Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2798701 | Diabetes Research and Clinical Practice | 2007 | 4 Pages |
Abstract
Aspirin showed an inhibitory effect on the formation of pentosidine, a cross-linking advanced glycation endproduct, in collagen incubated with glucose in vitro. IC50 was evaluated at 10 mmol/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.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Endocrinology
Authors
P. Urios, A.-M. Grigorova-Borsos, M. Sternberg,