| 3-Mercaptopyruvate sulfurtransferase/hydrogen sulfide protects cerebral endothelial cells against oxygen-glucose deprivation/reoxygenation-induced injury via mitoprotection and inhibition of the RhoA/ROCK pathway. | 3-Mercaptopyruvate sulfurtransferase/hydrogen sulfide protects cerebral endothelial cells against oxygen-glucose deprivation/reoxygenation-induced injury via mitoprotection and inhibition of the RhoA/ROCK pathway.
Zhang F, Chen S, Wen JY, Chen ZW. | 12/19/2020 |
| The study revealed a significant role of MPST in hydrogen sulfide metabolism in the pancreas in experimental model of acute pancreatitis. | Hydrogen sulfide formation in experimental model of acute pancreatitis.
Bronowicka-Adamska P, Hutsch T, Gawryś-Kopczyńska M, Maksymiuk K, Wróbel M. | 05/16/2020 |
| Presented is alternative pathway of production of hydrogen sulfide and/or polysulfides from (poly)sulfurated catalytic-site cysteine of reaction intermediates of MST via thioredoxin reduction. | Alternative pathway of H(2)S and polysulfides production from sulfurated catalytic-cysteine of reaction intermediates of 3-mercaptopyruvate sulfurtransferase.
Nagahara N, Koike S, Nirasawa T, Kimura H, Ogasawara Y. | 02/17/2018 |
| observations indicate that 3MST is probably not responsible for the increased production of H2S following permanent middle cerebral artery occlusion. | Brain 3-Mercaptopyruvate Sulfurtransferase (3MST): Cellular Localization and Downregulation after Acute Stroke.
Zhao H, Chan SJ, Ng YK, Wong PT., Free PMC Article | 10/7/2017 |
| 3-Mercaptopyruvate sulphurtransferase and not cystathionine gamma-lyase is the primary regulator of coronary artery hydrogen sulfide production and function. | MPST but not CSE is the primary regulator of hydrogen sulfide production and function in the coronary artery.
Kuo MM, Kim DH, Jandu S, Bergman Y, Tan S, Wang H, Pandey DR, Abraham TP, Shoukas AA, Berkowitz DE, Santhanam L., Free PMC Article | 05/7/2016 |
| Hydrogen sulfide (H2 S) is synthesized in peripheral neurons through two mitochondrial enzymes, cysteine aminotransferase (CAT) and mercaptopyruvate sulfurtransferase (MPST). | Contribution of cysteine aminotransferase and mercaptopyruvate sulfurtransferase to hydrogen sulfide production in peripheral neurons.
Miyamoto R, Otsuguro K, Yamaguchi S, Ito S. | 08/30/2014 |
| 3MST exists in the neurons of medullary respiratory nuclei and its expression can be up-regulated by chronic intermittent hypoxia in adult rat | Chronic intermittent hypoxia promotes expression of 3-mercaptopyruvate sulfurtransferase in adult rat medulla oblongata.
Li M, Nie L, Hu Y, Yan X, Xue L, Chen L, Zhou H, Zheng Y. | 08/9/2014 |
| SiRNA silencing of 3-MPST reduced basal bioenergetic parameters and prevented the stimulating effect of 3-MP on mitochondrial bioenergetics. | Intramitochondrial hydrogen sulfide production by 3-mercaptopyruvate sulfurtransferase maintains mitochondrial electron flow and supports cellular bioenergetics.
Módis K, Coletta C, Erdélyi K, Papapetropoulos A, Szabo C. | 03/30/2013 |
| Thus, sulfur oxides are suggested to release in the redox cycle of persulfide of mercaptopyruvate sulfurtransferase. | Is novel signal transducer sulfur oxide involved in the redox cycle of persulfide at the catalytic site cysteine in a stable reaction intermediate of mercaptopyruvate sulfurtransferase?
Nagahara N, Nirasawa T, Yoshii T, Niimura Y. | 06/16/2012 |
| 3-mercaptopyruvate sulfurtransferase (3MST) and cysteine aminotransferase (CAT) are localized to vascular endothelium in the thoracic aorta and produce hydrogen sulfide. | Vascular endothelium expresses 3-mercaptopyruvate sulfurtransferase and produces hydrogen sulfide.
Shibuya N, Mikami Y, Kimura Y, Nagahara N, Kimura H. | 02/8/2010 |
| the redox state regulates MST activity at the enzymatic level, and MST controls redox to maintain cellular redox homeostasis | Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteine-sulfenate in the maintenance of redox homeostasis.
Nagahara N, Katayama A. | 01/21/2010 |
| during thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase, an intersubunit disulfide bond serves as a redox switch for activation | Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation.
Nagahara N, Yoshii T, Abe Y, Matsumura T. | 01/21/2010 |