Proteomic analysis of methyl parathion-responsive proteins in zebrafish (Danio rerio) brain

Comp Biochem Physiol C Toxicol Pharmacol. 2011 Jan;153(1):67-74. doi: 10.1016/j.cbpc.2010.08.009. Epub 2010 Sep 15.

Abstract

Methyl parathion (MP), an organophosphorus pesticide used worldwide, has been associated with a wide spectrum of toxic effects on organisms in the environment. This study set out to analyze the alteration of protein profiles in MP-exposed zebrafish (Danio rerio) brain and find the proteins responsive to MP toxicity. Zebrafish were subjected to 1, 3 and 5mg/L MP and the proteomic changes in their brains were revealed using two-dimensional gel electrophoresis. Six protein spots were observed to be significantly changed by MP exposure. Among these, 4 spots were down-regulated, while 2 spots were up-regulated. These altered spots were excised from the gels and identified by matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry and database searching. The results indicate that these proteins were involved in binding, catalysis, regulation of energy metabolism and cell structure. These data may provide novel biomarkers for the evaluation of MP contamination and useful insights for understanding the mechanisms of MP toxicity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholinesterase / metabolism
  • Animals
  • Brain / enzymology
  • Brain / metabolism*
  • Cholinesterase Inhibitors / toxicity
  • Insecticides / toxicity*
  • Methyl Parathion / toxicity*
  • Proteome / metabolism
  • RNA, Messenger / metabolism
  • Zebrafish / metabolism*
  • Zebrafish Proteins / genetics
  • Zebrafish Proteins / metabolism*

Substances

  • Cholinesterase Inhibitors
  • Insecticides
  • Proteome
  • RNA, Messenger
  • Zebrafish Proteins
  • Methyl Parathion
  • Acetylcholinesterase