ZFIN ID: ZDB-PUB-150410-6
Chemical proteomic analysis of the potential toxicological mechanisms of microcystin-RR in zebrafish (Danio rerio) liver
Tuo, X., Chen, J., Zhao, S., Xie, P.
Date: 2016
Source: Environmental toxicology   31(10): 1206-16 (Journal)
Registered Authors: Chen, Jun
Keywords: chemical proteomics, liver, microcystin-RR, toxicological mechanisms, zebrafish
MeSH Terms:
  • Animals
  • Chromatography, High Pressure Liquid
  • Cyanobacteria/metabolism
  • Cytoskeleton/drug effects
  • Electrophoresis, Gel, Two-Dimensional
  • Humans
  • Liver/drug effects*
  • Liver/metabolism
  • Microcystins/metabolism
  • Microcystins/toxicity*
  • Oxidative Stress/drug effects
  • Protein Phosphatase 1/antagonists & inhibitors
  • Protein Phosphatase 1/metabolism
  • Protein Phosphatase 2/antagonists & inhibitors
  • Protein Phosphatase 2/metabolism
  • Proteome/analysis
  • Proteome/drug effects*
  • Proteomics*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Zebrafish/metabolism*
PubMed: 25854999 Full text @ Env. Tox.
ABSTRACT

Microcystins (MCs) are common toxins produced by freshwater cyanobacteria, and they represent a potential health risk to aquatic organisms and animals, including humans. Specific inhibition of protein phosphatases 1 and 2A is considered the typical mechanism of MCs toxicity, but the exact mechanism has not been fully elucidated. To further our understanding of the toxicological mechanisms induced by MCs, this study is the first to use a chemical proteomic approach to screen proteins that exhibit special interactions with MC-arginine-arginine (MC-RR) from zebrafish (Danio rerio) liver. Seventeen proteins were identified via affinity blocking test. Integration of the results of previous studies and this study revealed that these proteins play a crucial role in various toxic phenomena of liver induced by MCs, such as the disruption of cytoskeleton assembly, oxidative stress, and metabolic disorder. Moreover, in addition to inhibition of protein phosphate activity, the overall toxicity of MCs was simultaneously modulated by the distribution of MCs in cells and their interactions with other target proteins. These results provide new insight into the mechanisms of hepatotoxicity induced by MCs.

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