Role of decorin on in vitro fibrillogenesis of type I collagen.
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.
Sini
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P
Department of Biochemsitry A. Castellani University of Pavia, Italia.
Denti
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A
Tira
M E
ME
Balduini
C
C
D000818:Animals; D002417:Cattle; D003094:Collagen / Q000502:physiology*; D058575:Decorin; D004591:Electrophoresis, Polyacrylamide Gel; D016326:Extracellular Matrix Proteins; D008855:Microscopy, Electron, Scanning; D011509:Proteoglycans / Q000502:physiology*
D058575:Decorin; D016326:Extracellular Matrix Proteins; D011509:Proteoglycans; D003094:Collagen