Aspirin inhibits the formation of pentosidine, a cross-linking advanced glycation end product, in collagen.
Aspirin showed an inhibitory effect on the formation of pentosidine, a cross-linking advanced glycation endproduct, in collagen incubated with glucose in vitro. IC(50) was evaluated at 10mmol/l. Aspirin might act by metallic ion chelating (as did EDTA and DTPA) and by oxygen radical scavenging. Since aspirin was reported to inhibit retinopathy in diabetic dogs, it could act partly by inhibiting advanced glycation endproduct accumulation in long-lived proteins like collagens.
Urios
P
P
Grigorova-Borsos
A-M
AM
Sternberg
M
M
D001120:Arginine / Q000031:analogs & derivatives* / Q000037:antagonists & inhibitors; D001241:Aspirin / Q000494:pharmacology*; D003094:Collagen / Q000187:drug effects / Q000378:metabolism*; D003432:Cross-Linking Reagents; D005947:Glucose / Q000494:pharmacology; D017127:Glycation End Products, Advanced / Q000378:metabolism*; D006031:Glycosylation / Q000187:drug effects; D008239:Lysine / Q000031:analogs & derivatives* / Q000037:antagonists & inhibitors
D003432:Cross-Linking Reagents; D017127:Glycation End Products, Advanced; D003094:Collagen; D001120:Arginine; C062187:pentosidine; D005947:Glucose; D008239:Lysine; D001241:Aspirin