The non-enzymic glycosylation of bovine lens proteins by glucosamine and its inhibition by aspirin, ibuprofen and glutathione.
Cataract is a long-term complication of diabetes mellitus. Diabetics have increased glucosamine levels and it is possible that the non-enzymic glycosylation of the lens structural proteins by glucosamine induces conformational changes in the lens that contribute to cataract formation. Aspirin and aspirin-like analgesics may protect against glycosylation. In this paper the binding of glucosamine to bovine lens proteins and the effects of aspirin, paracetamol and ibuprofen on this reaction were investigated. Significant binding of glucosamine to the lens proteins was found. Gel-chromatography indicated that beta H-crystallin was most reactive to the amino-sugar. Of the analgesics studied, aspirin was the most effective inhibitor of glycosylation, followed by the other anti-inflammatory drug, ibuprofen. Preincubation of the lens homogenate with aspirin was no more effective at decreasing binding of glucosamine than was simultaneous incubation with aspirin. Glutathione significantly inhibited glucosamine binding. Glucosamine is active in non-enzymic glycosylation but the reaction can be inhibited by agents thought to protect against cataract.
Nuffield Laboratory of Ophthalmology, University of Oxford, U.K.
R
R
Ajiboye
J J
JJ
Harding
D000818:Animals; D001241:Aspirin / Q000494:pharmacology*; D002417:Cattle; D003459:Crystallins / Q000378:metabolism*; D005944:Glucosamine / Q000378:metabolism*; D005978:Glutathione / Q000494:pharmacology*; D006031:Glycosylation; D007052:Ibuprofen / Q000494:pharmacology*
D003459:Crystallins; D005978:Glutathione; D005944:Glucosamine; D001241:Aspirin; D007052:Ibuprofen