期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1784, 期 12, 页码 1959-1964出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2008.07.016
关键词
Cataract; Oxidation; Cysteine; Disulphide; Label-free quantification; Mass spectrometry
资金
- National Institute of Health [RO1EY013570-03]
- National Health and Medical Research Council
Loss of protein thiols is a key feature associated with the onset of age-related nuclear cataract (ARNC), however, little is known about the specific sites of oxidation of the crystallins. We investigated cysteine residues in ARNC lenses and compared them with age-matched normal lenses. Proteomic analysis of tryptic digests revealed ten cysteine residues in older normal lenses that showed no significant oxidation compared to foetal counterparts (Cys 170 in beta A1/3-crystallin, Cys 32 in beta A4-crystallin, Cys 79 in beta B1-crystallin, Cys 22, Cys 78/79, C153 in gamma C-crystallin and Cys 22, Cys 24 and Cys 26 in gamma S-crystallin). Although these thiols were not oxidised in normal lenses past the 6th decade, they were present largely as disulphides in the ARNC lenses. By contrast, two cysteine residues, Cys 41 in gamma C-crystallin and Cys 18 in gamma D-crystallin, were not oxidised, even in advanced ARNC lenses. These cysteines are buried deep within the protein and any unfolding associated with cataract must be insufficient to expose them to the oxidative environment present in the centre of advanced ARNC lenses. The vast majority of the loss of protein thiol observed in such lenses is due to disulphide bond formation. Crown Copyright (c) 2008 Published by Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据