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Membrane Proteins of Human Erythrocytes Are Modified by Advanced Glycation End Products during Aging in the Circulation

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
258
Issue
1
Identifiers
DOI: 10.1006/bbrc.1999.0606
Disciplines
  • Biology
  • Medicine

Abstract

Abstract Recent immunological studies demonstrated that proteins in vivoin 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. N ε-(Carboxymethyl)lysine (CML) is one of the major AGE-structures demonstrated in vivoso 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.

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