Comparison of post-translational modifications of alpha A-crystallin from normal and hereditary cataract rats |
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| Authors: | N. Fujii N. Takeuchi N. Fujii T. Tezuka K. Kuge T. Takata A. Kamei T. Saito |
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| Affiliation: | (1) Research Reactor, Institute, Kyoto University, Kumatori, Sennan, Osaka, Japan;(2) Section of Biochemistry, Faculty of Pharmacy, Meijo University, Yagotoyama, Tempaku-ku, Nagoya, Japan |
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| Abstract: | Summary. In order to investigate the relationship between lens opacities and the various modifications of lens proteins, we analyzed and compared the properties of lens proteins of 85-day old normal Wistar rats and the hereditary cataract model, ICR/f rats. The present study identified many differences between normal and mutant lens proteins. In the ICR/f mutant rats, the relative amounts of gamma-crystallin decreased and high molecular weight (HMW) protein increased. Racemization and isomerization of Asp-151 of alpha A-crystallin was observed in the mutant ICR/f rats, and Met-1 of alpha A-crystallin was oxidized to methionine sulfoxide. These modifications were not found in the age-matched normal rats. These tendencies are consistent with aged and cataractous human lenses. |
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| Keywords: | : Aging – Alpha A-crystallin – Cataract – Isomerization – Oxidation – Racemization |
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