Isolation and some structural analyses of a proteodermatan sulphate from calf skin

Abstract

A proteodermatan sulphate was isolated from 0.15 M-NaCl and 0.45 M-NaCl extracts of newborn-calf skin. The proteoglycan was separated from collagen and hyaluronic acid by precipitation with cetylpyridinium chloride and CsCl-density-gradient centrifugation. Further purification was performed by ion-exchange, affinity and molecular-sieve chromatography. The proteoglycan bound to concanavalin A-Sepharose in 1 M-NaCl. It gave a positive reaction with periodic acid/Schiff reagent and contained 8.3% of uronic acid. The dermatan sulphate, the only glycosaminoglycan component, was composed of 74% iduronosylhexosamine units and 26% glucuronosylhexosamine units. The Mr was assessed to be 15000-20000 by gel chromatography. The core protein was found to be a sialoglycoprotein that had O-glycosidic oligosaccharides with N-acetylgalactosamine at the reducing termini. The molar ratio of oligosaccharide chains to dermatan sulphate was approx. 3:1. From these results the proposed structure of proteodermatan sulphate is: one dermatan sulphate chain (average Mr 17500), three O-glycosidic oligosaccharide chains and probably N-glycosidic oligosaccharide chain(s) bound to one core-protein molecule (Mr 55000).

Deficiency of the core proteins of dermatan sulphate proteoglycans in a variant form of Ehlers‐Danlos syndrome

“…Therefore, we analysed glycosaminoglycans, including proteodermatan sulphate, in the patient's skin. Because dermatan sulphates were present in skin as dermatan sulphate proteoglycans, which were composed of mol, mass 55 kd core proteins and mol, mass 17.5 kd dermatan sulphate chains [17, 18], the defect in dermatan sulphate chains was thought to indicate a defect in the core protein of dermatan sulphate proteoglycans or in the enzymes involved in the synthesis by dermatan sulphate of, for example, C5 epimerase and sulphotransferase. Radioimmunoassay of DS‐proteoglycan core protein could not be done as purified core protein standard is not available.…”

Decorin Is a Zn2+ Metalloprotein

“…The purified recombinant proteins were analyzed on SDS-PAGE and Western blot using two polyclonal antibodies that were raised against synthetic peptides corresponding to amino acid residues 31-47 and 309 -326 of the mouse decorin core proteins, respectively. 2 The protein concentrations were determined based on the absorbance at A 280 and the calculated molar extinction coefficient of the different protein constructs (38).…”

“…Decorin, a small chondroitin/dermatan sulfate proteoglycan, is found in the extracellular matrix of a variety of tissues such as skin (1)(2)(3), cartilage (4,5), and bone (6,7). This proteoglycan is composed of a 40-kDa core protein and one glycosaminoglycan chain attached to a serine residue in the N-terminal part of the protein.…”

Decorin inhibits macrophage colony-stimulating factor proliferation of macrophages and enhances cell survival through induction of p27Kip1 and p21Waf1

“…Decorin belongs to a family of small leucine-rich proteoglycans 4,5 and is found in the ECM of several of tissues such as skin, 6,7 cartilage, 8,9 and bone. 10 The biologic importance of these molecules is unclear.…”

“…1 At the inflammatory sites, proteoglycans are both secreted by activated mononuclear leukocytes and released as a result of extracellular matrix (ECM) degradation. Thus, proteoglycans, which are major constituents of the ECM, are another class of molecules produced by monocytes and macrophages 2,3 that are potential modulators of the immune response.Decorin belongs to a family of small leucine-rich proteoglycans 4,5 and is found in the ECM of several of tissues such as skin, 6,7 cartilage, 8,9 and bone. 10 The biologic importance of these molecules is unclear.…”