The inhibition of sugar-induced structural alterations in collagen by aspirin and other compounds.

Abstract:

:With age human collagen demonstrates, amongst other changes, reductions in solubility, elasticity and permeability. Many of these changes have been attributed to non-enzymic glycosylation (glycation)-a spontaneous addition of sugar molecules to any protein with free amino groups. The resulting formation and accumulation of Advanced Glycation End-products, some of which may be cross-links, has been shown in both long- and short-lived proteins. We have shown that glycation of human corneal and scleral collagen increases with age and that this is accompanied by increases in cross-linking and collagen intermolecular spacing. We have now investigated several compounds that have been used to inhibit glycation, including aspirin, and have shown that all the inhibitors also prevent the increase in intermolecular spacing caused by glycation.

authors

Malik NS,Meek KM

doi

10.1006/bbrc.1994.1282

subject

Has Abstract

pub_date

1994-03-15 00:00:00

pages

683-6

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(84)71282-4

journal_volume

199

pub_type

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