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γ-Crystallin redox-detox in the lens.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2018 Nov 16; Vol. 293 (46), pp. 18010-18011. - Publication Year :
- 2018
-
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.<br /> (© 2018 Quinlan and Hogg.)
- Subjects :
- Amino Acid Substitution
Cataract physiopathology
Cysteine chemistry
Humans
Mutation
Oxidation-Reduction
Oxidoreductases Acting on Sulfur Group Donors genetics
gamma-Crystallins genetics
Disulfides metabolism
Lens, Crystalline metabolism
Oxidoreductases Acting on Sulfur Group Donors metabolism
gamma-Crystallins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1083-351X
- Volume :
- 293
- Issue :
- 46
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 30446601
- Full Text :
- https://doi.org/10.1074/jbc.H118.006240