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Evidence of Preferential Protein Targets for Age‐Related Modifications in Peripheral Blood Lymphocytes
Author(s) -
POGGIOLI SYLVIE,
MARY JEAN,
BAKALA HILAIRE,
FRIGUET BERTRAND
Publication year - 2004
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1297.034
Subject(s) - blot , glycation , gel electrophoresis , chemistry , proteomics , biochemistry , microbiology and biotechnology , two dimensional gel electrophoresis , intracellular , western blot , antibody , blood proteins , advanced glycation end product , proteome , biology , immunology , receptor , gene
A bstract : Oxidatively modified proteins have been analyzed in aging human peripheral blood lymphocytes since protein modification by oxidation and other related pathways 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. Advanced glycation end products (AGE) were quantified and the pattern of glycated proteins analyzed by two‐dimensional gel electrophoresis followed by Western blotting using an anti‐AGE antibody raised against glycated RNAse. The protein silver stain and the immunoblot patterns were not superimposable, indicating that glycoxidative modifications are targeting only a restricted set of proteins. Modification of proteins with the lipid peroxidation product 4‐hydroxy‐2‐nonenal has also been studied. The patterns of modified proteins have been analyzed using two‐ dimensional gel electrophoresis followed by Western blotting with an antibody recognizing 4‐hydroxy‐2‐nonenal protein adducts using the same proteomic approach as for glycoxidative modifications. Specific protein targets for these modifications, that might serve as biomarkers of aging lymphocytes, are currently characterized and identified by mass spectrometry.