alexa Accelerated aging of Asp 58 in αA crystallin and human cataract formation.
Ophthalmology

Ophthalmology

Journal of Clinical & Experimental Ophthalmology

Author(s): Hooi MY, Raftery MJ, Truscott RJ

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Abstract Racemisation of amino acids is one of the most abundant modifications in long-lived proteins. In this study racemisation of Asp 58 in the small heat shock protein, αA crystallin, was investigated. In normal human lenses, levels of l-isoAsp, d-isoAsp and d-Asp increased with age, such that by age 70 they accounted for approximately half of the total Asp at this site. Levels of d-isoAsp were significantly higher in all cataract lenses than age-matched normal lenses. The introduction of d-isoAsp in αA crystallin could therefore be associated with the development of cataract. Its more rapid formation in cataract lenses may represent an example of accelerated protein aging leading to a human age-related disease. Crown Copyright © 2012. Published by Elsevier Ltd. All rights reserved. This article was published in Exp Eye Res and referenced in Journal of Clinical & Experimental Ophthalmology

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