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

• Published in: Antioxidants Vol. 8; no. 5; p. 116
• Main Authors: Nagahara, Noriyuki, Tanaka, Mio, Tanaka, Yukichi, Ito, Takaaki
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 01.05.2019; MDPI
• Subjects: 3-Mercaptopyruvate sulfurtransferase; Antioxidants; Cytosol; Enzymes; Fractions; Gene expression; Hydrogen sulfide; knockout mouse; Laboratory animals; mercaptopyruvate sulfurtransferase; Mitochondria; Pathogenesis; Phosphatase; Polyclonal antibodies; Polymerase chain reaction; Proteins; real-time quantitative polymerase chain reaction; Rhodanese; Rodents; Sulfurtransferase; Thermal cycling; United States > US; Japan; real-time quantitative polymerase chain reaction; rhodanese; mercaptopyruvate sulfurtransferase; knockout mouse
• ISSN: 2076-3921; 2076-3921
• DOI: 10.3390/antiox8050116

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.