ZFIN ID: ZDB-PUB-080506-3
A proteome map of the zebrafish (Danio rerio) lens reveals similarities between zebrafish and mammalian crystallin expression
Posner, M., Hawke, M., Lacava, C., Prince, C.J., Bellanco, N.R., and Corbin, R.W.
Date: 2008
Source: Molecular Vision   14: 806-814 (Journal)
Registered Authors: Posner, Mason
Keywords: none
MeSH Terms:
  • Animals
  • Crystallins/metabolism*
  • Densitometry
  • Electrophoresis, Gel, Two-Dimensional
  • Gene Expression Regulation*
  • Humans
  • Lens, Crystalline/chemistry*
  • Mutant Proteins/metabolism
  • Phosphoproteins/metabolism
  • Proteome/analysis*
  • Sequence Homology, Amino Acid
  • Solubility
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Zebrafish/metabolism*
  • alpha-Crystallins/chemistry
  • alpha-Crystallins/metabolism
  • beta-Crystallins/chemistry
  • beta-Crystallins/metabolism
  • gamma-Crystallins/chemistry
  • gamma-Crystallins/metabolism
PubMed: 18449354
FIGURES
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.
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