晶状体蛋白的翻译后修饰

Research on post-translational modification of crystallins in lens

晶状体蛋白(α-、β-、γ-晶状体蛋白)可发生翻译后修饰,且在不同的位点发生不同类型的翻译后修饰,从而影响晶状体蛋白的功能。部分翻译后修饰不仅增加晶状体蛋白的不溶性,也改变晶状体蛋白的构象,最终促进白内障的形成;有些翻译后修饰则与白内障的形成无关,可能与晶状体蛋白的发育或保护作用有关。研究晶状体蛋白的翻译后修饰及调控,对深入了解晶状体发育、衰老、白内障形成等过程有重要意义。就其在蛋白质水平上阐明有关晶状体的生理及病理过程进行综述。

Stability and regular assembly of lens protein contribute to lens integrity and transparency. Post-translational modification of lens proteins, including α-, β- and γ-erystallins, were found in various types, which have been suspected to have an influence on lens functions. Some types of post-translational modifications cause accumulation of insoluble aggregates and cross-linked products of α-, β- and γ-erystallins and transformation of conformation of erystallins, leading to cataract formation. On the other hand, some types of post-translational modifications seem to have no influence on cataract formation, and these post-translational modifications are intimately related to erystallins development or erystallins protection. It is important to investigate the mechanism and regulation of post-translational modifications of crystallins for the study of process of lens development, senescence and cataract formation and the clarification of biological and pathological essence of lens on protein level.