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Toxins 2015, 7(6), 2221-2231;

Proteasome as a Molecular Target of Microcystin-LR

School of Chemistry and Biological Engineering, University of Science and Technology Beijing, Beijing 100083, China
Author to whom correspondence should be addressed.
Academic Editor: John P. Berry
Received: 5 May 2015 / Revised: 27 May 2015 / Accepted: 12 June 2015 / Published: 17 June 2015
(This article belongs to the Section Marine and Freshwater Toxins)
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Proteasome degrades proteins in eukaryotic cells. As such, the proteasome is crucial in cell cycle and function. This study proved that microcystin-LR (MC-LR), which is a toxic by-product of algal bloom, can target cellular proteasome and selectively inhibit proteasome trypsin-like (TL) activity. MC-LR at 1 nM can inhibit up to 54% of the purified 20S proteasome TL activity and 43% of the proteasome TL activity in the liver of the cyprinid rare minnow (Gobiocypris rarus). Protein degradation was retarded in GFP-CL1-transfected PC-3 cells because MC-LR inhibited the proteasome TL activity. Docking studies indicated that MC-LR blocked the active site of the proteasome β2 subunit; thus, the proteasome TL activity was inhibited. In conclusion, MC-LR can target proteasome, selectively inhibit proteasome TL activity, and retard protein degradation. This study may be used as a reference of future research on the toxic mechanism of MC-LR. View Full-Text
Keywords: microcystin-LR; proteasome trypsin-like activity; mechanism; molecular docking microcystin-LR; proteasome trypsin-like activity; mechanism; molecular docking

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Zhu, Z.; Zhang, L.; Shi, G. Proteasome as a Molecular Target of Microcystin-LR. Toxins 2015, 7, 2221-2231.

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