Role of decorin on in vitro fibrillogenesis of type I collagen |
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Authors: | Patrizia Sini Antonella Denti M. Enrica Tira Cesare Balduini |
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Affiliation: | (1) Department of Biochemistry “A. Castellani”, University of Pavia, via Bassi 21, 27100 Pavia, Italia |
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Abstract: | Tendon and corneal decorins are differently iduronated dermatan sulphate/proteoglycan (DS/PG) and the biochemical parameter that differentiates type I collagens is the hydroxylysine glycoside content. We have examined the effect of tendon and corneal decorins on the individual phases (tlag, dA/dt) of differently glycosylated type I collagens fibril formation, at molar ratios PG:collagen monomer ranging from 0.15 : 1 to 0.45 : 1. The results obtained indicate that decorins exert a different effect on the individual phases of fibril formation, correlated to the degree of glycosylation of collagen: at the same PG:collagen ratio the fibril formation of highly glycosylated corneal collagen is more efficiently inhibited than that of the poorly glycosylated one (tendon). Moreover tendon and corneal decorins exert a higher control on the fibrillogenesis of homologous collagen with respect to the heterologous one. These data suggest a possible tissue-specificity of the interaction decorin/type I collagen correlated to the structure of the PG and collagen present in extracellular matrices. This revised version was published online in November 2006 with corrections to the Cover Date. |
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Keywords: | proteoglycans extracellular matrix collagen decorin collagen fibrillogenesis |
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