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A proteodermatan sulfate (PDS) was extracted from fresh calf skin with 3 M MgCl2 in the presence of protease inhibitors and purified repeatedly by dimethylaminoethyl (DEAE)-cellulose chromatography. The average molecular weights were estimated to be 112000 for PDS and 56000 for core protein from chondroitinase ABC-treated PDS in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Unsaturated disaccharide of the glycosaminoglycan side chain (molecular weight=20000) of PDS was found to be mainly composed (96.8%) of ΔDi-4S [2-acetamido-2-deoxy-3-O-(β-D-gluco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose] as determined by high-performance liquid chromatography (HPLC).Affinity-purified rat antibody against the core protein of PDS reacted specifically with PDS, but there was no cross-reaction with extracellular molecules such as Al-Di proteoglycan from cartilage, fibronectin, laminin, and types I, II, III and IV collagens. Furthermore, high specificity of the antibody to PDS was also observed by immunoblotting after SDS-PAGE. Indirect immunofluorescence staining of anti-core protein antibody in tissues generally appeared along with interstitial collagen (types I, II and III). However, the fine reticular fiber composed of types I and III collagens in liver was not stained.On the basis of these findings and of biochemical characterization of PDS, it is postulated that PDS possibly contributes to promotion of collagen fibrillogenesis and deposition in the extracellular matrix in vivo.

Biochemical and immunochemical characterization of proteodermatan sulfate from calf skin.