期刊
FEBS LETTERS
卷 579, 期 30, 页码 6745-6748出版社
WILEY
DOI: 10.1016/j.febslet.2005.11.004
关键词
human lens; aquaporin 0 (AQP0); post-translation modifications; calpains
资金
- NEI NIH HHS [EY05786] Funding Source: Medline
Opacities (cataracts) in the lens of the eye are a leading cause of preventable blindness. Aquaporins function as water channels, and the C-terminus is postulated as a regulatory domain. The C-terminal domain of aquaporin 0 (AQP0) develops numerous truncation sites during lens aging. The purpose of the present experiment was to determine if the calcium-activated protease m-calpain (EC 3.4.22.17) was responsible for truncation of human AQP0. AQP0 was isolated from young human donors, incubated with recombinant m-calpain, and the cleavage sites on the released peptides; were determined by on-line electrospray ionization mass spectrometry. We found that four cleavage sites on human AQP0 could be tentatively assigned to in-calpain. This is the first evidence for possible calpain activity in human lens. Because the cause(s) of 17 other cleavage sites was unknown, the data also suggested that other, as yet unknown, proteases or non-enzymatic mechanisms are more active than calpain in human lens. (c) 2005 Federation of European Biochemical Societies. 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