
Comprehensive overview of human serum albumin glycation in diabetes mellitus
Author(s) -
Hongyan Qiu,
Ningning Hou,
Junfeng Shi,
Yongping Liu,
Chengxia Kan,
Fang Han,
Xiaodong Sun
Publication year - 2021
Publication title -
world journal of diabetes
Language(s) - English
Resource type - Journals
ISSN - 1948-9358
DOI - 10.4239/wjd.v12.i7.1057
Subject(s) - medicine , diabetes mellitus , glycation , albumin , human serum albumin , bioinformatics , endocrinology , biochemistry , chemistry , biology
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 in vivo 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.