title: Glypicans.
abstract: A family of lipid-linked heparan sulfate (HS) proteoglycans, later named glypicans, were identified some 15 years ago. The discoveries that mutations in genes involved in glypican assembly cause developmental defects have brought them into focus. Glypicans have a characteristic pattern of 14 conserved cysteine residues. There are also two-three attachment sites for HS side-chains near the membrane anchor. The HS side-chains consist of a repeating disaccharide back-bone that is regionally and variably modified by epimerization and different types of sulfations, creating a variety of binding sites for polycationic molecules, especially growth factors. Recycling forms of glypican-1 are potential vehicles for transport of cargo into and through cells. The glypican-1 core protein is S-nitrosylated and nitric oxide released from these sites cleave the HS chains at glucosamine units lacking N-substitution. This processing is necessary for polyamine uptake.
authors.affiliation: Department of Cell and Molecular Biology, BMC C13, Lund University, SE-221 84, Lund, Sweden. lars-ake.fransson@medkem.lu.se
authors.forename: Lars-Ake
authors.initials: LA
authors.lastname: Fransson
mesh_terms: D000818:Animals; D001692:Biological Transport; D018507:Gene Expression Regulation, Developmental; D006133:Growth Substances / Q000378:metabolism; D019812:Heparan Sulfate Proteoglycans / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D006497:Heparan Sulfate / Q000378:metabolism; D006801:Humans; D009569:Nitric Oxide / Q000378:metabolism; D011073:Polyamines / Q000378:metabolism
chemical_list: D006133:Growth Substances; D019812:Heparan Sulfate Proteoglycans; D006497:Heparan Sulfate; D009569:Nitric Oxide; D011073:Polyamines