ArticleThe FEBS journal2006
Gene duplication and separation of functions in alphaB-crystallin from zebrafish (Danio rerio).
Article in The FEBS journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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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
25 citing papers in PubMed, 46 citations in OpenAlex.
- Contributions of aquatic organisms to understanding the vertebrate ocular lens.Frontiers in ophthalmology · 2026Review
- Zebrafish as a model for crystallin-associated congenital cataracts in humans.Frontiers in cell and developmental biology · 2025Review
- Zebrafish: unraveling genetic complexity through duplicated genes.Development genes and evolution · 2024Review
- 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
- The generation and characterization of a transgenic zebrafish line with lens-specific Cre expression.Molecular vision · 2024Article
- Impact of α-crystallin protein loss on zebrafish lens development.Experimental eye research · 2023Article
- Interplay between Nrf2 and αB-crystallin in the lens and heart of zebrafish under proteostatic stress.Frontiers in molecular biosciences · 2023Article
- Single cell transcriptomics of the developing zebrafish lens and identification of putative controllers of lens development.Experimental eye research · 2021Article
- α-Crystallins in the Vertebrate Eye Lens: Complex Oligomers and Molecular Chaperones.Annual review of physical chemistry · 2021Review
- Article
- Species-Specific Structural and Functional Divergence of α-Crystallins: Zebrafish αBa- and Rodent αA(ins)-Crystallin Encode Activated Chaperones.Biochemistry · 2015Article
- A conserved role of αA-crystallin in the development of the zebrafish embryonic lens.Experimental eye research · 2015Article
- Loss of the small heat shock protein αA-crystallin does not lead to detectable defects in early zebrafish lens development.Experimental eye research · 2013Article
- Evolution of crystallins for a role in the vertebrate eye lens.Protein science : a publication of the Protein Society · 2013Review
- Changes in zebrafish (Danio rerio) lens crystallin content during development.Molecular vision · 2013Article
- Comparative proteomics analysis of degenerative eye lenses of nocturnal rice eel and catfish as compared to diurnal zebrafish.Molecular vision · 2013Article
- Functional validation of hydrophobic adaptation to physiological temperature in the small heat shock protein αA-crystallin.PloS one · 2012Article
- Structure/function studies of dogfish alpha-crystallin, comparison with bovine alpha-crystallin.Molecular vision · 2009Article
- The zebrafish lens proteome during development and aging.Molecular vision · 2009Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
We previously reported that zebrafish alphaB-crystallin is not constitutively expressed in nervous or muscular tissue and has reduced chaperone-like activity compared with its human ortholog. Here we characterize the tissue expression pattern and chaperone-like activity of a second zebrafish alphaB-crystallin. Expressed sequence tag analysis of adult zebrafish lens revealed the presence of a novel alpha-crystallin transcript designated cryab2 and the resulting protein alphaB2-crystallin. The deduced protein sequence was 58.2% and 50.3% identical with human alphaB-crystallin and zebrafish alphaB1-crystallin, respectively. RT-PCR showed that alphaB2-crystallin is expressed predominantly in lens but, reminiscent of mammalian alphaB-crystallin, also has lower constitutive expression in heart, brain, skeletal muscle and liver. The chaperone-like activity of purified recombinant alphaB2 protein was assayed by measuring its ability to prevent the chemically induced aggregation of alpha-lactalbumin and lysozyme. At 25 degrees C and 30 degrees C, zebrafish alphaB2 showed greater chaperone-like activity than human alphaB-crystallin, and at 35 degrees C and 40 degrees C, the human protein provided greater protection against aggregation. 2D gel electrophoresis indicated that alphaB2-crystallin makes up approximately 0.16% of total zebrafish lens protein. Zebrafish is the first species known to express two different alphaB-crystallins. Differences in primary structure, expression and chaperone-like activity suggest that the two zebrafish alphaB-crystallins perform divergent physiological roles. After gene duplication, zebrafish alphaB2 maintained the widespread protective role also found in mammalian alphaB-crystallin, while zebrafish alphaB1 adopted a more restricted, nonchaperone role in the lens. Gene duplication may have allowed these functions to separate, providing a unique model for studying structure-function relationships and the regulation of tissue-specific expression patterns.
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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.