Examining the reaction of NO and H
            <sub>2</sub>
            S and the possible cross-talk between the two signaling pathways

Bianco, Christopher L.; Fukuto, Jon M.

doi:10.1073/pnas.1513510112

Cited by 22 publications

(13 citation statements)

References 12 publications

(9 reference statements)

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“…In mammals these two enzymes are the major sources of intracellular H 2 S production (Figs 4 & 5) [126]. H 2 S is now recognized as an important signaling molecule in animals, akin to NO and H 2 O 2 [142–144]. It can exert its effects through post- and pre-translational modifications of protein-Cys residues, resulting in protein- or metabolite- S- persulfides (R- SS H; [127, 145, 146]).…”

Section: Flux-direction In the Transsulfuration Pathwaymentioning

confidence: 99%

NADPH-dependent and -independent disulfide reductase systems

Miller

Holmgren

Arnér

et al. 2018

Free Radical Biology and Medicine

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Summary Over the past seven decades, research on autotrophic and heterotrophic model organisms has defined how the flow of electrons (“reducing power”) from high-energy inorganic sources, through biological systems, to low-energy inorganic products like water, powers all of Life’s processes. Universally, an initial major biological recipient of these electrons is nicotinamide adenine dinucleotide-phosphate, which thereby transits from an oxidized state (NADP+) to a reduced state (NADPH). A portion of this reducing power is then distributed via the cellular NADPH-dependent disulfide reductase systems as sequential reductions of disulfide bonds. Along the disulfide reduction pathways, some enzymes have active sites that use the selenium-containing amino acid, selenocysteine, in place of the common but less reactive sulfur-containing cysteine. In particular, the mammalian/metazoan thioredoxin systems are usually selenium-dependent as, across metazoan phyla, most thioredoxin reductases are selenoproteins. Among the roles of the NADPH-dependent disulfide reductase systems, the most universal is that they provide the reducing power for the production of DNA precursors by ribonucleotide reductase (RNR). Some studies, however, have uncovered examples of NADPH-independent disulfide reductase systems that can also support RNR. These systems are summarized here and their implications are discussed.

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Section: Flux-direction In the Transsulfuration Pathwaymentioning

confidence: 99%

NADPH-dependent and -independent disulfide reductase systems

Miller

Holmgren

Arnér

et al. 2018

Free Radical Biology and Medicine

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“…Âàaeëèâèì á³îðåãóëÿòîðîì ó ïîïåðå-äaeåíí³ ðîçâèòêó àðòåð³éíî¿ ã³ïåðòåíç³¿ º ñ³ðêîâîäåíü, ÿêèé òàêîae ïðèéìàº ó÷àñòü â ðå´ó-ëÿö³¿ êë³òèííîãî îêèñíî-â³äíîâíîãî ãîìåîñòàçó, ãàëüìóþ÷è íàñë³äêè îêèñíîãî ñòðåñó. Ñ³ðêîâîäåíü ³íäóêóº ïðîäóêö³þ åíäîòåë³éíî¿ ñèíòàçè, ùî ñïðèÿº âàçîäèëÿòàö³¿ [4].…”

Section: âñòóïunclassified

The changes of some indicators of endothelial dysfunction in response to physical activity in individuals with arterial hypertension

Dronyk

Yavorsky

Sklyarov

et al. 2019

AML

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Ëüâ³âñüêèé íàö³îíàëüíèé ìåäè÷íèé óí³âåðñèòåò ³ìåí³ Äàíèëà Ãàëèöüêîãî 1 Êàôåäðà ïðîïåäåâòèêè âíóòð³øíüî¿ ìåäèöèíè ¹2 (çàâ.-ïðîô. Äóäêà Ð.ß.) 2 Êàôåäðà á³îõ³ì³¿ (çàâ.-ïðîô. Ñêëÿðîâ Î.ß.) 3 Êàôåäðà íåâðîëî´³¿ (çàâ. ïðîô. Íåãðè÷ Ò.².) Ðåôåðàò Ìåòà. Âèçíà÷èòè í³òðîçî-îêñèäàòèâíèé ñòàí, âì³ñò ñ³ðêîâîäíþ òà êîðòèçîëó â ñèðîâàòö³ êðîâ³ ó îñ³á ç àðòåð³éíîþ ã³ïåðòåíç³ºþ ²² ñòàä³¿ çà óìîâ ô³çè÷íîãî íàâàíòàaeåííÿ. Ìàòåð³àë ³ ìåòîäè. Îáñòåaeåíî 30 îñ³á ç àðòåð³éíîþ ã³ïåðòåíç³ºþ ²² ñòàä³¿. Îáñòåaeóâàí³ îñîáè âèêîíóâàëè íà âåëîåðãîìåòð³ äâîñòóïåíåâå ô³çè÷íå íàâàíòàaeåííÿ ç ³íòåíñèâí³ñòþ, ÿêà â³äïîâ³äàëà 50 ³ 75 % íàëåaeíîãî ìàêñèìàëüíîãî ñïîaeèâàííÿ êèñíþ îð´à-í³çìîì. Ðåçóëüòàòè é îáãîâîðåííÿ. Ó ñèðîâàòö³ êðîâ³ ïàö³-ºíò³â äî òà ï³ñëÿ ô³çè÷íîãî íàâàíòàaeåííÿ âèçíà÷àëè âì³ñò ÒÁÊ-àêòèâíèõ ïðîäóêò³â, ñ³ðêîâîäíþ, L-àðã³-í³íó, í³òðèò-àí³îíó, ñóìó í³òðèò³â òà í³òðàò³â, êîðòèçîëó, àêòèâí³ñòü ÑÎÄ, êàòàëàçè, àðã³íàçè. Â³äì³-÷åíî â³ðîã³äíå çá³ëüøåííÿ L-àðã³í³íó òà ñ³ðêîâîäíþ íà òë³ çìåíøåííÿ âì³ñòó í³òðèò-àí³îíó. Âèñëîâëåíî ïðèïóùåííÿ, ùî â îñ³á ç ã³ïåðòîí³÷íîþ õâîðîáîþ çà âïëèâó ô³çè÷íîãî íàâàíòàaeåííÿ çíèaeóºòüñÿ ñèíòåç NO, à âàçîäèëàòàö³ÿ òà âàçîïðîòåêö³ÿ çä³éñíþþòüñÿ çà ðàõóíîê ï³äâèùåííÿ ð³âíÿ ñ³ðêîâîäíþ. Âèñíîâêè. Ï³äâèùåííÿ ð³âíÿ L-àðã³í³íó ³ ñ³ðêîâîäíþ òà çíèaeåííÿ ð³âíÿ í³òðèò-àí³îíó ìîaeíà ââàaeàòè ìàðêåðàìè îö³íêè íåãàéíèõ çì³í ó ïàö³ºíò³â ç àðòå-ð³éíîþ ã³ïåðòåíç³ºþ ï³ñëÿ ô³çè÷íîãî íàâàíòàaeåííÿ. Øâèäê³ñòü ðåàãóâàííÿ ôåðìåíòíèõ ñèñòåì ó â³äïî-â³äü íà ô³çè÷íå íàâàíòàaeåííÿ ó ïàö³ºíò³â ïðè ï³ä-âèùåíí³ àðòåð³éíîãî òèñêó º ð³çíîþ.

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“…Both NO and H 2 S are important gasotransmitters and regulate diverse physiological functions through interaction [ 62 , 63 , 64 ]. H 2 S influences NO production and its metabolites by affecting NO synthase, and NO is also shown to alter H 2 S bioavailability by acting on H 2 S-generating enzymes.…”

Section: Potential Forming Mechanisms Of Protein S mentioning

confidence: 99%

H2S-Mediated Protein S-Sulfhydration: A Prediction for Its Formation and Regulation

Stokes

et al. 2017

Molecules

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Protein S-sulfhydration is a newly discovered post-translational modification of specific cysteine residue(s) in target proteins, which is involved in a broad range of cellular functions and metabolic pathways. By changing local conformation and the final activity of target proteins, S-sulfhydration is believed to mediate most cellular responses initiated by H2S, a novel gasotransmitter. In comparison to protein S-sulfhydration, nitric oxide-mediated protein S-nitrosylation has been extensively investigated, including its formation, regulation, transfer and metabolism. Although the investigation on the regulatory mechanisms associated with protein S-sulfhydration is still in its infancy, accumulated evidence suggested that protein S-sulfhydration may share similar chemical features with protein S-nitrosylation. Glutathione persulfide acts as a major donor for protein S-sulfhydration. Here, we review the present knowledge on protein S-sulfhydration, and also predict its formation and regulation mechanisms based on the knowledge from protein S-nitrosylation.

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Examining the reaction of NO and H ₂ S and the possible cross-talk between the two signaling pathways

Cited by 22 publications

References 12 publications

NADPH-dependent and -independent disulfide reductase systems

NADPH-dependent and -independent disulfide reductase systems

The changes of some indicators of endothelial dysfunction in response to physical activity in individuals with arterial hypertension

H2S-Mediated Protein S-Sulfhydration: A Prediction for Its Formation and Regulation

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Examining the reaction of NO and H 2 S and the possible cross-talk between the two signaling pathways

Cited by 22 publications

References 12 publications

NADPH-dependent and -independent disulfide reductase systems

NADPH-dependent and -independent disulfide reductase systems

The changes of some indicators of endothelial dysfunction in response to physical activity in individuals with arterial hypertension

H2S-Mediated Protein S-Sulfhydration: A Prediction for Its Formation and Regulation

Contact Info

Product

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Examining the reaction of NO and H ₂ S and the possible cross-talk between the two signaling pathways