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- Table of Contents
Facts about Glypican-1.
May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (through the heparan sulfate side chains) with both kinds of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling.
Human | |
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Gene Name: | GPC1 |
Uniprot: | P35052 |
Entrez: | 2817 |
Belongs to: |
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glypican family |
FLJ38078; Glypican 1; glypican proteoglycan 1; glypican; glypican-1; GPC1
Mass (kDA):
61.68 kDA
Human | |
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Location: | 2q37.3 |
Sequence: | 2; NC_000002.12 (240435663..240468076) |
Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Endosome. S-nitrosylated form recycled in endosomes. Localizes to CAV1-containing vesicles close to the cell surface. Cleavage of heparan sulfate side chains takes place mainly in late endosomes. Associates with both forms of PRNP in lipid rafts. Colocalizes with APP in perinuclear compartments and with CP in intracellular compartments. Associates with fibrillar APP amyloid-beta peptides in lipid rafts in Alzheimer disease brains.; [Secreted glypican-1]: Secreted, extracellular space.
PMID: 2148568 by David G., et al. Molecular cloning of a phosphatidylinositol-anchored membrane heparan sulfate proteoglycan from human lung fibroblasts.
PMID: 12732622 by Mani K., et al. Prion, amyloid beta-derived Cu(II) ions, or free Zn(II) ions support S-nitroso-dependent autocleavage of glypican-1 heparan sulfate.