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Membrane sulfated glycosaminoglycans refer collectively to linear sulfated polysaccharide chains—such as heparan sulfate, chondroitin sulfate, dermatan sulfate, and keratan sulfate—that are covalently attached to specific core proteins to form proteoglycans present on the cell surface[1][4][5]. The two major membrane proteoglycan families are syndecans (type I membrane proteins with heparan and/or chondroitin sulfate chains) and glypicans (glycosylphosphatidylinositol-anchored, with heparan sulfate chains)[1][4]. These structures mediate and modulate cell adhesion, growth factor signaling, migration, tissue remodeling, and inflammation, and are implicated in the etiology of cancer and various inflammatory and fibrotic diseases[1][2][4][5]. Their biological effects are determined by the patterns of sulfation, chain length, and the core protein to which they are attached[2][4].
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