Nagahara Noriyuki, Tanaka Mio, Tanaka Yukichi, Ito Takaaki
Isotope Research Laboratory, Nippon Medical School, Tokyo 113-8602, Japan.
Department of Pathology, Kanagawa Children's Medical Center, Yokohama 232-8555, Japan.
Antioxidants (Basel). 2019 May 1;8(5):116. 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.
抗氧化酶3-巯基丙酮酸硫转移酶(MST,EC 2.8.1.2)定位于细胞质和线粒体中,而与之进化相关的酶硫氰酸酶(硫代硫酸盐硫转移酶,TST,EC 2.8.1.1)定位于线粒体中。最近,已证实这两种酶都能产生硫化氢和多硫化物。对肝脏线粒体进行亚细胞分级分离显示,MST基因敲除(KO)/野生型小鼠的TST活性比约为2.5;正如预期的那样,仅在野生型小鼠中检测到MST活性。通过实时定量聚合酶链反应分析测得,KO/野生型小鼠的TST mRNA表达比约为3.3。得出的结论是,TST在MST-KO小鼠中过表达。