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Gene Review

GPC1  -  glypican 1

Homo sapiens

Synonyms: Glypican-1, glypican
 
 
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Disease relevance of GPC1

  • 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 [1].
  • We used monoclonal antibodies specific for the cell surface HSPGs (syndecans, glypican), for matrix HSPG (perlecan), and for heparan sulfate carbohydrate (HS) to investigate their immunohistochemical expression in 20 specimens with chronic cholestatic liver disease and in five normal human liver specimens [2].
  • In summary, these observations suggest that altered HSPGs contribute to enhanced signaling of FGF-2 via FGFR1c in gliomas with glypican-1 playing a significant role in this mitogenic pathway [3].
  • Immunohistochemical analysis revealed a highly significant overexpression of glypican-1 in human astrocytoma and oligodendroglioma samples compared with nonneoplastic gliosis [3].
  • Gingival specimens from healthy, gingivitis, or chronic periodontitis sites were stained by means of antibodies against B- and T-lymphocytes and also syndecan-1, syndecan-4, and glypican [4].
 

Psychiatry related information on GPC1

 

High impact information on GPC1

  • Mutations in GPC3, a glypican gene, cause the Simpson-Golabi-Behmel overgrowth syndrome [6].
  • Affinity isolation and enzymatic degradation demonstrated that HBP released from human neutrophils binds to endothelial cell-surface proteoglycans, such as syndecans and glypican [7].
  • The cell-surface heparan sulfate proteoglycan glypican-1 regulates growth factor action in pancreatic carcinoma cells and is overexpressed in human pancreatic cancer [8].
  • Here we show that the glycosylphosphatidylinositol- (GPI-) anchored HSPG glypican-1 is strongly expressed in human pancreatic cancer, both by the cancer cells and the adjacent fibroblasts, whereas expression of glypican-1 is low in the normal pancreas and in chronic pancreatitis [8].
  • Growth factor-induced shedding of syndecan-1 confers glypican-1 dependence on mitogenic responses of cancer cells [9].
 

Chemical compound and disease context of GPC1

 

Biological context of GPC1

  • 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 [1].
  • One recovered GPC4 cDNA with an open reading frame of 1668nt encodes a putative protein containing three heparan sulfate glycosylation signals and the 14 signature cysteines of the glypican family [11].
  • Functional promoter activity of the rat GPC1 sequence was demonstrated by its ability to drive the expression of a luciferase reporter gene in several cell types [12].
  • One of the genomic clones extended approximately 2.8 kb 5' of the exon 1 coding sequence, and is thus likely to contain sequences that regulate GPC1 gene expression [12].
  • The rat GPC1 gene is approximately 15kb in length and consists of eight exons interrupted by introns of varying lengths [12].
 

Anatomical context of GPC1

 

Associations of GPC1 with chemical compounds

  • Mammalian homologues of the Drosophila slit protein are ligands of the heparan sulfate proteoglycan glypican-1 in brain [14].
  • Analysis of luciferase and green fluorescent protein transgene expression showed superior transduction efficiency of Ad5.pK7 in keratinocytes and Ad5.RGD.pK7 in fibroblasts. mRNA expression of alpha(upsilon) integrin, syndecan-1 and glypican-1 was significantly higher in primary fibroblasts than CAR [16].
  • We have investigated the expression patterns and subcellular localization in nervous tissue of glypican, a major glycosylphosphatidylinositol-anchored heparan sulfate proteoglycan that is predominantly synthesized by neurons, and of biglycan, a small, leucine-rich chondroitin sulfate proteoglycan [10].
  • Transfection of COS-1 cells with an epitope-tagged glypican cDNA demonstrated transport of the full-length proteoglycan to the nucleus, and there are also dynamic changes in the pattern of glypican immunoreactivity in the nucleus of C6 cells both during cell division and correlated with different phases of the cell cycle [10].
  • The glypican family, which currently includes glypican, the developmentally regulated rat intestinal transcript OCI-5, and cerebroglycan, is characterized by a similar core protein size and almost complete conservation of cysteine residues [17].
 

Physical interactions of GPC1

 

Enzymatic interactions of GPC1

 

Regulatory relationships of GPC1

 

Other interactions of GPC1

 

Analytical, diagnostic and therapeutic context of GPC1

References

  1. Glypican-1 is overexpressed in human breast cancer and modulates the mitogenic effects of multiple heparin-binding growth factors in breast cancer cells. Matsuda, K., Maruyama, H., Guo, F., Kleeff, J., Itakura, J., Matsumoto, Y., Lander, A.D., Korc, M. Cancer Res. (2001) [Pubmed]
  2. Heparan sulfate proteoglycan expression in chronic cholestatic human liver diseases. Roskams, T., Rosenbaum, J., De Vos, R., David, G., Desmet, V. Hepatology (1996) [Pubmed]
  3. Glypican-1 is frequently overexpressed in human gliomas and enhances FGF-2 signaling in glioma cells. Su, G., Meyer, K., Nandini, C.D., Qiao, D., Salamat, S., Friedl, A. Am. J. Pathol. (2006) [Pubmed]
  4. Cell-surface proteoglycan expression by lymphocytes from peripheral blood and gingiva in health and periodontal disease. Manakil, J.F., Sugerman, P.B., Li, H., Seymour, G.J., Bartold, P.M. J. Dent. Res. (2001) [Pubmed]
  5. Different heparan sulfate proteoglycans serve as cellular receptors for human papillomaviruses. Shafti-Keramat, S., Handisurya, A., Kriehuber, E., Meneguzzi, G., Slupetzky, K., Kirnbauer, R. J. Virol. (2003) [Pubmed]
  6. Mutations in GPC3, a glypican gene, cause the Simpson-Golabi-Behmel overgrowth syndrome. Pilia, G., Hughes-Benzie, R.M., MacKenzie, A., Baybayan, P., Chen, E.Y., Huber, R., Neri, G., Cao, A., Forabosco, A., Schlessinger, D. Nat. Genet. (1996) [Pubmed]
  7. Heparin-binding protein targeted to mitochondrial compartments protects endothelial cells from apoptosis. Olofsson, A.M., Vestberg, M., Herwald, H., Rygaard, J., David, G., Arfors, K.E., Linde, V., Flodgaard, H., Dedio, J., Müller-Esterl, W., Lundgren-Akerlund, E. J. Clin. Invest. (1999) [Pubmed]
  8. The cell-surface heparan sulfate proteoglycan glypican-1 regulates growth factor action in pancreatic carcinoma cells and is overexpressed in human pancreatic cancer. Kleeff, J., Ishiwata, T., Kumbasar, A., Friess, H., Büchler, M.W., Lander, A.D., Korc, M. J. Clin. Invest. (1998) [Pubmed]
  9. Growth factor-induced shedding of syndecan-1 confers glypican-1 dependence on mitogenic responses of cancer cells. Ding, K., Lopez-Burks, M., Sánchez-Duran, J.A., Korc, M., Lander, A.D. J. Cell Biol. (2005) [Pubmed]
  10. Glypican and biglycan in the nuclei of neurons and glioma cells: presence of functional nuclear localization signals and dynamic changes in glypican during the cell cycle. Liang, Y., Häring, M., Roughley, P.J., Margolis, R.K., Margolis, R.U. J. Cell Biol. (1997) [Pubmed]
  11. Glypican 3 and glypican 4 are juxtaposed in Xq26.1. Huber, R., Mazzarella, R., Chen, C.N., Chen, E., Ireland, M., Lindsay, S., Pilia, G., Crisponi, L. Gene (1998) [Pubmed]
  12. Organization, 5'-flanking sequence and promoter activity of the rat GPC1 gene. Asundi, V.K., Keister, B.F., Carey, D.J. Gene (1998) [Pubmed]
  13. Glypican-1 is a VEGF165 binding proteoglycan that acts as an extracellular chaperone for VEGF165. Gengrinovitch, S., Berman, B., David, G., Witte, L., Neufeld, G., Ron, D. J. Biol. Chem. (1999) [Pubmed]
  14. Mammalian homologues of the Drosophila slit protein are ligands of the heparan sulfate proteoglycan glypican-1 in brain. Liang, Y., Annan, R.S., Carr, S.A., Popp, S., Mevissen, M., Margolis, R.K., Margolis, R.U. J. Biol. Chem. (1999) [Pubmed]
  15. Agrin is a major heparan sulfate proteoglycan accumulating in Alzheimer's disease brain. Verbeek, M.M., Otte-Höller, I., van den Born, J., van den Heuvel, L.P., David, G., Wesseling, P., de Waal, R.M. Am. J. Pathol. (1999) [Pubmed]
  16. Strategies to enhance transductional efficiency of adenoviral-based gene transfer to primary human fibroblasts and keratinocytes as a platform in dermal wounds. Stoff, A., Rivera, A.A., Banerjee, N.S., Michael Mathis, J., Espinosa-de-Los-Monteros, A., Le, L.P., De la Torre, J.I., Vasconez, L.O., Broker, T.R., Richter, D.F., Stoff-Khalili, M.A., Curiel, D.T. Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society. (2006) [Pubmed]
  17. K-glypican: a novel GPI-anchored heparan sulfate proteoglycan that is highly expressed in developing brain and kidney. Watanabe, K., Yamada, H., Yamaguchi, Y. J. Cell Biol. (1995) [Pubmed]
  18. Correlation of glypican-1 expression with TGF-beta, BMP, and activin receptors in pancreatic ductal adenocarcinoma. Kayed, H., Kleeff, J., Keleg, S., Jiang, X., Penzel, R., Giese, T., Zentgraf, H., B??chler, M.W., Korc, M., Friess, H. Int. J. Oncol. (2006) [Pubmed]
  19. Glypican-1 as an Abeta binding HSPG in the human brain: its localization in DIG domains and possible roles in the pathogenesis of Alzheimer's disease. Watanabe, N., Araki, W., Chui, D.H., Makifuchi, T., Ihara, Y., Tabira, T. FASEB J. (2004) [Pubmed]
  20. Subcellular localization of PP5/TFPI-2 in human placenta: a possible role of PP5/TFPI-2 as an anti-coagulant on the surface of syncytiotrophoblasts. Udagawa, K., Yasumitsu, H., Esaki, M., Sawada, H., Nagashima, Y., Aoki, I., Jin, M., Miyagi, E., Nakazawa, T., Hirahara, F., Miyazaki, K., Miyagi, Y. Placenta (2002) [Pubmed]
  21. Modulations of glypican-1 heparan sulfate structure by inhibition of endogenous polyamine synthesis. Mapping of spermine-binding sites and heparanase, heparin lyase, and nitric oxide/nitrite cleavage sites. Ding, K., Sandgren, S., Mani, K., Belting, M., Fransson, L.A. J. Biol. Chem. (2001) [Pubmed]
  22. Processing by convertases is not required for glypican-3-induced stimulation of hepatocellular carcinoma growth. Capurro, M.I., Shi, W., Sandal, S., Filmus, J. J. Biol. Chem. (2005) [Pubmed]
  23. Distribution and clinical significance of heparan sulfate proteoglycans in ovarian cancer. Davies, E.J., Blackhall, F.H., Shanks, J.H., David, G., McGown, A.T., Swindell, R., Slade, R.J., Martin-Hirsch, P., Gallagher, J.T., Jayson, G.C. Clin. Cancer Res. (2004) [Pubmed]
  24. Characterization of glypican-5 and chromosomal localization of human GPC5, a new member of the glypican gene family. Veugelers, M., Vermeesch, J., Reekmans, G., Steinfeld, R., Marynen, P., David, G. Genomics (1997) [Pubmed]
  25. GPC6, a novel member of the glypican gene family, encodes a product structurally related to GPC4 and is colocalized with GPC5 on human chromosome 13. Paine-Saunders, S., Viviano, B.L., Saunders, S. Genomics (1999) [Pubmed]
  26. Characterization of Slit protein interactions with glypican-1. Ronca, F., Andersen, J.S., Paech, V., Margolis, R.U. J. Biol. Chem. (2001) [Pubmed]
  27. Augmented synthesis and differential localization of heparan sulfate proteoglycans in Duchenne muscular dystrophy. Alvarez, K., Fadic, R., Brandan, E. J. Cell. Biochem. (2002) [Pubmed]
  28. Expression pattern alterations of syndecans and glypican-1 in normal and pathological trophoblast. Crescimanno, C., Marzioni, D., Paradinas, F.J., Schrurs, B., Mühlhauser, J., Todros, T., Newlands, E., David, G., Castellucci, M. J. Pathol. (1999) [Pubmed]
 
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