Amino Acids

, Volume 25, Issue 3, pp 275–281

Maillard reaction products in tissue proteins: New products and new perspectives

  • S. R. Thorpe
  • J. W. Baynes
Review Article

DOI: 10.1007/s00726-003-0017-9

Cite this article as:
Thorpe, S. & Baynes, J. Amino Acids (2003) 25: 275. doi:10.1007/s00726-003-0017-9

Summary.

 The chemical modification of protein by nonenzymatic browning or Maillard reactions increases with age and in disease. Maillard products are formed by reactions of both carbohydrate- and lipid-derived intermediates with proteins, leading to formation of advanced glycation and lipoxidation end-products (AGE/ALEs). These modifications and other oxidative modifications of amino acids increase together in proteins and are indicators of tissue aging and pathology. In this review, we describe the major pathways and characteristic products of chemical modification of proteins by carbohydrates and lipids during the Maillard reactions and identify major intersections between these pathways. We also describe a new class of intracellular sulfhydryl modifications, Cys-AGE/ALEs, that may play an important role in regulatory biology and represent a primitive link between nonenzymatic and enzymatic chemistry in biological systems.

Keywords: Advanced glycation end-product (AGE) – Advanced lipoxidation end-product (ALE) – Nε-(carboxymethyl)lysine – Glyoxal – Maillard reaction – Methylglyoxal

Copyright information

© Springer-Verlag/Wien 2003

Authors and Affiliations

  • S. R. Thorpe
    • 1
  • J. W. Baynes
    • 1
  1. 1.Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina, U.S.A.US
  2. 2.School of Medicine, University of South Carolina, Columbia, South Carolina, U.S.A.US