Accelerated aging of Asp 58 in alpha A crystallin and human cataract formation

作者：Hooi Michelle Y S; Raftery Mark J; Truscott Roger J W^*

来源：Experimental Eye Research, 2013, 106: 34-39.

DOI：10.1016/j.exer.2012.10.013

• human age-related cataract
• posttranslational modification
• blindness
• protein denaturation
• racemisation

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, alpha A 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 aA 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.

• 出版日期2013-1