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 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.
Kueper
Thomas
T
R & D, Beiersdorf AG, Hamburg, Germany. Thomas.Kueper@beiersdorf.com
Grune
Tilman
T
Muhr
Gesa-Meike
GM
Lenz
Holger
H
Wittern
Klaus-Peter
KP
Wenck
Horst
H
Stäb
Franz
F
Blatt
Thomas
T
D001120:Arginine / Q000031:analogs & derivatives / Q000378:metabolism; D015153:Blotting, Western; D002478:Cells, Cultured; D005145:Face; D017127:Glycation End Products, Advanced / Q000378:metabolism* / Q000494:pharmacology; D006031:Glycosylation; D006037:Glyoxal / Q000494:pharmacology*; D006801:Humans; D008239:Lysine / Q000031:analogs & derivatives / Q000378:metabolism; D009646:Norleucine / Q000031:analogs & derivatives / Q000378:metabolism; D011758:Pyrroles / Q000378:metabolism; D011765:Pyruvaldehyde / Q000494:pharmacology*; D012867:Skin / Q000187:drug effects / Q000378:metabolism*; D014746:Vimentin / Q000302:isolation & purification / Q000378:metabolism*
D017127:Glycation End Products, Advanced; D011758:Pyrroles; D014746:Vimentin; D006037:Glyoxal; D011765:Pyruvaldehyde; C059571:2-formyl-5-(hydroxymethyl)pyrrole-1-norleucine; D009646:Norleucine; D001120:Arginine; C062187:pentosidine; D008239:Lysine