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Modification of Vimentin
Author(s) -
Kueper Thomas,
Grune Tilman,
Muhr GesaMeike,
Lenz Holger,
Wittern KlausPeter,
Wenck Horst,
Stäb Franz,
Blatt Thomas
Publication year - 2008
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.1433.039
Subject(s) - methylglyoxal , vimentin , pentosidine , chemistry , maillard reaction , glycation , lysine , advanced glycation end product , arginine , biochemistry , intermediate filament protein , intermediate filament , amino acid , cell , biology , cytoskeleton , immunology , enzyme , receptor , immunohistochemistry
In a recent study, we were able to show that the intermediate filament protein vimentin aggregates in human dermal fibroblasts because of modification by the advanced glycation endproduct carboxymethyllysine (CML). In this work, we investigated the formation of intracellular CML in relation to the concentration of glucose in the culture medium. The natural degradation product of glucose, methylglyoxal, was able to induce the aggregation of vimentin. This dicarbonyl leads to the formation of the modifications MG‐H1 and carboxyethyllysine (CEL) as a result of the reaction with arginine and lysine residues of proteins. Furthermore, we found that the protein vimentin was modified, not only by CML and CEL, but also by pentosidine and pyrraline. These findings underline the special position of vimentin as a preferential target of the Maillard reaction in human skin.