ArticleProceedings of the National Academy of Sciences of the United States of America1997
Targeted disruption of the mouse alpha A-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein alpha B-crystallin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
122 citing papers in PubMed, 1 synthesis or guideline pooled it, 336 citations in OpenAlex.
- Pooled it
- Review
- Contributions of aquatic organisms to understanding the vertebrate ocular lens.Frontiers in ophthalmology · 2026Review
- Analysis of mouse lens morphological and proteomic abnormalities following deletion of the βB3-crystallin promoter.Experimental eye research · 2025Article
- Cataract induction in an arthropod reveals how lens crystallins contribute to the formation of biological glass.PloS one · 2025Article
- HSPB4/CRYAA Protect Photoreceptors during Retinal Detachment in Part through FAIM2 Regulation.Neurology international · 2024Article
- Loss of αBa-crystallin, but not αA-crystallin, increases age-related cataract in the zebrafish lens.Experimental eye research · 2024Article
- Aqueous humor perturbations in chronic smokers: a proteomic study.Scientific reports · 2024Article
- Loss of αBa-crystallin, but not αA-crystallin, increases age-related cataract in the zebrafish lens.bioRxiv : the preprint server for biology · 2024Article
- Study of The Molecular Nature of Congenital Cataracts in Patients from The Volga-Ural Region.Current issues in molecular biology · 2023Article
- Expression of αA-crystallin (CRYAA)Aging · 2023Article
- Impact of α-crystallin protein loss on zebrafish lens development.Experimental eye research · 2023Article
- BMP3 is a novel locus involved in the causality of ocular coloboma.Human genetics · 2022Article
- Insights on Human Small Heat Shock Proteins and Their Alterations in Diseases.Frontiers in molecular biosciences · 2022Review
- Structural and functional analysis of SNP rs76740365 G>A in exon-3 of the alpha A-crystallin gene in lens epithelial cells.Molecular vision · 2022Article
- Loss of αA or αB-Crystallin Accelerates Photoreceptor Cell Death in a Mouse Model of P23H Autosomal Dominant Retinitis Pigmentosa.International journal of molecular sciences · 2021Article
- Inherited cataracts: Genetic mechanisms and pathways new and old.Experimental eye research · 2021Review
- HspB4/αA-Crystallin Modulates Neuroinflammation in the Retina via the Stress-Specific Inflammatory Pathways.Journal of clinical medicine · 2021Article
- The multifaceted nature of αB-crystallin.Cell stress & chaperones · 2020Review
- c-MAF deletion in adult C57BL/6J mice induces cataract formation and abnormal differentiation of lens fiber cells.Experimental animals · 2020Article
62 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
alpha A-crystallin (alpha A) and alpha B-crystallin (alpha B) are among the predominant proteins of the vertebrate eye lens. In vitro, the alpha-crystallins, which are isolated together as a high molecular mass aggregate, exhibit a number of properties, the most interesting of which is their ability to function as molecular chaperones for other proteins. Here we begin to examine the in vivo functions of alpha-crystallin by generating mice with a targeted disruption of the alpha A gene. Mice that are homozygous for the disrupted allele produce no detectable alpha A in their lenses, based on protein gel electrophoresis and immunoblot analysis. Initially, the alpha A-deficient lenses appear structurally normal, but they are smaller than the lenses of wild-type littermates. alpha A-/- lenses develop an opacification that starts in the nucleus and progresses to a general opacification with age. Light and transmission electron microscopy reveal the presence of dense inclusion bodies in the central lens fiber cells. The inclusions react strongly with antibodies to alpha B but not significantly with antibodies to beta- or gamma-crystallins. In addition, immunoblot analyses demonstrate that a significant portion of the alpha B in alpha A-/- lenses shifts into the insoluble fraction. These studies suggest that alpha A is essential for maintaining lens transparency, possibly by ensuring that alpha B or proteins closely associated with this small heat shock protein remain soluble.
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