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Advanced glycation end products in human senile and diabetic cataractous lenses

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Abstract

The authors prepared water-soluble (WSF), urea-soluble (USF), alkali-soluble (ASF), sonicated (SF), sonicated insoluble (SIF) and membrane (MF) fractions of lens proteins from human senile and diabetic cataractous lenses and age-matched clear lenses. Levels of advanced glycation end products (AGEs) including carboxymethyl lysine (CML), a glycoxidation product, were determined by both non-competitive and competitive enzyme-linked immunosorbent assay (ELISA). Distribution of AGEs in the various protein fractions was ascertained by SDS-PAGE and Western blotting. An overall increase in the levels of AGEs in diabetic cataractous lenses as compared to senile cataractous lenses and clear lenses has been observed. ASF and SF , both of which originated from the urea-insoluble fraction, showed the highest levels of AGEs. However, no clear-cut differences in CML levels were seen among clear lenses and senile and diabetic cataractous lenses. AGEs were found to be distributed mostly in the high molecular aggregates in all the fractions. These data suggest that AGEs contribute to protein aggregation and subsequent insolubilization.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, Medical College of Georgia, Augusta, GA, USA

    Shamshad Zarina, Hui-Ren Zhao & Edathara Abraham

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  1. Shamshad Zarina
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  2. Hui-Ren Zhao
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  3. Edathara Abraham
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Zarina, S., Zhao, HR. & Abraham, E. Advanced glycation end products in human senile and diabetic cataractous lenses. Mol Cell Biochem 210, 29–34 (2000). https://doi.org/10.1023/A:1007015416572

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