The nuclear region of the lens is metabolically quiescent, but it is far from inert chemically. Without cellular renewal and with decades of environmental exposures, the lens proteome, lipidome, and metabolome change. The lens crystallins have evolved exquisite mechanisms for resisting, slowing, adapting to, and perhaps even harnessing the effects of these cumulative chemical modifications to minimize the amount of light-scattering aggregation in the lens over a lifetime. Redox chemistry is a major factor in these damages and mitigating adaptations, and as such, it is likely to be a key component of any successful therapeutic strategy for preserving or rescuing lens transparency, and perhaps flexibility, during aging. Protein redox chemistry is typically mediated by Cys residues. This review will therefore focus primarily on the Cys-rich γ-crystallins of the human lens, taking care to extend these findings to the β- and α-crystallins where pertinent.

晶状体的核区域在代谢上是静止的，但在化学上却远非惰性。如果没有细胞更新，并且经过数十年的环境暴露，晶状体蛋白质组、脂质组和代谢组会发生变化。晶状体蛋白已经进化出精致的机制来抵抗、减缓、适应，甚至可能利用这些累积的化学修饰的影响，以最大限度地减少晶状体在一生中光散射聚集的数量。氧化还原化学是这些损害和减轻适应的主要因素，因此，它可能是任何成功的治疗策略的关键组成部分，以在老化过程中保持或挽救晶状体透明度，也许还有灵活性。蛋白质氧化还原化学通常由半胱氨酸残基介导。因此，本综述将主要关注人类晶状体中富含半胱氨酸的 γ-晶状体蛋白，并注意将这些发现扩展到相关的 β-和 α-晶状体蛋白。