THE INHIBITION OF SUGAR-INDUCED STRUCTURAL ALTERATIONS IN COLLAGEN BYASPIRIN AND OTHER COMPOUNDS

With age human collagen demonstrates, amongst other changes, reduction s in solubility, elasticity and permeability. Many of these changes ha ve been attributed to non-enzymic glycosylation (glycation) - a sponta neous addition of sugar molecules to any protein with free amino group s. The resulting formation and accumulation of Advanced Glycation End- products, some of which may be cross-links, has been shown in both lon g- and short-lived proteins. We have shown that glycation of human cor neal and scleral collagen increases with age and that this is accompan ied by increases in cross-linking and collagen intermolecular spacing. We have now investigated several compounds that have been used to inh ibit glycation, including aspirin, and have shown that all the inhibit ors also prevent the increase in intermolecular spacing caused by glyc ation. (C) 1994 Academic Press, Inc.