Cohen Margo P
Institute for Metabolic Research, University City Science Center, 3508 Market Street, Suite 420, Philadelphia, PA 19104, USA.
Arch Biochem Biophys. 2003 Nov 1;419(1):25-30. doi: 10.1016/j.abb.2003.08.012.
Modification of proteins by nonenzymatic glycation is one of the underlying factors contributory to the development of complications of diabetes. In general, the nature of this structural modification falls into two broad categories: nonenzymatic glycation per se, which refers to the attachment of free carbohydrate to proteins in the Amadori construct, and Advanced Glycation Endproducts (AGE), which refers to a heterogeneous group of carbohydrate-modified products generated from the Amadori adduct by oxidation, polymerization, and other spontaneous reactions. This review will focus on the role of nonenzymatically glycated proteins, and in particular glycated serum albumin, in the pathogenesis of diabetic complications, and on pharmacologic approaches to mitigate their deleterious effects. Potential intervention strategies to lessen the influence of AGE-modified proteins, as well as of other contributory abnormalities, are discussed elsewhere in this volume.
蛋白质的非酶糖基化修饰是导致糖尿病并发症发生的潜在因素之一。一般来说,这种结构修饰的性质可分为两大类:非酶糖基化本身,是指游离碳水化合物与阿马多里产物中的蛋白质结合;晚期糖基化终产物(AGE),是指由阿马多里加合物通过氧化、聚合及其他自发反应生成的一组异质性碳水化合物修饰产物。本综述将聚焦于非酶糖基化蛋白质,尤其是糖化血清白蛋白在糖尿病并发症发病机制中的作用,以及减轻其有害影响的药理学方法。减轻AGE修饰蛋白以及其他相关异常影响的潜在干预策略将在本卷其他部分讨论。