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proteoglycan
Proteoglycans are proteins that are heavily glycosylated. The basic proteoglycan unit consists of a "core protein" with one or more covalently attached glycosaminoglycan (GAG) chain(s). The point of attachment is a serine (Ser) residue to which the glycosaminoglycan is joined through a tetrasaccharide bridge (e.g. chondroitin sulfate-GlcA-Gal-Gal-Xyl-PROTEIN). The Ser residue is generally in the sequence -Ser-Gly-X-Gly- (where X can be any amino acid residue but Proline), although not every protein with this sequence has an attached glycosaminoglycan. The chains are long, linear carbohydrate polymers that are negatively charged under physiological conditions due to the occurrence of sulfate and uronic acid groups. Proteoglycans occur in the connective tissue.
==Types==
Proteoglycans are categorized by their relative size (large and small) and the nature of their glycosaminoglycan chains.〔PMID:25701227 〕
Types include:
Certain members are considered members of the "small leucine-rich proteoglycan family" (SLRP). These include decorin, biglycan, fibromodulin and lumican.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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