Sulfur signaling: Is the agent sulfide or sulfane?

Toohey, John I.

doi:10.1016/j.ab.2011.01.044

Cited by 259 publications

(229 citation statements)

References 69 publications

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“…Moreover, Toohey also noted that the previously implicated reaction for protein sulfhydration (protein -SH + H 2 S ? protein -SSH) is not a balanced chemical equation [26].…”

Section: Discussionmentioning

confidence: 99%

Polysulfide exerts a protective effect against cytotoxicity caused by t‐buthylhydroperoxide through Nrf2 signaling in neuroblastoma cells

et al. 2013

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a b s t r a c tPolysulfide is a bound sulfur species derived from endogenous H 2 S. When mouse neuroblastoma, Neuro2A cells were exposed to tert-butyl hydroperoxide after treatment with polysulfide, a significant decline in cell toxicity was observed. Rapid uptake of polysulfides induced translocation of Nrf2 into the nucleus, resulting in acceleration of GSH synthesis and HO-1 expression. We demonstrated that polysulfide reversibly modified Keap1 to form oxidized dimers and induced the translocation of Nrf2. Moreover, polysulfide treatment accelerated Akt phosphorylation, which is a known pathway of Nrf2 phosphorylation. Thus, polysulfide may mediate the activation of Nrf2 signaling, thereby exerting protective effects against oxidative damage in Neuro2A cells.

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“…Moreover, Toohey also noted that the previously implicated reaction for protein sulfhydration (protein -SH + H 2 S ? protein -SSH) is not a balanced chemical equation [26].…”

Section: Discussionmentioning

confidence: 99%

Polysulfide exerts a protective effect against cytotoxicity caused by t‐buthylhydroperoxide through Nrf2 signaling in neuroblastoma cells

et al. 2013

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“…These are briefly described in the next few paragraphs; detailed reviews can be found in Refs. (75,86,134,135,167,168,181,196). The downstream consequences of these initial signaling events on ion channel permeability, transport processes, enzyme activity, or structural proteins are not considered.…”

Section: Mechanism Of H 2 S Signalingmentioning

confidence: 99%

Hydrogen sulfide as an oxygen sensor

Olson

2013

Clinical Chemistry and Laboratory Medicine

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Significance: Although oxygen (O 2 )-sensing cells and tissues have been known for decades, the identity of the O 2 -sensing mechanism has remained elusive. Evidence is accumulating that O 2 -dependent metabolism of hydrogen sulfide (H 2 S) is this enigmatic O 2 sensor. Recent Advances: The elucidation of biochemical pathways involved in H 2 S synthesis and metabolism have shown that reciprocal H 2 S/O 2 interactions have been inexorably linked throughout eukaryotic evolution; there are multiple foci by which O 2 controls H 2 S inactivation, and the effects of H 2 S on downstream signaling events are consistent with those activated by hypoxia. H 2 S-mediated O 2 sensing has been demonstrated in a variety of O 2 -sensing tissues in vertebrate cardiovascular and respiratory systems, including smooth muscle in systemic and respiratory blood vessels and airways, carotid body, adrenal medulla, and other peripheral as well as central chemoreceptors. Critical Issues: Information is now needed on the intracellular location and stoichometry of these signaling processes and how and which downstream effectors are activated by H 2 S and its metabolites. Future Directions: Development of specific inhibitors of H 2 S metabolism and effector activation as well as cellular organelle-targeted compounds that release H 2 S in a timeor environmentally controlled way will not only enhance our understanding of this signaling process but also provide direction for future therapeutic applications. Antioxid. Redox Signal. 22, 377-397.

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“…Substrate specificity of the RLDs with catalytic activity is dependent on the constitution of the active site center, with either a conserved CRXGX(T/R) motif in the case of thiosulfate sulfurtransferases (EC 2.8.1.1), or a more defined CG(S/T)GV(T/S) motif in the case of MPSTs (1,5). Rhodanese-like enzymes bind sulfur in the form of persulfides, with a formal redox status of S 0 at their conserved active site cysteine residue (6,7). To date the physiological function of rhodanese-like proteins is not fully understood, but has been linked to a wide variety of biological processes, including the detoxification of cyanide, the homeostasis of cellular sulfur in general, the participation in the degradation of L-cysteine, mitochondrial production of hydrogen sulfide (H 2 S) as signaling molecule, in addition to the biosynthesis of enzymatic cofactors, vitamins, and sulfur-containing nucleic acids (8 -13).…”

mentioning

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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Sulfur signaling: Is the agent sulfide or sulfane?

Cited by 259 publications

References 69 publications

Polysulfide exerts a protective effect against cytotoxicity caused by t‐buthylhydroperoxide through Nrf2 signaling in neuroblastoma cells

Polysulfide exerts a protective effect against cytotoxicity caused by t‐buthylhydroperoxide through Nrf2 signaling in neuroblastoma cells

Hydrogen sulfide as an oxygen sensor

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

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