Modification of vimentin: a general mechanism of nonenzymatic glycation in human skin

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 c...

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Bibliographic Details
Published in:Annals of the New York Academy of Sciences 2008-04, Vol.1126 (1), p.328-332
Main Authors: Kueper, Thomas, Grune, Tilman, Muhr, Gesa-Meike, Lenz, Holger, Wittern, Klaus-Peter, Wenck, Horst, Stäb, Franz, Blatt, Thomas
Format: Article
Language:English
Subjects:
Arginine - analogs & derivatives
Arginine - metabolism
Blotting, Western
Cells, Cultured
Face
Glycation End Products, Advanced - metabolism
Glycation End Products, Advanced - pharmacology
Glycosylation
Glyoxal - pharmacology
Humans
Lysine - analogs & derivatives
Lysine - metabolism
Norleucine - analogs & derivatives
Norleucine - metabolism
Pyrroles - metabolism
Pyruvaldehyde - pharmacology
Skin - drug effects
Skin - metabolism
Vimentin - isolation & purification
Vimentin - metabolism
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Summary: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.
ISSN:0077-8923
1749-6632
DOI:10.1196/annals.1433.039