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).
This paper describes a case of skin cancer resembling carcinoma en cuirasse associated with multiple bone lesions, which were both judged to be due to metastasis of poorly differentiated carcinoma of the stomach, the primary lesion excised ten years previously. Overt bone involvement had been observed for more than two years and a half. Histologic examination of a skin biopsy specimen showed that carcinoma cells had infiltrated into the middle and lower dermis, forming clusters and strands in an abundance of fibrous stromata. No primary lesion was detected in the remnant stomach at autopsy.
The N-glycosidically linked oligosaccharides were liberated by hydrazinolysis from purified proteodermatan sulphate from newborn-calf skin and reduced with NaB3H4 at the reducing terminal sugar. One asparagine-linked oligosaccharide chain was linked to one core-protein molecule in proteodermatan sulphate. Structural sequences were analysed by using exoglycosidase digestion. These oligosaccharides were composed of di- and tri-antennary oligosaccharide structures of complex type.
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