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- W142445669 abstract "Bone matrix proteoglycans and glycoproteins are proportionally the most abundant constituents of the noncollagenous proteins in bone matrix. Proteoglycan are characterized by the covalent attachment of long chain polysaccharides (glycosaminoglycans, GAGs) to core protein molecules. GAGs are composed of repeating carbohydrate units that are sulfated to varying degrees, and include chondroitin sulfate (CS), dermatan sulfate (DS), keratan sulfate (KS), and heparin sulfate (HS). Different subclasses of proteoglycan are generally characterized by the structure of the core protein and by the nature of the GAG. Proteoglycans with protein cores composed of the leucine-rich repeat sequences such as decorin, biglycan, fibromodulin, and osteoadherin, are the predominant form found in mineralized matrix, although hyaluronan-binding forms are present during early stages of osteogenesis. They participate in matrix organization and in regulating growth factor activity. Glycoproteins, such as alkaline phosphatase, osteonectin, RGD-containing proteins (osteoadherin, thrombospondin, fibronectin, vitronectin, osteopontin, bone sialoprotein), fibrillin, and tetranectin are produced at different stages of osteoblastic maturation. They exhibit a broad array of functions ranging from control of cell proliferation, cell-matrix interactions, and mediation of hydroxyapatite deposition. The ectopic expression of bone matrix proteins may also play a significant role in pathological states such as bone metastasis in certain forms of cancer and atherosclerosis." @default.
- W142445669 created "2016-06-24" @default.
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- W142445669 date "2002-01-01" @default.
- W142445669 modified "2023-10-13" @default.
- W142445669 title "Bone Matrix Proteoglycans and Glycoproteins" @default.
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- W142445669 doi "https://doi.org/10.1016/b978-012098652-1.50116-5" @default.
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