Protein Modifications as Manifestations of Hyperglycemic Glucotoxicity in Diabetes and Its Complications

Author:

Zheng Hong12,Wu Jinzi1,Jin Zhen1,Yan Liang-Jun1

Affiliation:

1. Department of Pharmaceutical Sciences, UNT System College of Pharmacy, UNT Health Science Center, Fort Worth, TX, USA.

2. Department of Basic Theory of Traditional Chinese Medicine, College of Basic Medicine, Shandong University of Traditional Chinese Medicine, Jinan, Shandong, China.

Abstract

Diabetes and its complications are hyperglycemic toxicity diseases. Many metabolic pathways in this array of diseases become aberrant, which is accompanied with a variety of posttranslational protein modifications that in turn reflect diabetic glucotoxicity. In this review, we summarize some of the most widely studied protein modifications in diabetes and its complications. These modifications include glycation, carbonylation, nitration, cysteine S-nitrosylation, acetylation, sumoylation, ADP-ribosylation, O-GlcNAcylation, and succination. All these posttranslational modifications can be significantly attributed to oxidative stress and/or carbon stress induced by diabetic redox imbalance that is driven by activation of pathways, such as the polyol pathway and the ADP-ribosylation pathway. Exploring the nature of these modifications should facilitate our understanding of the pathological mechanisms of diabetes and its associated complications.

Publisher

SAGE Publications

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