Journal
EXPERIMENTAL GERONTOLOGY
Volume 37, Issue 10-11, Pages 1207-1215Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/S0531-5565(02)00145-6
Keywords
aging; human lymphocytes; protein glycation; advanced glycation end products; aging biomarkers; proteomics
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Advanced glycation end products (AGE) have been analyzed in aging human peripheral blood lymphocytes since protein glycation and glycoxidation are believed to contribute to the intracellular age-related accumulation of damaged proteins, a process that has been associated with the cellular functional deficits that occur with age. The appearance of AGE in cell lysates was monitored with an enzyme-linked immunosorbent assay using an anti-AGE antibody raised against glycated RNAse. When lymphocyte cytosolic extracts from old donors (86-91 years old) were compared with those from young donors (20-25 years old), a small but significant 40% increase of protein glycation was observed. In both age groups, further analysis of the pattern, of glycated proteins by two-dimensional gel electrophoresis followed by western blotting with the same anti-AGE antibody, showed that the protein silver stain and the immunoblot patterns were not superimposable indicating that glycoxidative modifications are targeting only a restricted set of proteins. Among these preferential protein targets, seven of them exhibited a significant age-related increased immunoreactivity with the anti-AGE antibody suggesting that the corresponding modified proteins might serve as biomarkers of aging lymphocytes. (C) 2002 Elsevier Science Inc. All rights reserved.
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