Chemical modification of muscle protein in diabetes
Chemical modification of muscle protein in diabetes
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DOI：
10.1016/j.abb.2004.03.012
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发表时间：
2004-05-15
影响因子：
3.9
通讯作者：
Baynes, JW
中科院分区：
文献类型：
--
作者：
Alt, N;Carson, JA;Baynes, JW
在总骨骼肌（腓肠肌）和肌原纤维蛋白中测量糖化（果糖-赖氨酸，FL）和高级糖氧化和脂氧化终产物（AGE/ALE）的水平，并与对照组和糖尿病大鼠的不溶性皮肤胶原中相同化合物的水平进行比较。总肌肉和肌原纤维蛋白中的FL水平是皮肤胶原中FL水平的3-5%。总肌肉和肌原纤维蛋白中的AGE/ALE、N-羧甲基赖氨酸（CML）和N-羧乙基赖氨酸也显著较低，与皮肤胶原蛋白中的25%水平相似。新描述的巯基AGE/ALE，S-（羧甲基）半胱氨酸（CMC），也在肌肉中进行了测量; CMC水平与CML的水平相当，并在糖尿病反应中类似地增加。虽然糖尿病患者肌肉蛋白中FL和AGE/ALE增加，但相对增加量小于皮肤胶原蛋白。这些数据表明，肌肉蛋白质在糖尿病中被部分保护以防止糖化和AGE/ALE形成的增加。(C)2004年爱思唯尔公司All rights reserved.
Levels of glycation (fructose-lysine, FL) and advanced glycoxidation and lipoxidation end-products (AGE/ALEs) were measured in total skeletal (gastrocnemius) muscle and myofibril protein and compared to levels of the same compounds in insoluble skin collagen of control and diabetic rats. Levels of FL in total muscle and myofibril protein were 3-5% the level of FL in skin collagen. The AGE/ALEs, N-epsilon-(carboxymethyl)lysine (CML) and N-epsilon-(carboxyethyl)lysine, were also significantly lower in total muscle and myofibril protein, similar to25% of levels in skin collagen. The newly described sulfhydryl AGE/ALE, S-(carboxymethyl)cysteine (CMC), was also measured in muscle; levels of CMC were comparable to those of CML and increased similarly in response to diabetes. Although FL and AGE/ALEs increased in muscle protein in diabetes, the relative increase was less than that seen in skin collagen. These data indicate that muscle protein is partially protected against the increase in both glycation and AGE/ALE formation in diabetes. (C) 2004 Elsevier Inc. All rights reserved.