CHARACTERIZATION OF A HEPARAN-SULFATE AND A PECULIAR CHONDROITIN 4-SULFATE PROTEOGLYCAN FROM PLATELETS - INHIBITION OF THE AGGREGATION PROCESS BY PLATELET CHONDROITIN SULFATE PROTEOGLYCAN

CHARACTERIZATION OF A HEPARAN-SULFATE AND A PECULIAR CHONDROITIN 4-SULFATE PROTEOGLYCAN FROM PLATELETS - INHIBITION OF THE AGGREGATION PROCESS BY PLATELET CHONDROITIN SULFATE PROTEOGLYCAN

Author Nader, Helena Bonciani Autor UNIFESP Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Abstract A high molecular weight chondroitin sulfate proteoglycan (M(r) 240,000) is released from platelet surface during aggregation induced by several pharmacological agents. Some details on the structure of this compound are reported. Beta-elimination with alkali and borohydride produces chondroitin sulfate chains with a molecular weight of 40,000. The combined results indicate a proteoglycan molecule containing 5-6 chondroitin sulfate chains and a protein core rich in serine and glycine residues. Degradation with chondroitinase AC shows that a 4-sulfated disaccharide is the only disaccharide released from this chondroitin sulfate, characterizing it as a chondroitin 4-sulfate homopolymer. It is shown that this proteoglycan inhibits the aggregation of platelets induced by ADP. Analysis of the sulfated glycosaminoglycans not released during aggregation revealed the presence of a heparan sulfate in the platelets. Degradation by heparitinases I and II yielded the four disaccharide units of heparan sulfates: N,O-disulfated disaccharide, N-sulfated disaccharide, N-acetylated 6-sulfated disaccharide, and N-acetylated disaccharide. The possible role of the sulfated glycosaminoglycans on cell-cell interaction is discussed in view of the present findings.
Language English
Date 1991-06-05
Published in Journal Of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 266, n. 16, p. 10518-10523, 1991.
ISSN 0021-9258 (Sherpa/Romeo, impact factor)
Publisher Amer Soc Biochemistry Molecular Biology Inc
Extent 10518-10523
Origin http://www.jbc.org/content/266/16/10518.abstract
Access rights Open access Open Access
Type Article
Web of Science ID WOS:A1991FP08600079
URI http://repositorio.unifesp.br/11600/44197

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