Protective effect of SENP3-mediated SUMOylation against cadmium toxicity Hongquan Zhu (The Journal of Toxicological Sciences, 42, 233-240, 2017)
This article has been retracted due to plagiarism of the following paper recently accepted by the editorial committee:
Increased SUMO-2/3-ylation mediated by SENP3 degradation is protective against cadmium-induced caspase 3–dependentcytotoxicity by Jia Luo, Sonam Gurung, Laura Lee, Jeremy M Henley, Kevin A Wilkinson, and Chun Guo,The Journal of Toxicological Sciences, 42, 529-538, 2017.
Accordingly, it shall not be regarded as an original paper. The author has acknowledged his plagiarism, and his apologies have been accepted. The author obtained the manuscript by improper means and submitted it to the journal as his own work. Since the manuscript had not been published yet, the editorial committee was unable to detect the plagiarism.
Toshiyuki Kaji, Ph.D. Editor-in-Chief The Journal of Toxicological Sciences
Increased post-translational modification of proteins by SUMO-2/3 is a cytoprotective response against cell stress induced by ischaemia and reperfusion. However, it is still unclear what other cell stressors trigger protein SUMOylation, what mechanisms enhance and maintain the enhanced SUMOylation, and if it is a general protective mediator against other cytotoxic stresses. Here, we show increased levels of SUMOylation and decreased levels of the SUMO deconjugating enzyme SENP3 in PC12 cells treated with the toxic heavy metal cadmium. In addition, SENP3 knockdown reduced cadmium-induced caspase 3 cleavage and cell death in PC12 cells, while SENP3 overexpression enhanced cell death. These results suggest that SENP3 is an important regulator of the cellular response to cadmium stress in PC12 cells. Our findings are consistent with previous reports of decreased SENP3 and increased SUMOylation in ischaemia, and imply that the regulation of SENP3 levels and subsequent changes in SUMOylation could be a cytoprotective mechanism against caspase 3-mediated cell death.
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