong, P.E., de Zeeuw, D. Exp. Nephrol. (2001) [Pubmed]
  8. Regulated expression of syndecan in vascular smooth muscle cells and cloning of rat syndecan core protein cDNA. Cizmeci-Smith, G., Asundi, V., Stahl, R.C., Teichman, L.J., Chernousov, M., Cowan, K., Carey, D.J. J. Biol. Chem. (1992) [Pubmed]
  9. Direct binding of syndecan-4 cytoplasmic domain to the catalytic domain of protein kinase C alpha (PKC alpha) increases focal adhesion localization of PKC alpha. Lim, S.T., Longley, R.L., Couchman, J.R., Woods, A. J. Biol. Chem. (2003) [Pubmed]
  10. Fibroblast growth factor 2 endocytosis in endothelial cells proceed via syndecan-4-dependent activation of Rac1 and a Cdc42-dependent macropinocytic pathway. Tkachenko, E., Lutgens, E., Stan, R.V., Simons, M. J. Cell. Sci. (2004) [Pubmed]
  11. Expression of syndecan-1 and -3 during embryogenesis of the central nervous system in relation to binding with midkine. Nakanishi, T., Kadomatsu, K., Okamoto, T., Ichihara-Tanaka, K., Kojima, T., Saito, H., Tomoda, Y., Muramatsu, T. J. Biochem. (1997) [Pubmed]
  12. Syndecan-4 is a primary-response gene induced by basic fibroblast growth factor and arterial injury in vascular smooth muscle cells. Cizmeci-Smith, G., Langan, E., Youkey, J., Showalter, L.J., Carey, D.J. Arterioscler. Thromb. Vasc. Biol. (1997) [Pubmed]
  13. Protein kinase C regulation of glypican-1, syndecan-1 and syndecan-4 mRNAs expression during rat Sertoli cell development. Brucato, S., Villers, C. Biochimie (2002) [Pubmed]
  14. Heparan sulfate chains with antimitogenic properties arise from mesangial cell-surface proteoglycans. Wang, A., Miralem, T., Templeton, D.M. Metab. Clin. Exp. (1999) [Pubmed]
  15. Heparan sulfate regulates targeting of syndecan-1 to a functional domain on the cell surface. Yang, Y., Børset, M., Langford, J.K., Sanderson, R.D. J. Biol. Chem. (2003) [Pubmed]
  16. Heparan sulfate proteoglycans as adhesive and anti-invasive molecules. Syndecans and glypican have distinct functions. Liu, W., Litwack, E.D., Stanley, M.J., Langford, J.K., Lander, A.D., Sanderson, R.D. J. Biol. Chem. (1998) [Pubmed]
  17. Regulation of inositol phospholipid binding and signaling through syndecan-4. Couchman, J.R., Vogt, S., Lim, S.T., Lim, Y., Oh, E.S., Prestwich, G.D., Theibert, A., Lee, W., Woods, A. J. Biol. Chem. (2002) [Pubmed]
  18. Heparan sulfate chains from glypican and syndecans bind the Hep II domain of fibronectin similarly despite minor structural differences. Tumova, S., Woods, A., Couchman, J.R. J. Biol. Chem. (2000) [Pubmed]
  19. 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. Wu, X., Kan, M., Wang, F., Jin, C., Yu, C., McKeehan, W.L. Cancer Res. (2001) [Pubmed]
  20. Heparan sulfate proteoglycans modulate monocyte migration across cerebral endothelium. Floris, S., van den Born, J., van der Pol, S.M., Dijkstra, C.D., De Vries, H.E. J. Neuropathol. Exp. Neurol. (2003) [Pubmed]
  21. Localization of the transmembrane proteoglycan syndecan-4 and its regulatory kinases in costameres of rat cardiomyocytes: a deconvolution microscopic study. VanWinkle, W.B., Snuggs, M.B., De Hostos, E.L., Buja, L.M., Woods, A., Couchman, J.R. Anat. Rec. (2002) [Pubmed]
  22. Cell surface heparan sulfate proteoglycans: target and partners of the basic fibroblast growth factor in rat Sertoli cells. Brucato, S., Bocquet, J., Villers, C. Eur. J. Biochem. (2002) [Pubmed]
WikiGenes - Universities