ArticleInvestigative ophthalmology & visual science2009
Mechanism of cataract formation in alphaA-crystallin Y118D mutation.
Article in Investigative ophthalmology & visual science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Crosstalk between endoplasmic reticulum stress and mitochondrial homeostasis: A new perspective on ophthalmic disease treatment.Journal of cell communication and signaling · 2026Review
- Reversible cold-induced lens opacity in a hibernator reveals a molecular target for treating cataracts.The Journal of clinical investigation · 2024Article
- Refolding Increases the Chaperone-like Activity of αInternational journal of molecular sciences · 2023Article
- Association of alkaptonuria and low dose nitisinone therapy with cataract formation in a large cohort of patients.JIMD reports · 2022Article
- Cataract-causing allele in CRYAA (Y118D) proceeds through endoplasmic reticulum stress in mouse model.Zoological research · 2021Article
- Article
- p62 expression and autophagy in αB-crystallin R120G mutant knock-in mouse model of hereditary cataract.Experimental eye research · 2013Article
- Age-dependent racemization of serine residues in a human chaperone protein.Protein science : a publication of the Protein Society · 2013Article
- Patterns of gene expression in microarrays and expressed sequence tags from normal and cataractous lenses.Human genomics · 2012Article
- Altered chaperone-like activity of alpha-crystallins promotes cataractogenesis.The Journal of biological chemistry · 2010Article
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7 authors.
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Abstract
purposeThe aim of this study was to elucidate the molecular mechanisms that lead to a dominant nuclear cataract in a mouse harboring the Y118D mutation in the alphaA-crystallin gene.
methodsThe physicochemical properties of alpha-crystallin obtained from mouse lenses with the Y118D mutation as well as a recombinant Y118D alphaA-crystallin were studied using gel filtration, two-dimensional (2D) gel electrophoresis, multi-angle light scattering, circular dichroism, fluorescence, and chaperone activities.
resultsBoth native alpha-crystallin from mutant lens and recombinant alphaA-Y118D displayed higher molecular mass distribution than the wild-type. Circular dichroism spectra indicated changes in the secondary structures of alphaA-Y118D. The alphaA-Y118D protein prevented nonspecific protein aggregation more effectively than wild-type alphaA-crystallin. The gel filtration and 2D gel electrophoresis analysis showed a significant reduction of Y118D mutant protein in comparison with wild-type alphaA protein of heterozygous mutant lenses. Quantitative RT-PCR results confirmed a decrease in alphaA and alphaB transcripts in the homozygous mutant alpha A(Y118D/Y118D) lenses.
conclusionsThe alphaA-Y118D mutant protein itself displays an increased chaperone-like activity. However, the dominant nuclear cataract is associated with a significant decrease in the amount of alphaA-crystallin, leading to a reduction in total chaperone capacity needed for maintaining lens transparency.
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