In vitro glycoxidation of insoluble fibrous type I collagen: solubilization and advanced glycation end products.
The deleterious effects of glycoxidation are dependent on the half-life of proteins. Collagen, the main component of extracellular matrices, is a long live protein and thus may be sensitive to the glycoxidation process. We incubated calf skin fibrous type I collagen in PBS at 37 degrees C with glucose. The fibrous type I collagen was solubilized and an increase in the amount of advanced glycation end products of the solubilized fraction was observed. As there was no bacterial contamination and no proteolytic activities in the incubation medium, the solubilization of fibrous type I collagen is probably due to the speculative production of the free radicals in our experimental conditions. To test this hypothesis, fibrous type I collagen was incubated in PBS with AAPH (2,2'azo-bis 2-aminodinopropane) a free radicals generator. AAPH induced a dramatic and dose dependent solubilization of fibrous type I collagen.
Meli
M
M
Department of Biochemistry, University Hospital, 42055 Saint-Etienne, France.
Granouillet
R
R
Reynaud
E
E
Chamson
A
A
Frey
J
J
Perier
C
C
D000578:Amidines / Q000494:pharmacology; D000818:Animals; D001120:Arginine / Q000031:analogs & derivatives* / Q000032:analysis; D002417:Cattle; D024042:Collagen Type I / Q000737:chemistry* / Q000378:metabolism*; D017127:Glycation End Products, Advanced / Q000032:analysis*; D006031:Glycosylation; D008239:Lysine / Q000031:analogs & derivatives* / Q000032:analysis; D012995:Solubility
D000578:Amidines; D024042:Collagen Type I; D017127:Glycation End Products, Advanced; C048496:N(6)-carboxymethyllysine; C046728:2,2'-azobis(2-amidinopropane); D001120:Arginine; C062187:pentosidine; D008239:Lysine