Journal
SCIENCE
Volume 350, Issue 6261, Pages 674-677Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aac9145
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Funding
- NIH [EY017370, EY05681, EY02687, UL1RR024986, GM007767]
- American Foundation for Pharmaceutical Education
- Research to Prevent Blindness
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Cataracts reduce vision in 50% of individuals over 70 years of age and are a common form of blindness worldwide. Cataracts are caused when damage to the major lens crystallin proteins causes their misfolding and aggregation into insoluble amyloids. Using a thermal stability assay, we identified a class of molecules that bind alpha-crystallins (cryAA and cryAB) and reversed their aggregation in vitro. The most promising compound improved lens transparency in the R49C cryAA and R120G cryAB mouse models of hereditary cataract. It also partially restored protein solubility in the lenses of aged mice in vivo and in human lenses ex vivo. These findings suggest an approach to treating cataracts by stabilizing alpha-crystallins.
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