Intervention strategies to prevent pathogenetic effects of glycated albumin

Arch Biochem Biophys. 2003 Nov 1;419(1):25-30. doi: 10.1016/j.abb.2003.08.012.

Abstract

Modification of proteins by nonenzymatic glycation is one of the underlying factors contributory to the development of complications of diabetes. In general, the nature of this structural modification falls into two broad categories: nonenzymatic glycation per se, which refers to the attachment of free carbohydrate to proteins in the Amadori construct, and Advanced Glycation Endproducts (AGE), which refers to a heterogeneous group of carbohydrate-modified products generated from the Amadori adduct by oxidation, polymerization, and other spontaneous reactions. This review will focus on the role of nonenzymatically glycated proteins, and in particular glycated serum albumin, in the pathogenesis of diabetic complications, and on pharmacologic approaches to mitigate their deleterious effects. Potential intervention strategies to lessen the influence of AGE-modified proteins, as well as of other contributory abnormalities, are discussed elsewhere in this volume.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Antibodies, Monoclonal / therapeutic use
  • Carbohydrate Metabolism
  • Diabetes Mellitus / etiology
  • Diabetic Nephropathies / complications
  • Diabetic Nephropathies / physiopathology
  • Diabetic Nephropathies / prevention & control*
  • Extracellular Matrix Proteins / metabolism
  • Forecasting
  • Glycation End Products, Advanced / metabolism
  • Glycosylation
  • Humans
  • Models, Biological
  • Protein Binding
  • Protein Kinase C / metabolism
  • Serum Albumin / immunology
  • Serum Albumin / pharmacology*
  • Transforming Growth Factor beta / metabolism

Substances

  • Antibodies, Monoclonal
  • Extracellular Matrix Proteins
  • Glycation End Products, Advanced
  • Serum Albumin
  • Transforming Growth Factor beta
  • glycated serum albumin
  • Protein Kinase C