γ-Crystallin redox–detox in the lens

γ-Crystallin redox–detox in the lens.

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Item Type: Article
Status: Published
Official URL: https://doi.org/10.1074/jbc.H118.006240
Journal or Publication Title: Journal of Biological Chemistry
Volume: 293
Number: 46
Page Range: pp. 18010-18011
Date: 2018
Divisions: ACRF Centenary Cancer Research Centre
Depositing User: General Admin
Identification Number: 10.1074/jbc.H118.006240
ISSN: 0021-9258
Date Deposited: 04 Jan 2021 23:07
Abstract:

In the vertebrate eye, limiting oxidation of proteins and lipids is key to maintaining lens function and avoiding cataract formation. A study by Serebryany et al. 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.

Creators:
Creators
Email
Quinlan, Roy A.
UNSPECIFIED
Hogg, Philip J.
UNSPECIFIED
Last Modified: 04 Jan 2021 23:07
URI: https://eprints.centenary.org.au/id/eprint/594

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