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Journal articles on the topic 'Mercaptopyruvate sulfurtransferase'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 February 2022

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1

Nagahara, Noriyuki. "Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System." Biomolecules 10, no. 6 (May 28, 2020): 826. http://dx.doi.org/10.3390/biom10060826.

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Glutaredoxin (EC 1.15–1.21) is known as an oxidoreductase that protects cysteine residues within proteins against oxidative stress. Glutaredoxin catalyzes an electron transfer reaction that donates an electron to substrate proteins in the reducing system composed of glutaredoxin, glutathione, glutathione reductase, and nicotinamide-adenine dinucleotide phosphate (reduced form). 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) is a cysteine enzyme that catalyzes transsulfuration, and glutaredoxin activates 3-mercaptopyruvate sulfurtransferase in the reducing system. Interestingly, even when glutathione or glutathione reductase was absent, 3-mercaptopyruvate sulfurtransferase activity increased, probably because reduced glutaredoxin was partly present and able to activate 3-mercaptopyruvate sulfurtransferase until depletion. A study using mutant Escherichia coli glutaredoxin1 (Cys14 is the binding site of glutathione and was replaced with a Ser residue) confirmed these results. Some inconsistency was noted, and glutaredoxin with higher redox potential than either 3-mercaptopyruvate sulfurtransferase or glutathione reduced 3-mercaptopyruvate sulfurtransferase. However, electron-transfer enzymatically proceeded from glutaredoxin to 3-mercaptopyruvate sulfurtransferase.

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2

Nagahara, Noriyuki. "Catalytic Site Cysteines of Thiol Enzyme: Sulfurtransferases." Journal of Amino Acids 2011 (December 28, 2011): 1–7. http://dx.doi.org/10.4061/2011/709404.

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Thiol enzymes have single- or double-catalytic site cysteine residues and are redox active. Oxidoreductases and isomerases contain double-catalytic site cysteine residues, which are oxidized to a disulfide via a sulfenyl intermediate and reduced to a thiol or a thiolate. The redox changes of these enzymes are involved in their catalytic processes. On the other hand, transferases, and also some phosphatases and hydrolases, have a single-catalytic site cysteine residue. The cysteines are redox active, but their sulfenyl forms, which are inactive, are not well explained biologically. In particular, oxidized forms of sulfurtransferases, such as mercaptopyruvate sulfurtransferase and thiosulfate sulfurtransferase, are not reduced by reduced glutathione but by reduced thioredoxin. This paper focuses on why the catalytic site cysteine of sulfurtransferase is redox active.

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3

Porter, Dale W., and Steven I. Baskin. "Specificity studies of 3-mercaptopyruvate sulfurtransferase." Journal of Biochemical Toxicology 10, no. 6 (October 1995): 287–92. http://dx.doi.org/10.1002/jbt.2570100602.

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4

Mitidieri, Emma, Teresa Tramontano, Danila Gurgone, Valentina Citi, Vincenzo Calderone, Vincenzo Brancaleone, Antonia Katsouda, et al. "Mercaptopyruvate acts as endogenous vasodilator independently of 3-mercaptopyruvate sulfurtransferase activity." Nitric Oxide 75 (May 2018): 53–59. http://dx.doi.org/10.1016/j.niox.2018.02.003.

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5

Nagahara, Noriyuki. "S9-2 Mercaptopyruvate sulfurtransferase and hydrogen sulfide." Nitric Oxide 39 (May 2014): S12. http://dx.doi.org/10.1016/j.niox.2014.03.044.

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6

Alphey, Magnus S., Roderick A. M. Williams, Jeremy C. Mottram, Graham H. Coombs, and William N. Hunter. "The Crystal Structure ofLeishmania major3-Mercaptopyruvate Sulfurtransferase." Journal of Biological Chemistry 278, no. 48 (September 1, 2003): 48219–27. http://dx.doi.org/10.1074/jbc.m307187200.

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7

Nagahara, Noriyuki, Taro Yoshii, Yasuko Abe, and Tomohiro Matsumura. "Thioredoxin-dependent Enzymatic Activation of Mercaptopyruvate Sulfurtransferase." Journal of Biological Chemistry 282, no. 3 (November 27, 2006): 1561–69. http://dx.doi.org/10.1074/jbc.m605931200.

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8

Tomita, Masahiro, Noriyuki Nagahara, and Takaaki Ito. "Expression of 3-Mercaptopyruvate Sulfurtransferase in the Mouse." Molecules 21, no. 12 (December 11, 2016): 1707. http://dx.doi.org/10.3390/molecules21121707.

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9

Peleli, Maria, Sofia-Iris Bibli, Zhen Li, Athanasia Chatzianastasiou, Aimilia Varela, Antonia Katsouda, Sven Zukunft, et al. "Cardiovascular phenotype of mice lacking 3-mercaptopyruvate sulfurtransferase." Biochemical Pharmacology 176 (June 2020): 113833. http://dx.doi.org/10.1016/j.bcp.2020.113833.

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10

Katsouda, Antonia, Nikos Malissovas, Andreas Papapetropoulos, and Dimitris Beis. "Function of 3-mercaptopyruvate sulfurtransferase in zebrafish (Danio rerio)." Nitric Oxide 47 (May 2015): S38. http://dx.doi.org/10.1016/j.niox.2015.02.092.

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11

Kimura, Hideo, Norihiro Shibuya, Yoshinori Mikami, Yuka Kimura, and Noriyuki Nagahara. "Vascular endothelium expresses 3-mercaptopyruvate sulfurtransferase and produces H2S." Neuroscience Research 68 (January 2010): e117. http://dx.doi.org/10.1016/j.neures.2010.07.2088.

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12

Abdollahi Govar, Armita, Gábor Törő, Peter Szaniszlo, Athanasia Pavlidou, Sofia‐Iris Bibli, Ketan Thanki, Vicente A. Resto, et al. "3‐Mercaptopyruvate sulfurtransferase supports endothelial cell angiogenesis and bioenergetics." British Journal of Pharmacology 177, no. 4 (March 4, 2019): 866–83. http://dx.doi.org/10.1111/bph.14574.

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13

Yadav, Pramod Kumar, Victor Vitvitsky, Sebastián Carballal, Javier Seravalli, and Ruma Banerjee. "Thioredoxin regulates human mercaptopyruvate sulfurtransferase at physiologically-relevant concentrations." Journal of Biological Chemistry 295, no. 19 (March 16, 2020): 6299–311. http://dx.doi.org/10.1074/jbc.ra120.012616.

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3-Mercaptopyruvate sulfur transferase (MPST) catalyzes the desulfuration of 3-mercaptopyruvate (3-MP) and transfers sulfane sulfur from an enzyme-bound persulfide intermediate to thiophilic acceptors such as thioredoxin and cysteine. Hydrogen sulfide (H2S), a signaling molecule implicated in many physiological processes, can be released from the persulfide product of the MPST reaction. Two splice variants of MPST, differing by 20 amino acids at the N terminus, give rise to the cytosolic MPST1 and mitochondrial MPST2 isoforms. Here, we characterized the poorly-studied MPST1 variant and demonstrated that substitutions in its Ser–His–Asp triad, proposed to serve a general acid–base role, minimally affect catalytic activity. We estimated the 3-MP concentration in murine liver, kidney, and brain tissues, finding that it ranges from 0.4 μmol·kg−1 in brain to 1.4 μmol·kg−1 in kidney. We also show that N-acetylcysteine, a widely-used antioxidant, is a poor substrate for MPST and is unlikely to function as a thiophilic acceptor. Thioredoxin exhibits substrate inhibition, increasing the KM for 3-MP ∼15-fold compared with other sulfur acceptors. Kinetic simulations at physiologically-relevant substrate concentrations predicted that the proportion of sulfur transfer to thioredoxin increases ∼3.5-fold as its concentration decreases from 10 to 1 μm, whereas the total MPST reaction rate increases ∼7-fold. The simulations also predicted that cysteine is a quantitatively-significant sulfane sulfur acceptor, revealing MPST's potential to generate low-molecular-weight persulfides. We conclude that the MPST1 and MPST2 isoforms are kinetically indistinguishable and that thioredoxin modulates the MPST-catalyzed reaction in a physiologically-relevant concentration range.

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14

Nagahara, Noriyuki, Taro Okazaki, and Takeshi Nishino. "Cytosolic Mercaptopyruvate Sulfurtransferase Is Evolutionarily Related to Mitochondrial Rhodanese." Journal of Biological Chemistry 270, no. 27 (July 7, 1995): 16230–35. http://dx.doi.org/10.1074/jbc.270.27.16230.

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15

Nagahara, Noriyuki, Mio Tanaka, Yukichi Tanaka, and Takaaki Ito. "Novel Characterization of Antioxidant Enzyme, 3-Mercaptopyruvate Sulfurtransferase-Knockout Mice: Overexpression of the Evolutionarily-Related Enzyme Rhodanese." Antioxidants 8, no. 5 (May 1, 2019): 116. http://dx.doi.org/10.3390/antiox8050116.

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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.

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16

Mikami, Yoshinori, Norihiro Shibuya, Yuka Kimura, Noriyuki Nagahara, Yuki Ogasawara, and Hideo Kimura. "Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide." Biochemical Journal 439, no. 3 (October 13, 2011): 479–85. http://dx.doi.org/10.1042/bj20110841.

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H2S (hydrogen sulfide) has recently been recognized as a signalling molecule as well as a cytoprotectant. We recently demonstrated that 3MST (3-mercaptopyruvate sulfurtransferase) produces H2S from 3MP (3-mercaptopyruvate). Although a reducing substance is required for an intermediate persulfide at the active site of 3MST to release H2S, the substance has not been identified. In the present study we show that Trx (thioredoxin) and DHLA (dihydrolipoic acid) associate with 3MST to release H2S. Other reducing substances, such as NADPH, NADH, GSH, cysteine and CoA, did not have any effect on the reaction. We also show that 3MST produces H2S from thiosulfate. The present study provides a new insight into a mechanism for the production of H2S by 3MST.

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17

Shibuya, N., Y. Mikami, Y. Kimura, N. Nagahara, and H. Kimura. "Vascular Endothelium Expresses 3-Mercaptopyruvate Sulfurtransferase and Produces Hydrogen Sulfide." Journal of Biochemistry 146, no. 5 (July 15, 2009): 623–26. http://dx.doi.org/10.1093/jb/mvp111.

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18

Mikami, Yoshinori, Norihiro Shibuya, Yuka Kimura, Yuki Ogasawara, Kazuyuki Ishii, and Hideo Kimura. "Dihydrolipoic acid is a cofactor of 3-mercaptopyruvate sulfurtransferase for reducing 3-mercaptopyruvate to generate hydrogen sulfide." Neuroscience Research 68 (January 2010): e117-e118. http://dx.doi.org/10.1016/j.neures.2010.07.2089.

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19

Katz, Y., V. Gazit, and D. Ben-Shachar. "3-mercaptopyruvate sulfurtransferase activity in brain and liver in the mouse." Biological Psychiatry 42, no. 1 (July 1997): 47S. http://dx.doi.org/10.1016/s0006-3223(97)87080-1.

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20

Ostrakhovitch, Elena A., Shin Akakura, Reiko Sanokawa-Akakura, and Siamak Tabibzadeh. "3-Mercaptopyruvate sulfurtransferase disruption in dermal fibroblasts facilitates adipogenic trans-differentiation." Experimental Cell Research 385, no. 2 (December 2019): 111683. http://dx.doi.org/10.1016/j.yexcr.2019.111683.

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21

Yadav, Pramod Kumar, Kazuhiro Yamada, Taurai Chiku, Markos Koutmos, and Ruma Banerjee. "Structure and Kinetic Analysis of H2S Production by Human Mercaptopyruvate Sulfurtransferase." Journal of Biological Chemistry 288, no. 27 (May 22, 2013): 20002–13. http://dx.doi.org/10.1074/jbc.m113.466177.

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22

Nagahara, Noriyuki, and Nori Sawada. "The Mercaptopyruvate Pathway in Cysteine Catabolism: A Physiologic Role and Related Disease of the Multifunctional 3-Mercaptopyruvate Sulfurtransferase." Current Medicinal Chemistry 13, no. 10 (April 1, 2006): 1219–30. http://dx.doi.org/10.2174/092986706776360914.

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23

Singh, Poonam, Pooja Rao, and Rahul Bhattacharya. "Dose and Time-Dependent Effects of Cyanide on Thiosulfate Sulfurtransferase, 3-Mercaptopyruvate Sulfurtransferase, and Cystathionine λ-Lyase Activities." Journal of Biochemical and Molecular Toxicology 27, no. 12 (August 8, 2013): 499–507. http://dx.doi.org/10.1002/jbt.21514.

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24

Moeller, Bryant M., Daune L. Crankshaw, Jacquie Briggs, Herbert T. Nagasawa, and Steven E. Patterson. "In-vitro mercaptopyruvate sulfurtransferase species comparison in humans and common laboratory animals." Toxicology Letters 274 (May 2017): 64–68. http://dx.doi.org/10.1016/j.toxlet.2017.04.005.

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25

Nagahara, Noriyuki. "Regulation of Mercaptopyruvate Sulfurtransferase Activity Via Intrasubunit and Intersubunit Redox-Sensing Switches." Antioxidants & Redox Signaling 19, no. 15 (November 20, 2013): 1792–802. http://dx.doi.org/10.1089/ars.2012.5031.

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26

Zhao, Heng, Su-Jing Chan, Yee-Kong Ng, and Peter T. H. Wong. "Brain 3-Mercaptopyruvate Sulfurtransferase (3MST): Cellular Localization and Downregulation after Acute Stroke." PLoS ONE 8, no. 6 (June 21, 2013): e67322. http://dx.doi.org/10.1371/journal.pone.0067322.

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27

Spallarossa, Andrea, Aristodemo Carpen, Fabio Forlani, Silvia Pagani, Martino Bolognesi, and Domenico Bordo. "SseA, a 3-mercaptopyruvate sulfurtransferase fromEscherichia coli: crystallization and preliminary crystallographic data." Acta Crystallographica Section D Biological Crystallography 59, no. 1 (December 20, 2002): 168–70. http://dx.doi.org/10.1107/s0907444902019248.

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28

Porter, Dale W., and Steven I. Baskin. "The effect of three α-keto acids on 3-mercaptopyruvate sulfurtransferase activity." Journal of Biochemical Toxicology 11, no. 1 (1996): 45–50. http://dx.doi.org/10.1002/(sici)1522-7146(1996)11:1<45::aid-jbt6>3.0.co;2-v.

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29

Wing, David A., and Steven I. Baskin. "Modifiers of mercaptopyruvate sulfurtransferase catalyzed conversion of cyanide to thiocyanate in vitro." Journal of Biochemical Toxicology 7, no. 2 (1992): 65–72. http://dx.doi.org/10.1002/jbt.2570070203.

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30

Wróbel, Maria, and Halina Jurkowska. "Menadione effect on l-cysteine desulfuration in U373 cells." Acta Biochimica Polonica 54, no. 2 (May 23, 2007): 407–11. http://dx.doi.org/10.18388/abp.2007_3263.

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The non-cytotoxic concentration (20 microM) of menadione (2-methyl-1,4-naphthoquinone), after 1 h of incubation, leads to loss of the activity of rhodanese by 33%, 3-mercaptopyruvate sulfurtransferase by 20%, as well as the level of sulfane sulfur by about 23% and glutathione by 12%, in the culture of U373 cells, in comparison with the control culture. Reactive oxygen species generated by menadione oxidize sulfhydryl groups in active centers of the investigated enzymes, inhibiting them and saving cysteine for glutathione synthesis. A decreased sulfane sulfur level can be correlated with an oxidative stress.

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31

Casin, Kevin M., and John W. Calvert. "Harnessing the Benefits of Endogenous Hydrogen Sulfide to Reduce Cardiovascular Disease." Antioxidants 10, no. 3 (March 4, 2021): 383. http://dx.doi.org/10.3390/antiox10030383.

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Cardiovascular disease is the leading cause of death in the U.S. While various studies have shown the beneficial impact of exogenous hydrogen sulfide (H2S)-releasing drugs, few have demonstrated the influence of endogenous H2S production. Modulating the predominant enzymatic sources of H2S—cystathionine-β-synthase, cystathionine-γ-lyase, and 3-mercaptopyruvate sulfurtransferase—is an emerging and promising research area. This review frames the discussion of harnessing endogenous H2S within the context of a non-ischemic form of cardiomyopathy, termed diabetic cardiomyopathy, and heart failure. Also, we examine the current literature around therapeutic interventions, such as intermittent fasting and exercise, that stimulate H2S production.

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32

Nagahara, Noriyuki, Qing Li, and Nori Sawada. "Do Antidotes for Acute Cyanide Poisoning Act on Mercaptopyruvate Sulfurtransferase to Facilitate Detoxification?" Current Drug Targets - Immune, Endocrine & Metabolic Disorders 3, no. 3 (September 1, 2003): 198–204. http://dx.doi.org/10.2174/1568008033340162.

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33

Frendo, J., and M. Wróbel. "The activity of 3-mercaptopyruvate sulfurtransferase in erythrocytes from patients with polycythemia vera." Acta Biochimica Polonica 44, no. 4 (December 31, 1997): 771–73. http://dx.doi.org/10.18388/abp.1997_4380.

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34

Shibuya, Norihiro, Makiko Tanaka, Mikiharu Yoshida, Yuki Ogasawara, Tadayasu Togawa, Kazuyuki Ishii, and Hideo Kimura. "3-Mercaptopyruvate Sulfurtransferase Produces Hydrogen Sulfide and Bound Sulfane Sulfur in the Brain." Antioxidants & Redox Signaling 11, no. 4 (April 2009): 703–14. http://dx.doi.org/10.1089/ars.2008.2253.

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35

Gröger, Michael, Martin Wepler, Ulrich Wachter, Tamara Merz, Oscar McCook, Sandra Kress, Britta Lukaschewski, et al. "The Effects of Genetic 3-Mercaptopyruvate Sulfurtransferase Deficiency in Murine Traumatic-Hemorrhagic Shock." SHOCK 51, no. 4 (April 2019): 472–78. http://dx.doi.org/10.1097/shk.0000000000001165.

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36

Gero, Domokos, Akbar Ahmad, Attila Brunyanszki, Gabor Olah, Bartosz Szczesny, and Csaba Szabo. "3-Mercaptopyruvate sulfurtransferase deficient mice show accelerated glucose uptake and a dysregulated metabolic profile." Nitric Oxide 47 (May 2015): S35—S36. http://dx.doi.org/10.1016/j.niox.2015.02.086.

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37

Nagahara, Noriyuki, and Takeshi Nishino. "Role of Amino Acid Residues in the Active Site of Rat Liver Mercaptopyruvate Sulfurtransferase." Journal of Biological Chemistry 271, no. 44 (November 1, 1996): 27395–401. http://dx.doi.org/10.1074/jbc.271.44.27395.

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38

Miyamoto, Ryo, Ken-ichi Otsuguro, Soichiro Yamaguchi, and Shigeo Ito. "Contribution of cysteine aminotransferase and mercaptopyruvate sulfurtransferase to hydrogen sulfide production in peripheral neurons." Journal of Neurochemistry 130, no. 1 (March 27, 2014): 29–40. http://dx.doi.org/10.1111/jnc.12698.

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39

Croppi, Giorgia, Yueyang Zhou, Rong Yang, Yunfei Bian, Mingtao Zhao, Youtian Hu, Benfang Helen Ruan, Jing Yu, and Fang Wu. "Discovery of an Inhibitor for Bacterial 3-Mercaptopyruvate Sulfurtransferase that Synergistically Controls Bacterial Survival." Cell Chemical Biology 27, no. 12 (December 2020): 1483–99. http://dx.doi.org/10.1016/j.chembiol.2020.10.012.

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40

Li, Mingqiang, Lihong Nie, Yajie Hu, Xiang Yan, Lian Xue, Li Chen, Hua Zhou, and Yu Zheng. "Chronic intermittent hypoxia promotes expression of 3-mercaptopyruvate sulfurtransferase in adult rat medulla oblongata." Autonomic Neuroscience 179, no. 1-2 (December 2013): 84–89. http://dx.doi.org/10.1016/j.autneu.2013.08.066.

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41

Zhang, Yuan, Zhi-Han Tang, Zhong Ren, Shun-Lin Qu, Mi-Hua Liu, Lu-Shan Liu, and Zhi-Sheng Jiang. "Hydrogen Sulfide, the Next Potent Preventive and Therapeutic Agent in Aging and Age-Associated Diseases." Molecular and Cellular Biology 33, no. 6 (January 7, 2013): 1104–13. http://dx.doi.org/10.1128/mcb.01215-12.

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Hydrogen sulfide (H2S) is the third endogenous signaling gasotransmitter, following nitric oxide and carbon monoxide. It is physiologically generated by cystathionine-γ-lyase, cystathionine-β-synthase, and 3-mercaptopyruvate sulfurtransferase. H2S has been gaining increasing attention as an important endogenous signaling molecule because of its significant effects on the cardiovascular and nervous systems. Substantial evidence shows that H2S is involved in aging by inhibiting free-radical reactions, activating SIRT1, and probably interacting with the age-related geneKlotho. Moreover, H2S has been shown to have therapeutic potential in age-associated diseases. This article provides an overview of the physiological functions and effects of H2S in aging and age-associated diseases, and proposes the potential health and therapeutic benefits of H2S.

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42

Westrop, Gareth D., Ina Georg, and Graham H. Coombs. "The Mercaptopyruvate Sulfurtransferase of Trichomonas vaginalis Links Cysteine Catabolism to the Production of Thioredoxin Persulfide." Journal of Biological Chemistry 284, no. 48 (September 17, 2009): 33485–94. http://dx.doi.org/10.1074/jbc.m109.054320.

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43

TANABE, Shinzo, Yuki OGASAWARA, Masashi NAWATA, and Koji KAWANABE. "Preparation of a sulfurtransferase substrate, sodium 3-mercaptopyruvate, from 3-bromopyruvic acid and sodium hydrosulfide." CHEMICAL & PHARMACEUTICAL BULLETIN 37, no. 10 (1989): 2843–45. http://dx.doi.org/10.1248/cpb.37.2843.

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44

Nagahara, Noriyuki. "Multiple role of 3-mercaptopyruvate sulfurtransferase: antioxidative function, H2S and polysulfide production and possible SOxproduction." British Journal of Pharmacology 175, no. 4 (January 11, 2018): 577–89. http://dx.doi.org/10.1111/bph.14100.

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45

Xia, Huijing, Zhen Li, Noriyuki Nagahara, Jean Carnal, and David Lefer. "Genetic Knockout of 3‐Mercaptopyruvate Sulfurtransferase Increases Acute Myocardial Ischemia/Reperfusion Injury in Aged Mice." FASEB Journal 34, S1 (April 2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.04685.

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46

Nawata, Masashi, Yuki Ogasawara, Koji Kawanabe, and Shinzo Tanabe. "Enzymatic assay of 3-mercaptopyruvate sulfurtransferase activity in human red blood cells using pyruvate oxidase." Analytical Biochemistry 190, no. 1 (October 1990): 84–87. http://dx.doi.org/10.1016/0003-2697(90)90137-x.

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47

Módis, Katalin, Antonia Asimakopoulou, Ciro Coletta, Andreas Papapetropoulos, and Csaba Szabo. "Oxidative stress suppresses the cellular bioenergetic effect of the 3-mercaptopyruvate sulfurtransferase/hydrogen sulfide pathway." Biochemical and Biophysical Research Communications 433, no. 4 (April 2013): 401–7. http://dx.doi.org/10.1016/j.bbrc.2013.02.131.

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48

Akahoshi, Noriyuki, Tatsuro Minakawa, Masashi Miyashita, Uran Sugiyama, Chihiro Saito, Rintaro Takemoto, Akihiro Honda, et al. "Increased Urinary 3-Mercaptolactate Excretion and Enhanced Passive Systemic Anaphylaxis in Mice Lacking Mercaptopyruvate Sulfurtransferase, a Model of Mercaptolactate-Cysteine Disulfiduria." International Journal of Molecular Sciences 21, no. 3 (January 27, 2020): 818. http://dx.doi.org/10.3390/ijms21030818.

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Mercaptopyruvate sulfurtransferase (Mpst) and its homolog thiosulfate sulfurtransferase (Tst = rhodanese) detoxify cyanide to thiocyanate. Mpst is attracting attention as one of the four endogenous hydrogen sulfide (H2S)/reactive sulfur species (RSS)-producing enzymes, along with cystathionine β-synthase (Cbs), cystathionine γ-lyase (Cth), and cysteinyl-tRNA synthetase 2 (Cars2). MPST deficiency was found in 1960s among rare hereditary mercaptolactate-cysteine disulfiduria patients. Mpst-knockout (KO) mice with enhanced liver Tst expression were recently generated as its model; however, the physiological roles/significances of Mpst remain largely unknown. Here we generated three independent germ lines of Mpst-KO mice by CRISPR/Cas9 technology, all of which maintained normal hepatic Tst expression/activity. Mpst/Cth-double knockout (DKO) mice were generated via crossbreeding with our previously generated Cth-KO mice. Mpst-KO mice were born at the expected frequency and developed normally like Cth-KO mice, but displayed increased urinary 3-mercaptolactate excretion and enhanced passive systemic anaphylactic responses when compared to wild-type or Cth-KO mice. Mpst/Cth-DKO mice were also born at the expected frequency and developed normally, but excreted slightly more 3-mercaptolactate in urine compared to Mpst-KO or Cth-KO mice. Our Mpst-KO, Cth-KO, and Mpst/Cth-DKO mice, unlike semi-lethal Cbs-KO mice and lethal Cars2-KO mice, are useful tools for analyzing the unknown physiological roles of endogenous H2S/RSS production.

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49

Ramasamy, S., S. Singh, P. Taniere, M. J. S. Langman, and M. C. Eggo. "Sulfide-detoxifying enzymes in the human colon are decreased in cancer and upregulated in differentiation." American Journal of Physiology-Gastrointestinal and Liver Physiology 291, no. 2 (August 2006): G288—G296. http://dx.doi.org/10.1152/ajpgi.00324.2005.

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H2S is highly toxic and selectively inhibits butyrate oxidation in colonocytes. Ineffective detoxification may result in mucosal insult, inflammation, and ultimately in colorectal cancer (CRC). Rhodanese can detoxify H2S and is comprised of two isoenzymes: thiosulfate sulfurtransferase (TST) and mercaptopyruvate sulfurtransferase (MST). Using specific antisera to discriminate TST from MST, we found that only TST could detoxify H2S. In sections of normal colon, both enzymes were located on the luminal mucosal surface, and they were expressed in the colonocytes but not in the mucin-secreting goblet cells. Expression of both enzymes was focally lost in ulcerative colitis and markedly reduced in advanced colon cancer, the disease progression correlating with the decreased expression of MST and TST. In HT-29 cells, a human colon cancer cell line, TST activity and expression were significantly increased by butyrate and by histone deacetylase inhibition, agents that promote HT-29 cell differentiation. Sulfide (0.1 mM) also increased TST activity, but higher sulfide concentrations (0.3–3 mM) were toxic. Preincubation in butyrate to increase TST expression, decreased sensitivity of the cells to sulfide toxicity. We conclude that decreased expression of TST (or MST) is a tumor marker for CRC. TST expression is increased in colonocyte differentiation. Dysregulation of TST expression and activity resulting in inability to effectively detoxify could be a factor in the cell loss and inflammation that accompany ulcerative colitis and ultimately then in CRC.

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Augsburger, Fiona, and Csaba Szabo. "Potential role of the 3-mercaptopyruvate sulfurtransferase (3-MST)—hydrogen sulfide (H2S) pathway in cancer cells." Pharmacological Research 154 (April 2020): 104083. http://dx.doi.org/10.1016/j.phrs.2018.11.034.

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