ArticleBiochemical and biophysical research communications2010
Activation of the unfolded protein response by a cataract-associated αA-crystallin mutation.
Article in Biochemical and biophysical research communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 24 citations in OpenAlex.
- Crosstalk between endoplasmic reticulum stress and mitochondrial homeostasis: A new perspective on ophthalmic disease treatment.Journal of cell communication and signaling · 2026Review
- Insights on Human Small Heat Shock Proteins and Their Alterations in Diseases.Frontiers in molecular biosciences · 2022Review
- Genotype, Age, Genetic Background, and Sex Influence Epha2-Related Cataract Development in Mice.Investigative ophthalmology & visual science · 2021Article
- Creatine kinase/α-crystallin interaction functions in cataract development.Biochemistry and biophysics reports · 2020Article
- GJA8 missense mutation disrupts hemichannels and induces cell apoptosis in human lens epithelial cells.Scientific reports · 2019Article
- CHOP is dispensable for lens transparency in wild-type and connexin50 mutant mice.Molecular vision · 2019Article
- Probing the changes in gene expression due to α-crystallin mutations in mouse models of hereditary human cataract.PloS one · 2018Article
- Downregulation of Smac attenuates H2O2-induced apoptosis via endoplasmic reticulum stress in human lens epithelial cells.Medicine · 2017Article
- The Cataract-linked Mutant Connexin50D47A Causes Endoplasmic Reticulum Stress in Mouse Lenses.The Journal of biological chemistry · 2016Article
- Lens ER-stress response during cataract development in Mip-mutant mice.Biochimica et biophysica acta · 2016Article
- Autophagy and UPR in alpha-crystallin mutant knock-in mouse models of hereditary cataracts.Biochimica et biophysica acta · 2016Article
- Differential role of arginine mutations on the structure and functions of α-crystallin.Biochimica et biophysica acta · 2016Review
- Ameliorative effects of SkQ1 eye drops on cataractogenesis in senescence-accelerated OXYS rats.Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie · 2015Article
- The unfolded protein response is activated in connexin 50 mutant mouse lenses.Experimental eye research · 2012Article
- Expressions of GRP78 and Bax associate with differentiation, metastasis, and apoptosis in non-small cell lung cancer.Molecular biology reports · 2012Article
- Oligomerization with wt αA- and αB-crystallins reduces proteasome-mediated degradation of C-terminally truncated αA-crystallin.Investigative ophthalmology & visual science · 2012Article
- Endoplasmic Reticulum Stress and Unfolded Protein Response Pathways: Potential for Treating Age-related Retinal Degeneration.Journal of ophthalmic & vision research · 2012Article
- Juvenile cataract-associated mutation of solute carrier SLC16A12 impairs trafficking of the protein to the plasma membrane.Investigative ophthalmology & visual science · 2011Article
- A knock-in mouse model for the R120G mutation of αB-crystallin recapitulates human hereditary myopathy and cataracts.PloS one · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
αA-crystallin is a lens chaperone that plays an essential role in the transparency and refractive properties of the lens. Mutations in αA-crystallin have been associated with the development of hereditary cataracts. The R49C mutation of αA-crystallin (αA-R49C) was identified in a four-generation Caucasian family with hereditary cataracts. The αA-R49C protein forms larger-than-normal oligomers in the lens and has decreased solubility. This aberrant αA-R49C oligomerization suggests that protein folding is altered. However, whether activation of the unfolded protein response (UPR) occurs during crystallin mutation-induced cataract formation and whether the UPR causes cell death under these conditions is unclear. We investigated UPR activation in an in vivo mouse model of αA-R49C using immunoblot analysis of lens extracts. We found that expression of the endoplasmic reticulum (ER) chaperone, BiP, was 5-fold higher in homozygous αA-R49C lenses than in wild type lenses. Analysis of proteins typically expressed during the UPR revealed that ATF-4 and CHOP levels were also higher in homozygous lenses than in wild type lenses, while the opposite was true of ATF-6 and XBP-1. Taken together, these findings show that mutation of αA-crystallin induces activation of the UPR during cataract formation. They also suggest that the UPR is an important mediator of cell death observed in homozygous αA-R49C lenses.
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