From the Department of Biosciences, University of Durham, Mountjoy Science Site, Durham DH13LE, United Kingdom.
Centenary Institute, NHMRC Clinical Trials Center, Sydney Medical School, University of Sydney, NSW 2006, Australia.
J Biol Chem. 2018 Nov 16;293(46):18010-18011. doi: 10.1074/jbc.H118.006240.
In the vertebrate eye, limiting oxidation of proteins and lipids is key to maintaining lens function and avoiding cataract formation. A study by Serebryany identifies a surprising contributor to the eye's oxidative defense in their demonstration that γD-crystallin (HγD) functions as an oxidoreductase and uses disulfide exchange to initiate aggregation of mutant crystallins that mimic oxidative damage. These insights suggest a mechanism by which a dynamic pool of closely packed proteins might avoid oxidation-driven protein-folding traps, providing new avenues to understand the basis of a human disease with global impact.
在脊椎动物的眼睛中，限制蛋白质和脂质的氧化对于维持晶状体功能和避免白内障形成至关重要。 Serebryany 的一项研究表明，γD-晶体蛋白 (HγD) 作为一种氧化还原酶发挥作用，并通过二硫键交换启动模拟氧化损伤的突变晶体蛋白的聚集，这为眼睛的氧化防御提供了一个令人惊讶的贡献因素。这些发现提示了一种机制，即通过一个紧密堆积的蛋白质动态库，可能避免氧化驱动的蛋白质折叠陷阱，为理解具有全球影响的人类疾病的基础提供了新的途径。
