衰老和糖尿病中人类胶原蛋白的糖基化
Glucosylation of human collagen in aging and diabetes mellitus.
作者信息
Schnider S L, Kohn R R
出版信息
J Clin Invest. 1980 Nov;66(5):1179-81. doi: 10.1172/JCI109950.
Abstract
Several of the characteristic complications of diabetes mellitus resemble age-like changes in collagen-rich tissues. It has been reported that increased glucosylation of hemoglobin and serum proteins occurs in diabetes. Glucosylation of insoluble human tendon collagen, a protein with little or no turnover was determined by a thiobarbituric acid method in 23 subjects as a function of age and the presence or absence of diabetes. Amounts of glucose and collagen solubilized by collagenase digestion of the samples were also determined. Glucosylation of collagen was found to increase with age and was markedly increased in juvenile onset diabetes. There appeared to be a limit to the amount of glucosylation that could occur, and older individuals with maturity-onset diabetes demonstrated glucosylation within that limit. The glucose nonenzymatically bound to human collagen may indicate the level of long-term control of the diabetes, and may play a role in the alteration of collagenous tissue properties that occurs in both aging and diabetes.
摘要
糖尿病的几种典型并发症类似于富含胶原蛋白组织的衰老样变化。据报道，糖尿病患者血红蛋白和血清蛋白的糖基化增加。采用硫代巴比妥酸法测定了23名受试者中不溶性人肌腱胶原蛋白（一种周转率很低或无周转率的蛋白质）的糖基化情况，该糖基化情况是年龄以及是否患有糖尿病的函数。还测定了通过胶原酶消化样品所溶解的葡萄糖和胶原蛋白量。发现胶原蛋白的糖基化随年龄增加，在青少年发病型糖尿病中显著增加。糖基化的量似乎存在一个限度，成年发病型糖尿病的老年个体的糖基化在该限度内。非酶促结合到人胶原蛋白上的葡萄糖可能表明糖尿病的长期控制水平，并可能在衰老和糖尿病中发生的胶原组织特性改变中起作用。
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