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Department of Biochemistry, Faculty of Pharmaceutical Sciences, Meijo University, Nagoya, Japan.
To study the contribution of glycation or the Maillard reaction to the spontaneous coloration of human crystalline lens in aging, we determined 1-deoxyfructosyl adduct and the fluorescent material, which are produced in the early stage of glycation, in the proteins of normal and colored human lenses of different ages. The amount of both glycation products in the lens increased significantly in proportion to aging or the advance of lens coloration. The insolubility of lens protein also increased with the advance of glycation. In addition, the present study showed that glucose and glucose-6-phosphate have higher reactivities with human lens protein than fructose and glucose-1-phosphate. This paper demonstrates that the deeper colored or older aged lens contains larger amounts of glycation products, and that glycation between lens protein and various sugars in vivo may be a serious factor in human lens coloration or insolubilization of lens protein.
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