ArticleThe Journal of biological chemistry2010
Altered chaperone-like activity of alpha-crystallins promotes cataractogenesis.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- The Mammalian Ocular Lens in Focus: Development, Anatomy, Physiology, Transparency, Biomechanics, and Age-related Challenges.Journal of visualized experiments : JoVE · 2026Review
- Periaxin gene variants are linked to age-related cataracts in Cx46 deficient lenses.Communications biology · 2025Article
- Oxysterol Compounds in Mouse Mutant αA- and αB-Crystallin Lenses Can Improve the Optical Properties of the Lens.Investigative ophthalmology & visual science · 2022Article
- Cataract-causing allele in CRYAA (Y118D) proceeds through endoplasmic reticulum stress in mouse model.Zoological research · 2021Article
- Mechanism of Action of VP1-001 in cryAB(R120G)-Associated and Age-Related Cataracts.Investigative ophthalmology & visual science · 2019Article
- Hypericin-mediated photooxidative damage of α-crystallin in human lens epithelial cells.Free radical biology & medicine · 2013Article
- Age-dependent racemization of serine residues in a human chaperone protein.Protein science : a publication of the Protein Society · 2013Article
- Novel roles for α-crystallins in retinal function and disease.Progress in retinal and eye research · 2012Review
- Oligomerization with wt αA- and αB-crystallins reduces proteasome-mediated degradation of C-terminally truncated αA-crystallin.Investigative ophthalmology & visual science · 2012Article
- Functional validation of hydrophobic adaptation to physiological temperature in the small heat shock protein αA-crystallin.PloS one · 2012Article
- Structural and functional properties of NH(2)-terminal domain, core domain, and COOH-terminal extension of αA- and αB-crystallins.Molecular vision · 2011Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Despite the enormous number of studies demonstrating changes in the chaperone-like activity of α-crystallins in vitro, little is known about how these changes influence life-long lens transparency in vivo. Using the γB-crystallin I4F mutant protein as a target for αA-crystallins, we examined how cataract phenotypes are modulated by interactions between α-crystallins with altered chaperone-like activities and γB-I4F proteins in vivo. Double heterozygous α-crystallin knock-out αA(+/-) αB(+/-) mice with a decreased amount of α-crystallins were used to simulate reduced total α-crystallin chaperone-like activity in vivo. We found that triple heterozygous αA(+/-) αB(+/-) γB(I4F/+) mice developed more severe whole cataracts than heterozygous γB(I4F/+) mice. Thus, total chaperone-like activity of α-crystallins is important for maintaining lens transparency. We further tested whether mutant αA-crystallin Y118D proteins with increased chaperone-like activity influenced the whole cataract caused by the γB-I4F mutation. Unexpectedly, compound αA(Y118D/+) γB(I4F/+) mutant lenses displayed severe nuclear cataracts, whereas the lens cortex remained unaffected. Thus, the synergistic effect of αA-Y118D and γB-I4F mutant proteins is detrimental to the transparency only in the lens core. α-Crystallins with different chaperone-like activities are likely required in the lens cortex and nucleus for maintaining transparency.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.