Membrane proteins of human erythrocytes are modified by advanced glycation end products during aging in the circulation

Biochem Biophys Res Commun. 1999 Apr 29;258(1):123-7. doi: 10.1006/bbrc.1999.0606.

Abstract

Recent immunological studies demonstrated that proteins in vivo in several diseases are subjected to post-translational modification by advanced glycation end products (AGEs), suggesting a potential role of AGEs in aging and age-enhanced disease processes such as diabetic complications, atherosclerosis and Alzheimer's disease. Nvarepsilon-(Carboxymethyl)lysine (CML) is one of the major AGE-structures demonstrated in vivo so far. In the present study, membrane proteins from young erythrocyte population were compared with those from senescent erythrocytes separated from the same individual in their CML-contents using a monoclonal antibody for CML (6D12). SDS-polyacrylamide gel electrophoresis and subsequent Western blot showed that 6D12 bound to the band 1, 2, 3, 4.2, 5, 6 and 7 proteins from senescent erythrocytes, but not to those from young erythrocytes. Furthermore, quantitative estimation of the reactivity of 6D12 to these erythrocyte membranes by ELISA showed that the reactivity of 6D12 to senescent erythrocyte membranes was 3- to 6-fold higher than that of young erythrocyte membranes. These results indicate that membrane proteins of circulating erythrocytes undergo CML-modification, and the modified proteins accumulated in an age-dependent manner during the life span of erythrocytes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aging / metabolism*
  • Enzyme-Linked Immunosorbent Assay
  • Erythrocyte Membrane / metabolism*
  • Glycation End Products, Advanced*
  • Humans
  • Membrane Proteins / metabolism*

Substances

  • Glycation End Products, Advanced
  • Membrane Proteins