糖化白蛋白的化学与临床研究近期热点
Recent topics in chemical and clinical research on glycated albumin.
作者信息
Ueda Yuki, Matsumoto Hideyuki
机构信息
Diagnostics Department, Research and Development Group, Asahi Kasei Pharma Corporation, Shizuoka, Japan.
Diagnostics Department, Research and Development Group, Asahi Kasei Pharma Corporation, Shizuoka, Japan
出版信息
J Diabetes Sci Technol. 2015 Mar;9(2):177-82. doi: 10.1177/1932296814567225. Epub 2015 Jan 21.
Abstract
The measuring method for glycated albumin (GA) has been developed as a new glycemic control marker since the beginning of the 21st century. Since GA has an advantage in reflecting glycemic status over a shorter period than hemoglobin A1c (HbA1c), much research and many reviews have been reported. However, so far there have been few reports on glycation sites based on the tertiary structure of human serum albumin (HSA) and the comparison of glycation rates between GA and HbA1c in detail. The present review discusses how the glycation sites of lysine residues in HSA are modified with glucose, whereas the glycation sites of lysine residues are located inside of HSA as well as the direct comparison of glycation rates between GA and HbA1c using human blood. Moreover, the most recent clinical researches on GA are described.
摘要
自21世纪初以来，糖化白蛋白（GA）的测量方法已被开发为一种新的血糖控制指标。由于GA在反映血糖状态方面比糖化血红蛋白（HbA1c）具有更短时间的优势，因此已有许多研究和综述报道。然而，迄今为止，基于人血清白蛋白（HSA）的三级结构的糖化位点以及GA和HbA1c糖化率的详细比较的报道很少。本综述讨论了HSA中赖氨酸残基的糖化位点如何被葡萄糖修饰，而赖氨酸残基的糖化位点位于HSA内部，以及使用人体血液对GA和HbA1c糖化率进行直接比较。此外，还描述了关于GA的最新临床研究。
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