Carnosine disaggregates glycated alpha-crystallin: an in vitro study.

@article{Seidler2004CarnosineDG,
  title={Carnosine disaggregates glycated alpha-crystallin: an in vitro study.},
  author={Norbert W. Seidler and George S Yeargans and Timothy G Morgan},
  journal={Archives of biochemistry and biophysics},
  year={2004},
  volume={427 1},
  pages={110-5}
}
Protein glycation, which promotes aggregation, involves the unwanted reaction of carbohydrate oxidation products with proteins. Glycation of lens alpha-crystallin occurs in vivo and may contribute to cataractogenesis. Anti-glycation compounds such as carnosine may be preventive, but interestingly carnosine reverses lens opacity in human trials. The mechanism for this observation may involve carnosine's ability to disaggregate glycated protein. We investigated this hypothesis using glycated… CONTINUE READING
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