Accelerated aging of Asp 58 in aA crystallin and human cataract formation

Authors

Michelle Yu Sung Hooi, University Of Sydney
Mark Raftery, University Of New South Wales
Roger J. Truscott, University of WollongongFollow

RIS ID

73418

Publication Details

Hooi, M. Yu Sung., Raftery, M. & Truscott, R. J. (2013). Accelerated aging of Asp 58 in αA crystallin and human cataract formation. Experimental Eye Research, 106 34-39.

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.