ArticleMolecular vision2008
A proteome map of the zebrafish (Danio rerio) lens reveals similarities between zebrafish and mammalian crystallin expression.
Article in Molecular vision, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
36 citing papers in PubMed, 48 citations in OpenAlex.
- Toxicoproteomic analysis reveals arsenic-induced alterations in eye lens proteins of Labeo rohita.Fish physiology and biochemistry · 2026Article
- Article
- Article
- Contributions of aquatic organisms to understanding the vertebrate ocular lens.Frontiers in ophthalmology · 2026Review
- Data-Independent Acquisition Parallel Accumulation-Serial Fragmentation (diaPASEF) Analysis of the Separated Zebrafish Lens Improves Identifications.Journal of the American Society for Mass Spectrometry · 2025Article
- Zebrafish as a model for crystallin-associated congenital cataracts in humans.Frontiers in cell and developmental biology · 2025Review
- 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
- 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
- Optical coherence elastography of cold cataract in porcine lens.Journal of biomedical optics · 2019Article
- Why does the zebrafish cloche mutant develop lens cataract?PloS one · 2019Article
- Transgenic zebrafish models reveal distinct molecular mechanisms for cataract-linked αA-crystallin mutants.PloS one · 2018Article
- The occhiolino (occ) mutant Zebrafish, a model for development of the optical function in the biological lens.Developmental dynamics : an official publication of the American Association of Anatomists · 2017Article
- Article
- The developmental effects of pentachlorophenol on zebrafish embryos during segmentation: A systematic view.Scientific reports · 2016Article
- Comprehensive and quantitative proteomic analyses of zebrafish plasma reveals conserved protein profiles between genders and between zebrafish and human.Scientific reports · 2016Article
- 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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
purposeTo characterize the crystallin content of the zebrafish lens using two-dimensional gel electrophoresis (2-DE). These data will facilitate future investigations of vertebrate lens development, function, and disease.
methodsAdult zebrafish lens proteins were separated by 2-DE, and the resulting spots were identified by matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS). The relative proportion of each crystallin was quantified by image analysis, and phosphospecific staining was used to identify phosphorylated alpha-crystallins. The proportion of each crystallin in the soluble and insoluble fraction of the lens was also determined by resolving these lens fractions separately by 2-DE.
resultsalpha-, beta-, and gamma-crystallins comprised 7.8, 36.0, and 47.2% of the zebrafish lens, respectively. While the alpha-crystallin content of the zebrafish lens is less than the amounts found in the human lens, the ratio of alphaA:alphaB crystallin is very similar. The phosphorylation pattern of zebrafish alphaA-crystallins was also similar to that of humans. The most abundant gamma-crystallins were the diverse gammaMs, comprising 30.5% of the lens. Intact zebrafish crystallins were generally more common in the soluble fraction with truncated versions more common in the insoluble fraction.
conclusionsWhile the total alpha- and gamma-crystallin content of the zebrafish lens differs from that of humans, similarities in alpha-crystallin ratios and modifications and a link between crystallin truncation and insolubility suggest that the zebrafish is a suitable model for the vertebrate lens. The proteome map provided here will be of value to future studies of lens development, function, and disease.
Indexed as
Identifiers
18449354PMC2358921W2139298045What OpenQuestion holds
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.