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Novel Characterization of Antioxidant Enzyme, 3-Mercaptopyruvate Sulfurtransferase-Knockout Mice: Overexpression of the Evolutionarily-Related Enzyme Rhodanese

1
Isotope Research Laboratory, Nippon Medical School, Tokyo 113-8602, Japan
2
Department of Pathology, Kanagawa Children’s Medical Center, Yokohama 232-8555, Japan
3
Department of Pathology and Experimental Medicine, Graduate School of Medical Science, Kumamoto University, Kumamoto 860-8556, Japan
*
Author to whom correspondence should be addressed.
Antioxidants 2019, 8(5), 116; https://doi.org/10.3390/antiox8050116
Received: 25 March 2019 / Revised: 24 April 2019 / Accepted: 26 April 2019 / Published: 1 May 2019
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Abstract

The antioxidant enzyme, 3-mercaptopyruvate sulfurtransferase (MST, EC 2.8.1.2) is localized in the cytosol and mitochondria, while the evolutionarily-related enzyme, rhodanese (thiosulfate sulfurtransferase, TST, EC 2.8.1.1) is localized in the mitochondria. Recently, both enzymes have been shown to produce hydrogen sulfide and polysulfide. Subcellular fractionation of liver mitochondria revealed that the TST activity ratio of MST-knockout (KO)/wild-type mice was approximately 2.5; MST activity was detected only in wild-type mice, as expected. The ratio of TST mRNA expression of KO/wild-type mice, as measured by real-time quantitative polymerase chain reaction analysis, was approximately 3.3. It is concluded that TST is overexpressed in MST-KO mice. View Full-Text
Keywords: knockout mouse; mercaptopyruvate sulfurtransferase; rhodanese; real-time quantitative polymerase chain reaction knockout mouse; mercaptopyruvate sulfurtransferase; rhodanese; real-time quantitative polymerase chain reaction
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Nagahara, N.; Tanaka, M.; Tanaka, Y.; Ito, T. Novel Characterization of Antioxidant Enzyme, 3-Mercaptopyruvate Sulfurtransferase-Knockout Mice: Overexpression of the Evolutionarily-Related Enzyme Rhodanese. Antioxidants 2019, 8, 116.

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