Sini P, Denti A, Tira M E, Balduini C
Department of Biochemsitry A. Castellani University of Pavia, Italia.
Glycoconj J. 1997 Nov;14(7):871-4. doi: 10.1023/a:1018550307649.
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.
肌腱和角膜核心蛋白聚糖是不同硫酸皮肤素/蛋白聚糖（DS/PG），而区分I型胶原蛋白的生化参数是羟赖氨酸糖苷含量。我们研究了肌腱和角膜核心蛋白聚糖在PG:胶原单体摩尔比从0.15:1到0.45:1范围内，对不同糖基化的I型胶原蛋白原纤维形成的各个阶段（延迟期、dA/dt）的影响。所得结果表明，核心蛋白聚糖对原纤维形成的各个阶段发挥不同作用，这与胶原蛋白的糖基化程度相关：在相同的PG:胶原比例下，高糖基化角膜胶原蛋白的原纤维形成比低糖基化的（肌腱）更有效地受到抑制。此外，相对于异源胶原蛋白，肌腱和角膜核心蛋白聚糖对同源胶原蛋白的原纤维形成具有更高的调控作用。这些数据表明，核心蛋白聚糖/I型胶原蛋白相互作用可能存在与细胞外基质中存在的PG和胶原蛋白结构相关的组织特异性。
