Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis

Nagahara, Noriyuki; Ito, Takaaki; Kitamura, Hitoshi; Nishino, Tokuzo

doi:10.1007/s004180050286

Cited by 196 publications

(182 citation statements)

References 26 publications

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“…Alternatively, H 2 S can be released from TUM1 in the presence of reducing systems like thioredoxin or glutathione (45,46). Inhibition of TUM1 conserves cysteine and contributes to an increase in the cysteine pool (47,48). An increase in the cysteine content in the cell results in an increase in the content of cellular reductants such as thioredoxin or glutathione.…”

Section: Discussionmentioning

confidence: 99%

Characterization and Interaction Studies of Two Isoforms of the Dual Localized 3-Mercaptopyruvate Sulfurtransferase TUM1 from Humans

Fräsdorf

Radon

Leimkühler

2014

Journal of Biological Chemistry

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Background: Localization and identification of interaction partners of two splice variants of the human 3-mercaptopyruvate sulfurtransferase TUM1. Results: We show that TUM1 interacts with proteins involved in Moco and FeS cluster biosynthesis. Conclusion: Human TUM1 is a dual localized protein in the cytosol and mitochondria with distinct roles in sulfur transfer and interaction partners. Significance: The study contributes to the sulfur transfer pathway for the biosynthesis of sulfur-containing biofactors.

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Section: Discussionmentioning

confidence: 99%

Characterization and Interaction Studies of Two Isoforms of the Dual Localized 3-Mercaptopyruvate Sulfurtransferase TUM1 from Humans

Fräsdorf

Radon

Leimkühler

2014

Journal of Biological Chemistry

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“…3f,g). As H 2 S-producing enzymes, CBS, CSE and 3MST along with DAO are localized to the renal cortex [33][34][35][36] , the administration of D-cysteine or L-cysteine protects the renal cortex but not the medulla (Fig. 3f,g).…”

Section: Article Nature Communications | Doi: 101038/ncomms2371mentioning

confidence: 99%

A novel pathway for the production of hydrogen sulfide from D-cysteine in mammalian cells

et al. 2013

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In eukaryotes, hydrogen sulphide acts as a signalling molecule and cytoprotectant. Hydrogen sulphide is known to be produced from L-cysteine by cystathionine b-synthase, cystathionine g-lyase and 3-mercaptopyruvate sulfurtransferase coupled with cysteine aminotransferase. Here we report an additional biosynthetic pathway for the production of hydrogen sulphide from D-cysteine involving 3-mercaptopyruvate sulfurtransferase and D-amino acid oxidase. Unlike the L-cysteine pathway, this D-cysteine-dependent pathway operates predominantly in the cerebellum and the kidney. Our study reveals that administration of D-cysteine protects primary cultures of cerebellar neurons from oxidative stress induced by hydrogen peroxide and attenuates ischaemia-reperfusion injury in the kidney more than L-cysteine. This study presents a novel pathway of hydrogen sulphide production and provides a new therapeutic approach to deliver hydrogen sulphide to specific tissues.

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“…MST is present in both the cytoplasmic and the mitochondrial compartments (17). CBS and CSE are cytoplasmic but might also be in the nucleus under some conditions because they are both substrates for sumoylation (18).…”

Section: Biogenesis Of H 2 Smentioning

confidence: 99%

Redox Biochemistry of Hydrogen Sulfide

Kabil

Banerjee

2010

Journal of Biological Chemistry

670

526

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H 2 S, the most recently discovered gasotransmitter, might in fact be the evolutionary matriarch of this family, being both ancient and highly reduced. Disruption of ␥-cystathionase in mice leads to cardiovascular dysfunction and marked hypertension, suggesting a key role for this enzyme in H 2 S production in the vasculature. However, patients with inherited deficiency in ␥-cystathionase apparently do not present vascular pathology. A mitochondrial pathway disposes sulfide and couples it to oxidative phosphorylation while also exposing cytochrome c oxidase to this metabolic poison. This report focuses on the biochemistry of H 2 S biogenesis and clearance, on the molecular mechanisms of its action, and on its varied biological effects.Sulfur cycles through several biologically relevant oxidation states ranging from Ϫ2 as in hydrogen and metal sulfides to ϩ6 in sulfate. H 2 S, a colorless gas with the odor of rotten eggs, is important in the biogeochemical sulfur cycle and is used as an energy source by microbes such as the purple and green sulfur bacteria. It is a weak acid with pK a1 and pK a2 of 6.9 and Ͼ12 (1) and an aqueous solubility of ϳ80 mM at 37°C. Hence, at the physiological pH of 7.4, the ratio of HS Ϫ :H 2 S is 3:1. For brevity, H 2 S is used to refer to the total free sulfide pool (i.e. H 2 S ϩ HS Ϫ ϩ S 2Ϫ ) in this report unless noted otherwise. The ready ionization of H 2 S at physiological pH suggests impeded permeation through the lipid bilayer when compared with other gases, viz. NO or CO. On the other hand, transport of the gas, H 2 S, across the membrane does not appear to be facilitated (2).The toxicity of H 2 S is thought to have influenced evolution. The presence of a metastable H 2 S-enriched oceanic stratum is postulated to have limited early metazoan colonization of the continental shelf (3), and an increase in H 2 S has been implicated in the Permian-Triassic extinction Ͼ250 million years ago (4). However, the reputation of H 2 S as a toxic gas is enjoying a facelift, with increasing numbers of reports that it modulates a range of biological processes. Despite the rising interest in H 2 S biochemistry, fundamental questions regarding regulation of its production, its mechanism of action, and its destruction remain. In addition, perhaps most critical to the field is the issue of what constitutes biologically relevant levels of H 2 S with reports varying over a 10 5 -fold concentration range. Using a gas chromatography-based chemiluminescent sulfur detection method, free H 2 S (H 2 S ϩ HS Ϫ ) in blood was estimated to be ϳ100 pM, and in tissues, it was estimated to be ϳ15 nM (5). These values are considerably lower than the ϳ30 -300 M concentrations reported in a spate of recent studies (reviewed in Ref. 6). The high values can be ascribed to technical artifacts introduced by long processing times and harsh (either acidic or alkaline) conditions used to shift the equilibrium toward H 2 S or S 2Ϫ , respectively. Under these conditions, sulfide leaches from iron-sulfur cluster-containing p...

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Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis

Cited by 196 publications

References 26 publications

Characterization and Interaction Studies of Two Isoforms of the Dual Localized 3-Mercaptopyruvate Sulfurtransferase TUM1 from Humans

Characterization and Interaction Studies of Two Isoforms of the Dual Localized 3-Mercaptopyruvate Sulfurtransferase TUM1 from Humans

A novel pathway for the production of hydrogen sulfide from D-cysteine in mammalian cells

Redox Biochemistry of Hydrogen Sulfide

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