AI Article Synopsis
- Microcystins (MCs), toxins from freshwater cyanobacteria, pose health risks to humans and aquatic life due to their mechanism of inhibiting protein phosphatases 1 and 2A.
- This study utilized a chemical proteomic approach to identify 17 proteins from zebrafish liver that interact with MC-arginine-arginine (MC-RR), revealing their involvement in liver toxicity phenomena like cytoskeleton disruption and oxidative stress.
- Findings suggest that MCs' overall toxicity is influenced not only by protein inhibition but also by how they distribute within cells and interact with other proteins, contributing to a better understanding of their hepatotoxic effects.
Article 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. © 2015 Wiley Periodicals, Inc. Environ Toxicol 31: 1206-1216, 2016.
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| http://dx.doi.org/10.1002/tox.22128 | DOI Listing |
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