ArticleBiochemistry2013
Comparative proteomic analysis identifies age-dependent increases in the abundance of specific proteins after deletion of the small heat shock proteins αA- and αB-crystallin.
Article in Biochemistry, 2013. 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, 17 citations in OpenAlex.
- Loss of αBa-crystallin, but not αA-crystallin, increases age-related cataract in the zebrafish lens.Experimental eye research · 2024Article
- Loss of αBa-crystallin, but not αA-crystallin, increases age-related cataract in the zebrafish lens.bioRxiv : the preprint server for biology · 2024Article
- Impact of α-crystallin protein loss on zebrafish lens development.Experimental eye research · 2023Article
- α-Crystallins in the Vertebrate Eye Lens: Complex Oligomers and Molecular Chaperones.Annual review of physical chemistry · 2021Review
- Article
- Probing the changes in gene expression due to α-crystallin mutations in mouse models of hereditary human cataract.PloS one · 2018Article
- Species-Specific Structural and Functional Divergence of α-Crystallins: Zebrafish αBa- and Rodent αA(ins)-Crystallin Encode Activated Chaperones.Biochemistry · 2015Article
- Review of application of mass spectrometry for analyses of anterior eye proteome.World journal of biological chemistry · 2014Review
- Newborn mouse lens proteome and its alteration by lysine 6 mutant ubiquitin.Journal of proteome research · 2014Article
- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Mice with deletion of genes for small heat shock proteins αA- and αB-crystallin (αA/αB(-/-)) develop cataracts. We used proteomic analysis to identify lens proteins that change in abundance after deletion of these α-crystallin genes. Wild-type (WT) and αA/αB(-/-) knockout (DKO) mice were compared using two-dimensional difference gel electrophoresis and mass spectrometric analysis, and protein identifications were validated by Mascot proteomic software. The abundance of histones H2A, H4, and H2B fragment, and a low molecular weight β1-catenin increased 2-3-fold in postnatal day 2 lenses of DKO lenses compared with WT lenses. Additional major increases were observed in abundance of βB2-crystallin and vimentin in 30-day-old lenses of DKO animals compared with WT animals. Lenses of DKO mice were comprised of nine protein spots containing βB2-crystallin at 10-40-fold higher abundance and three protein spots containing vimentin at ≥2-fold higher abundance than in WT lenses. Gel permeation chromatography identified a unique 328 kDa protein in DKO lenses, containing β-crystallin, demonstrating aggregation of β-crystallin in the absence of α-crystallins. Together, these changes provide biochemical evidence for possible functions of specific cell adhesion proteins, cytoskeletal proteins, and crystallins in lens opacities caused by the absence of the major chaperones, αA- and αB-crystallins.
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