Qiu Hong-Yan, Hou Ning-Ning, Shi Jun-Feng, Liu Yong-Ping, Kan Cheng-Xia, Han Fang, Sun Xiao-Dong
Department of Endocrinology, The Affiliated Hospital of Weifang Medical University, Weifang 261031, Shandong Province, China.
Department of Pathology, The Affiliated Hospital of Weifang Medical University, Weifang 261031, Shandong Province, China.
World J Diabetes. 2021 Jul 15;12(7):1057-1069. doi: 10.4239/wjd.v12.i7.1057.
The presence of excess glucose in blood is regarded as a sweet hurt for patients with diabetes. Human serum albumin (HSA) is the most abundant protein in human plasma, which undergoes severe non-enzymatic glycation with glucose in patients with diabetes; this modifies the structure and function of HSA. Furthermore, the advanced glycation end products produced by glycated HSA can cause pathological damage to the human body through various signaling pathways, eventually leading to complications of diabetes. Many potential glycation sites on HSA have different degrees of sensitivity to glucose concentration. This review provides a comprehensive assessment of the glycation sites of HSA; it also discusses the effects of glycation on the structure and function of HSA. Moreover, it addresses the relationship between HSA glycation and diabetes complications. Finally, it focuses on the value of non-enzymatic glycation of HSA in diabetes-related clinical applications.
血液中葡萄糖过量对糖尿病患者来说是一种甜蜜的伤害。人血清白蛋白(HSA)是人体血浆中含量最丰富的蛋白质,在糖尿病患者中它会与葡萄糖发生严重的非酶糖基化反应;这会改变HSA的结构和功能。此外,糖化HSA产生的晚期糖基化终产物可通过各种信号通路对人体造成病理损害,最终导致糖尿病并发症。HSA上许多潜在的糖基化位点对葡萄糖浓度有不同程度的敏感性。本综述全面评估了HSA的糖基化位点;还讨论了糖基化对HSA结构和功能的影响。此外,阐述了HSA糖基化与糖尿病并发症之间的关系。最后,重点关注HSA非酶糖基化在糖尿病相关临床应用中的价值。