The glycation of albumin: structural and functional impacts

Biochimie. 2011 Apr;93(4):645-58. doi: 10.1016/j.biochi.2010.12.003. Epub 2010 Dec 16.

Abstract

Oxidative stress and protein modifications are frequently observed in numerous disease states. Glucose constitutes a vital nutrient necessary to cellular oxygen metabolism. However, hyperglycemia-associated damage is an important factor in diabetes disorders. Albumin, the major circulating protein in blood, can undergo increased glycation in diabetes. From recent studies, it has become evident that protein glycation has important implications for protein activity, unfolding, and degradation, as well as for cell functioning. After giving a brief overview of the key role of albumin in overall antioxidant defense, this review examines its role as a target of glycation reactions. A synthesis of state of the art methods for measuring and characterizing albumin glycation is detailed. In light of recent data, we then report the impact of glycation on the structure of albumin and its various activities, especially its antioxidant and binding capacities. The biological impact of glycated albumin on cell physiology is also discussed, specifically the role of the protein as a biological marker of diabetes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Antioxidants / chemistry
  • Antioxidants / metabolism
  • Diabetes Mellitus / blood
  • Diabetes Mellitus / genetics
  • Diabetes Mellitus / metabolism
  • Disease / genetics
  • Glucose / chemistry
  • Glucose / metabolism
  • Glycosylation
  • Humans
  • Hyperglycemia / genetics*
  • Oxidative Stress / physiology*
  • Protein Processing, Post-Translational / genetics
  • Protein Processing, Post-Translational / physiology
  • Reactive Oxygen Species / chemistry
  • Serum Albumin / chemistry
  • Serum Albumin / metabolism*
  • Serum Albumin / pharmacology
  • Serum Albumin / physiology
  • Structure-Activity Relationship

Substances

  • Antioxidants
  • Reactive Oxygen Species
  • Serum Albumin
  • glycosylated serum albumin
  • Glucose