Glycation-induced crosslinking of calf lens crystallins.
To investigate the possible role of glycation in the onset of diabetic cataract we used calf lens crystallins as a model. After incubation with reducing sugars, the proteins were investigated by high-pressure gel permeation chromatography, SDS-PAGE and analytical ultracentrifugation. Glucose-6-phosphate incubation resulted in an increase in mean molecular weight of all crystallin fractions and the occurrence of high-molecular weight material, partly formed by disulphide bonds. The glycated crystallins showed a decrease of tryptophan fluorescence and an increase of a specific non-tryptophan fluorescence. This fluorescence was, however, not exclusively associated with the high molecular weight protein, but was present in all protein fractions.
van Boekel
M A
MA
Department of Biochemistry, University of Nijmegen, The Netherlands.
Hoenders
H J
HJ
D000818:Animals; D002386:Cataract / Q000209:etiology*; D002417:Cattle; D002850:Chromatography, Gel; D003459:Crystallins / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005690:Galactose / Q000494:pharmacology; D005947:Glucose / Q000494:pharmacology; D019298:Glucose-6-Phosphate; D005958:Glucosephosphates / Q000494:pharmacology; D006031:Glycosylation; D066298:In Vitro Techniques; D008970:Molecular Weight; D011489:Protein Denaturation
D003459:Crystallins; D005958:Glucosephosphates; D019298:Glucose-6-Phosphate; D005947:Glucose; D005690:Galactose