Ray Nicholas J
Research School of Chemistry, The Australian National University, Building 137, Sullivans Creek Road, Canberra, Australia.
Biophys Rev. 2015 Dec;7(4):353-368. doi: 10.1007/s12551-015-0176-4. Epub 2015 Aug 23.
This review examines both recent and historical literature related to the biophysical chemistry of the proteins in the ageing eye, with a particular focus on cataract development. The lens is a vital component of the eye, acting as an optical focusing device to form clear images on the retina. The lens maintains the necessary high transparency and refractive index by expressing crystallin proteins in high concentration and eliminating all large cellular structures that may cause light scattering. This has the consequence of eliminating lens fibre cell metabolism and results in mature lens fibre cells having no mechanism for protein expression and a complete absence of protein recycling or turnover. As a result, the crystallins are some of the oldest proteins in the human body. Lack of protein repair or recycling means the lens tends to accumulate damage with age in the form of protein post-translational modifications. The crystallins can be subject to a wide range of age-related changes, including isomerisation, deamidation and racemisation. Many of these modification are highly correlated with cataract formation and represent a biochemical mechanism for age-related blindness.
本综述研究了与衰老眼睛中蛋白质生物物理化学相关的近期和历史文献，特别关注白内障的形成。晶状体是眼睛的重要组成部分，作为一种光学聚焦装置，在视网膜上形成清晰的图像。晶状体通过高浓度表达晶状体蛋白并消除所有可能导致光散射的大细胞结构，维持必要的高透明度和折射率。这导致晶状体纤维细胞代谢被消除，成熟的晶状体纤维细胞没有蛋白质表达机制，并且完全没有蛋白质回收或周转。因此，晶状体蛋白是人体中最古老的一些蛋白质。缺乏蛋白质修复或回收意味着晶状体随着年龄增长往往会以蛋白质翻译后修饰的形式积累损伤。晶状体蛋白会经历多种与年龄相关的变化，包括异构化、脱酰胺化和消旋化。其中许多修饰与白内障形成高度相关，代表了与年龄相关失明的生化机制。
