Skip to content

Aspirin inhibits the formation of pentosidine, a cross-linking advanced glycation end product, in collagen

by P. Urios, A. M. Grigorova-Borsos, M. Sternberg
Diabetes Research and Clinical Practice ()
Get full text at journal


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. © 2007 Elsevier Ireland Ltd. All rights reserved.

Cite this document (BETA)

Readership Statistics

10 Readers on Mendeley
by Discipline
60% Agricultural and Biological Sciences
30% Medicine and Dentistry
10% Nursing and Health Professions
by Academic Status
40% Student > Ph. D. Student
20% Researcher
20% Student > Master

Sign up today - FREE

Mendeley saves you time finding and organizing research. Learn more

  • All your research in one place
  • Add and import papers easily
  • Access it anywhere, anytime

Start using Mendeley in seconds!

Sign up & Download

Already have an account? Sign in