Takemoto L, Boyle D
Division of Biology, Kansas State University, Manhattan 66506, USA.
Int J Biol Macromol. 1998 May-Jun;22(3-4):331-7. doi: 10.1016/s0141-8130(98)00031-2.
alpha-Crystallins possess molecular chaperone properties and are one of the most abundant of the lenticular proteins. Posttranslational modifications of these proteins have been implicated as a possible etiology of human cataracts. This article will review current knowledge concerning the effects of known posttranslational modifications upon the molecular chaperone properties and aggregation behavior of alpha-A and alpha-B crystallin. Based upon these effects, experimental approaches will be discussed that may be useful in the development of reagents that may selectively inhibit the cataractogenic process in the aging human lens.
α-晶状体蛋白具有分子伴侣特性,是晶状体中含量最为丰富的蛋白质之一。这些蛋白质的翻译后修饰被认为可能是人类白内障的病因之一。本文将综述有关已知翻译后修饰对α-A和α-B晶状体蛋白分子伴侣特性及聚集行为影响的现有知识。基于这些影响,将讨论一些实验方法,这些方法可能有助于开发能够选择性抑制老化人晶状体中致白内障过程的试剂。