Reactivity of hydrogen sulfide with peroxynitrite and other oxidants of biological interest

Carballal, Sebastián; Trujillo, Madia; Cuevasanta, Ernesto; Bartesaghi, Silvina; Möller, Matías N.; Folkes, Lisa K.; García-Bereguiaín, Miguel Angel; Gutiérrez‐Merino, Carlos; Wardman, Peter; Denicola, Ana; Radí, Rafael; Álvarez, Beatriz

doi:10.1016/j.freeradbiomed.2010.10.705

Cited by 201 publications

(182 citation statements)

References 73 publications

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“…Oxygenation of the outer sulfur atom of [3] would explain the need for the second equivalent of sulfide prior to oxygen consumption. As noted previously, the rate constant for oxygenation of the sulfide radical anion at pH 7.0 and 37°C is 7.5 ϫ 10 9 M Ϫ1 s Ϫ1 (31). Hydrolysis of [5] yields the thiosulfate [6], which following oxidation would yield the ferric product complex [7].…”

mentioning

confidence: 76%

Sulfide Oxidation by a Noncanonical Pathway in Red Blood Cells Generates Thiosulfate and Polysulfides

Vitvitsky

Yadav

Kurthen

et al. 2015

Journal of Biological Chemistry

149

195

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Background: RBCs produce H 2 S but, lacking mitochondria, are devoid of the canonical sulfide oxidation pathway. Results: RBCs utilize methemoglobin to catalyze H 2 S oxidation producing thiosulfate and polysulfide. Conclusion: In the presence of NADPH and a reductase, ferric sulfide hemoglobin is converted to oxyhemoglobin, completing the sulfide oxidation cycle. Significance: We describe a novel mechanism for H 2 S oxidation that may be pertinent to other hemeproteins.

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mentioning

confidence: 76%

Sulfide Oxidation by a Noncanonical Pathway in Red Blood Cells Generates Thiosulfate and Polysulfides

Vitvitsky

Yadav

Kurthen

et al. 2015

Journal of Biological Chemistry

149

195

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“…Departments of 1 Pathology and Medical Biology, nous modulator of oxidative stress either by direct scavenging of reactive oxygen species (ROS) and nitrogen species (14) or through increasing the intracellular glutathione (GSH) pool (15,16). H 2 S also confers cytoprotection via suppression of inflammation (17) and by protecting mitochondrial function and integrity (17,18).…”

Section: Overexpression Of Cystathionine γ-Lyase Suppresses Detrimentmentioning

confidence: 99%

Overexpression of Cystathionine γ-Lyase Suppresses Detrimental Effects of Spinocerebellar Ataxia Type 3

Snijder

Baratashvili

Grzeschik

et al. 2015

Mol Med

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Spinocerebellar ataxia type 3 (SCA3) is a polyglutamine (polyQ) disorder caused by a CAG repeat expansion in the ataxin-3 (ATXN3) gene resulting in toxic protein aggregation. Inflammation and oxidative stress are considered secondary factors contributing to the progression of this neurodegenerative disease. There is no cure that halts or reverses the progressive neurodegeneration of SCA3. Here we show that overexpression of cystathionine γ-lyase, a central enzyme in cysteine metabolism, is protective in a Drosophila model for SCA3. SCA3 flies show eye degeneration, increased oxidative stress, insoluble protein aggregates, reduced levels of protein persulfidation and increased activation of the innate immune response. Overexpression of Drosophila cystathionine γ-lyase restores protein persulfidation, decreases oxidative stress, dampens the immune response and improves SCA3-associated tissue degeneration. Levels of insoluble protein aggregates are not altered; therefore, the data implicate a modifying role of cystathionine γ-lyase in ameliorating the downstream consequence of protein aggregation leading to protection against SCA3-induced tissue degeneration. The cystathionine γ-lyase expression is decreased in affected brain tissue of SCA3 patients, suggesting that enhancers of cystathionine γ-lyase expression or activity are attractive candidates for future therapies.

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“…Later, PTP1B was also reported to act in tumorigenesis, myeloid differentiation, and macrophage activation, in which it can attenuate MAPK and Akt pathways. S-nitroso-N-acetylpenicillamine (SNAP), [2] S-nitrosoglutathione (GSNO), [3] glucose-SNAP-2, [4] S-nitroso-captopril, [5] DETA-NONOate, [6] sodium nitroprusside, [7] Snitrosocysteine ethyl ester. NO, nitric oxide.…”

Section: Detection Of Ptp Sulfhydrationmentioning

confidence: 99%

“…It is hypothesized that H 2 S/HS -may interact with H 2 O 2 to generate HSSH, which could only react with the catalytic cysteine (7,50). In addition, oxidized PTP1B adopting the cyclic sulfenamide conformation is considered a potential H 2 S target (50, 75).…”

Section: Ptp1b Sulfhydrationmentioning

confidence: 99%

Reactive Nitrogen Species and Hydrogen Sulfide as Regulators of Protein Tyrosine Phosphatase Activity

Heneberg

2014

Antioxidants & Redox Signaling

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Significance: Redox modifications of thiols serve as a molecular code enabling precise and complex regulation of protein tyrosine phosphatases (PTPs) and other proteins. Particular gasotransmitters and even the redox modifications themselves affect each other, of which a typical example is S-nitrosylation-mediated protection against the further oxidation of protein thiols. Recent Advances: For a long time, PTPs were considered constitutively active housekeeping enzymes. This view has changed substantially over the last two decades, and the PTP family is now recognized as a group of tightly and flexibly regulated fundamental enzymes. In addition to the conventional ways in which they are regulated, including noncovalent interactions, phosphorylation, and oxidation, the evidence that has accumulated during the past two decades suggests that many of these enzymes are also modulated by gasotransmitters, namely by nitric oxide (NO) and hydrogen sulfide (H 2 S). Critical Issues: The specificity and selectivity of the methods used to detect nitrosylation and sulfhydration remains to be corroborated, because several researchers raised the issue of false-positive results, particularly when using the most widespread biotin switch method. Further development of robust and straightforward proteomic methods is needed to further improve our knowledge of the full extent of the gasotransmitters-mediated changes in PTP activity, selectivity, and specificity. Further Directions: Results of the hitherto performed studies on gasotransmitter-mediated PTP signaling await translation into clinical medicine and pharmacotherapeutics. In addition to directly affecting the activity of particular PTPs, the use of reversible S-nitrosylation as a protective mechanism against oxidative stress should be of high interest. Antioxid. Redox Signal. 20, 2191-2209.

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Reactivity of hydrogen sulfide with peroxynitrite and other oxidants of biological interest

Cited by 201 publications

References 73 publications

Sulfide Oxidation by a Noncanonical Pathway in Red Blood Cells Generates Thiosulfate and Polysulfides

Sulfide Oxidation by a Noncanonical Pathway in Red Blood Cells Generates Thiosulfate and Polysulfides

Overexpression of Cystathionine γ-Lyase Suppresses Detrimental Effects of Spinocerebellar Ataxia Type 3

Reactive Nitrogen Species and Hydrogen Sulfide as Regulators of Protein Tyrosine Phosphatase Activity

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