Glypican
From Wikipedia, the free encyclopedia
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]
[edit] Structure
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]
[edit] Genes
[edit] References
- ^ Filmus, J. (2001). "Glypicans in growth control and cancer". Glycobiology 11 (3): 19R–23R. doi:. PMID 11320054.
- ^ De Cat, B, David, G. (2001). "Developmental roles of the glypicans". Semin. Cell. Dev. Biol. 12 (2): 117–125. doi:. PMID 11292377.
- ^ 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. doi:. PMID 9331333.
