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The glypican family of Heparan Sulfate proteoglycans are anchored to the cell-surface via a covalent linkage to glycosylphosphatidylinositol (GPI). Six glypican family members have been identified in vertebrates, two in Drosophila and one in C. elegans.[1]


All glypicans contain an N-terminal signal peptide and a hydrophobic domain in their C-terminal region, required for attachment of the GPI anchor. The amino acid sequences of the six vertebrate glypican family members vary from being 17% to 63% identical.[2] The location of 14 cysteine amino acids is conserved between the glypicans, suggesting the existence of a highly similar three-dimensional structure. The attachment of Heparan sulfate (HS) glycosaminoglycan chains to glypicans is restricted to the last 50 amino acids in the C-terminus, placing glypican HS chains close to the cell membrane.[3]


  • GPC1, GPC2, GPC3, GPC4, GPC5, GPC6


  1. ^ Filmus, J. (2001). "Glypicans in growth control and cancer". Glycobiology 11 (3): 19R-23R. PMID 11320054.
  2. ^ De Cat, B, David, G. (2001). "Developmental roles of the glypicans". Semin. Cell. Dev. Biol. 12 (2): 117-125. PMID 11292377.
  3. ^ Saunders S, Paine-Saunders S, and Lander AD. (1997). "Expression of the cell surface proteoglycan glypican-5 is developmentally regulated in kidney, limb, and brain". Dev. Biol. 190 (1): 78-93. PMID 9331333.
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Glypican". A list of authors is available in Wikipedia.
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