STRUCTURE OF COLLAGEN FIBRIL-ASSOCIATED, SMALL PROTEOGLYCANS OF MAMMALIAN ORIGIN

This chapter provides an overview of the structure of collagen fibril-associated, small proteoglycans (PGs) of mammalian origin. It focuses on the small dermatan sulfate collagen fibril-associated PGs from interstitial mammalian tissues and explains the structure of different glycosaminoglycans, along with the isolation and fractionation of small PGs, along with. All mammalian tissues contain PGs, which consist of a single protein core containing one to >200 glycosaminoglycan chains. The various types of PGs present in different tissues can be divided into two categories— namely, (1) cell-associated PGs and (2) extracellularmatrix PGs. Since the past decade, collagen fibril-associated PGs have begun to be characterized. These PGs have been isolated from normal bone, cartilage, scar, skin, and other connective tissues and have been shown to contain a protein core to which 1 or 2 glycosaminoglycan (GAG) chains are attached. Their molecular weights, in distinct contrast to the high density cartilage PG, range from 70 to 140 kDa and for this reason they are generally referred to as “the small PGs.” © 1991 Academic Press Inc.