链脲佐菌素诱导糖尿病中N-糖基化I型胶原蛋白的特性分析
Characterization of N-glycosylated type I collagen in streptozotocin-induced diabetes.
作者信息
Le Pape A, Muh J P, Bailey A J
出版信息
Biochem J. 1981 Aug 1;197(2):405-12. doi: 10.1042/bj1970405.
Abstract
The N epsilon-glycosylation of lysine and hydroxylysine residues in collagen from streptozotocin-induced-diabetic rats was confirmed and the stability of the complex shown to be due to an Amadori rearrangement. The studies also demonstrate the relative specificities of glucose, galactose and mannose in their reaction with collagen. The glycosylation of lysine in vitro occurs with glucose and galactose, but not with mannose, whereas only gucose reacts with hydroxylysine to any significant extent. Glycosylation of collagen occurs slowly during normal aging, but in contrast with reports suggesting accelerated aging of collagen in diabetic animals, we clearly demonstrated that the apparent increased stability is not due to an acceleration of the normal maturation process involving the reducible cross-links.
摘要
已证实链脲佐菌素诱导的糖尿病大鼠胶原蛋白中赖氨酸和羟赖氨酸残基的N-ε-糖基化，且该复合物的稳定性表明是由于阿马多里重排。这些研究还证明了葡萄糖、半乳糖和甘露糖与胶原蛋白反应的相对特异性。体外赖氨酸的糖基化发生在葡萄糖和半乳糖存在时，而甘露糖不存在时，然而只有葡萄糖能与羟赖氨酸发生显著反应。胶原蛋白的糖基化在正常衰老过程中发生缓慢，但与提示糖尿病动物胶原蛋白加速衰老的报道相反，我们清楚地证明，其明显增加的稳定性并非由于涉及可还原交联的正常成熟过程加速所致。
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