Qiu HY, Hou NN, Shi JF, Liu YP, Kan CX, Han F, Sun XD. Comprehensive overview of human serum albumin glycation in diabetes mellitus. World J Diabetes 2021; 12(7): 1057-1069 [PMID: 34326954 DOI: 10.4239/wjd.v12.i7.1057]
Corresponding Author of This Article
Xiao-Dong Sun, PhD, Professor, Department of Endocrinology, The Affiliated Hospital of Weifang Medical University, No. 2428 Yuhe Road, Weifang 261031, Shandong Province, China. sxdfriend@sina.com
Research Domain of This Article
Endocrinology & Metabolism
Article-Type of This Article
Review
Open-Access Policy of This Article
This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
Hong-Yan Qiu, Ning-Ning Hou, Jun-Feng Shi, Yong-Ping Liu, Cheng-Xia Kan, Xiao-Dong Sun, Department of Endocrinology, The Affiliated Hospital of Weifang Medical University, Weifang 261031, Shandong Province, China
Fang Han, Department of Pathology, The Affiliated Hospital of Weifang Medical University, Weifang 261031, Shandong Province, China
Author contributions: Qiu HY and Hou NN were responsible for conceptualization, methodology, data curation, and original draft preparation; Shi JF, Liu YP, Kan CX, and Han F were responsible for data curation and investigation; Sun XD was responsible for supervision, manuscript writing and editing, and funding acquisition.
Supported bythe National Natural Science Foundation of China, No. 81870593; Natural Science Foundation of Shandong Province of China, No. ZR2020MH106; and Medical Health Science and Technology Project of Shandong Province, No. 202003060400.
Conflict-of-interest statement: The authors declare that they have no conflict of interest to disclose.
Open-Access: This article is an open-access article that was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution NonCommercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/Licenses/by-nc/4.0/
Corresponding author: Xiao-Dong Sun, PhD, Professor, Department of Endocrinology, The Affiliated Hospital of Weifang Medical University, No. 2428 Yuhe Road, Weifang 261031, Shandong Province, China. sxdfriend@sina.com
Received: March 16, 2021 Peer-review started: March 16, 2021 First decision: May 3, 2021 Revised: May 6, 2021 Accepted: June 4, 2021 Article in press: June 4, 2021 Published online: July 15, 2021 Processing time: 118 Days and 2.5 Hours
Abstract
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.
Core Tip: In the case of hyperglycemia state, the glycation level of albumin in plasma is significantly increased, which alters the structure and function of albumin. Herein we review the different glycation sites and functional changes of glycated albumin, and discuss the relationship between albumin glycation and diabetes complications. The potential application value of glycated albumin in clinical is also discussed.
