A Proteome Map of the Zebrafish (Danio Rerio) Lens Reveals Similarities Between Zebrafish and Mammalian Crystallin Expression

Overview

Journal Mol Vis

Specialties Cell Biology
Molecular Biology
Ophthalmology

Date 2008 May 2

PMID 18449354

Citations 29

Authors

Mason Posner

Molly Hawke

Carrie Lacava

Courtney J Prince

Nicholas R Bellanco

Rebecca W Corbin

Affiliations

Soon will be listed here.

Abstract

Purpose: To 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.

Methods: Adult 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.

Results: alpha-, 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.

Conclusions: While 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.

Citing Articles

Loss of αBa-crystallin, but not αA-crystallin, increases age-related cataract in the zebrafish lens.

Posner M, Garver T, Kaye T, Brdicka S, Suttle M, Patterson B bioRxiv. 2024; .

PMID: 38260567 PMC: 10802301. DOI: 10.1101/2024.01.03.574085.

Impact of α-crystallin protein loss on zebrafish lens development.

Posner M, Murray K, Andrew B, Brdicka S, Roberts A, Franklin K Exp Eye Res. 2022; 227:109358.

PMID: 36572168 PMC: 9918708. DOI: 10.1016/j.exer.2022.109358.

Single cell transcriptomics of the developing zebrafish lens and identification of putative controllers of lens development.

Farnsworth D, Posner M, Miller A Exp Eye Res. 2021; 206:108535.

PMID: 33705730 PMC: 8092445. DOI: 10.1016/j.exer.2021.108535.

α-Crystallins in the Vertebrate Eye Lens: Complex Oligomers and Molecular Chaperones.

Sprague-Piercy M, Rocha M, Kwok A, Martin R Annu Rev Phys Chem. 2020; 72:143-163.

PMID: 33321054 PMC: 8062273. DOI: 10.1146/annurev-physchem-090419-121428.

Optical coherence elastography of cold cataract in porcine lens.

Zhang H, Wu C, Singh M, Nair A, Aglyamov S, Larin K J Biomed Opt. 2019; 24(3):1-7.

PMID: 30864348 PMC: 6444576. DOI: 10.1117/1.JBO.24.3.036004.

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