Summary: (from NCBI-Entrez) ..[read more]Cell surface heparan sulfate proteoglycans are composed of a membrane-associated protein core substituted with a variable number of heparan sulfate chains. Members of the glypican-related integral membrane proteoglycan family (GRIPS) contain a core protei
Karumanchi SA, et al.(Mol Cell. 2001) reported that Glypican 1 and glypican 4 are the lower-affinity binding receptors for ES by means of expressing cloning.
Liang Y, et al. (J Biol Chem. 1999) reported that five known rat and human Slit proteins contain 1523-1534 amino acids, and peptide sequences correspond best to those present in human Slit-1 and Slit-2. Binding of these ligands to the glypican-Fc fusion protein requires the presence of the heparan sulfate chains, but the interaction appears to be relatively specific for glypican-1 insofar as no other identified heparin-binding proteins were isolated using our affinity matrix. And they stated that Slit1 and Slit2 are functional ligands of glypican-1 in nervous tissue.
Liang Y, et al. (J Biol Chem. 1999) reported that five known rat and human Slit proteins contain 1523-1534 amino acids, and peptide sequences correspond best to those present in human Slit-1 and Slit-2. Binding of these ligands to the glypican-Fc fusion protein requires the presence of the heparan sulfate chains, but the interaction appears to be relatively specific for glypican-1 insofar as no other identified heparin-binding proteins were isolated using our affinity matrix. And they stated that Slit1 and Slit2 are functional ligands of glypican-1 in nervous tissue.