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Volumn 5, Issue , 2015, Pages

Identification of H2S3 and H2S produced by 3-mercaptopyruvate sulfurtransferase in the brain

Author keywords

[No Author keywords available]

Indexed keywords

3-MERCAPTOPYRUVATE SULPHURTRANSFERASE; 3-MERCAPTOPYRUVIC ACID; CYSTEINE; HYDROGEN SULFIDE; RECOMBINANT PROTEIN; SULFIDE; SULFURTRANSFERASE; THIOSULFATE SULFURTRANSFERASE;

EID: 84943311542     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep14774     Document Type: Article
Times cited : (181)

References (41)
  • 1
    • 0029876402 scopus 로고    scopus 로고
    • The possible role of hydrogen sulfide as an endogenous neuromodulator
    • Abe, K., Kimura, H. The possible role of hydrogen sulfide as an endogenous neuromodulator. J Neurosci 16, 1066-1071 (1996).
    • (1996) J Neurosci , vol.16 , pp. 1066-1071
    • Abe, K.1    Kimura, H.2
  • 2
    • 0031589557 scopus 로고    scopus 로고
    • The possible role of hydrogen sulfide as an endogenous smooth muscle relaxant in synergy with nitric oxide
    • Hosoki, R., Matsuki, N., Kimura, H. The possible role of hydrogen sulfide as an endogenous smooth muscle relaxant in synergy with nitric oxide. Biochem Biophys Res Commun 237, 527-531 (1997).
    • (1997) Biochem Biophys Res Commun , vol.237 , pp. 527-531
    • Hosoki, R.1    Matsuki, N.2    Kimura, H.3
  • 3
    • 0035503695 scopus 로고    scopus 로고
    • The vasorelaxant effect of H2S as a novel endogenous gaseous KATP channel opener
    • Zhao, W., Zhang, J., Lu, Y., Wang, R. The vasorelaxant effect of H2S as a novel endogenous gaseous KATP channel opener. EMBO J 20, 6008-6016 (2001).
    • (2001) EMBO J , vol.20 , pp. 6008-6016
    • Zhao, W.1    Zhang, J.2    Lu, Y.3    Wang, R.4
  • 4
    • 9444263079 scopus 로고    scopus 로고
    • Hydrogen sulfide protects neurons from oxidative stress
    • Kimura, Y., Kimura, H. Hydrogen sulfide protects neurons from oxidative stress. FASEB J 18, 1165-1167 (2004).
    • (2004) FASEB J , vol.18 , pp. 1165-1167
    • Kimura, Y.1    Kimura, H.2
  • 5
    • 34848828558 scopus 로고    scopus 로고
    • Hydrogen sulfide attenuates myocardial ischemia-reperfusion injury by preservation of mitochondrial function
    • Elrod, J. W. et al. Hydrogen sulfide attenuates myocardial ischemia-reperfusion injury by preservation of mitochondrial function. Proc Natl Acad Sci USA 104, 15560-15565 (2007).
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 15560-15565
    • Elrod, J.W.1
  • 6
    • 84873470505 scopus 로고    scopus 로고
    • A novel pathway for the production of hydrogen sulfide from D-cysteine in mammalian cells
    • Shibuya, N. et al., A novel pathway for the production of hydrogen sulfide from D-cysteine in mammalian cells. Nat. Commun 4, 1366 (2013).
    • (2013) Nat. Commun , vol.4 , pp. 1366
    • Shibuya, N.1
  • 7
    • 84875910694 scopus 로고    scopus 로고
    • Sulfhydration mediates neuroprotective actions of parkin
    • Vandiver, M. S. et al. Sulfhydration mediates neuroprotective actions of parkin. Nat Commun 4, 1626 (2013).
    • (2013) Nat Commun , vol.4 , pp. 1626
    • Vandiver, M.S.1
  • 8
    • 0028008735 scopus 로고
    • Characterization of a trisulphide derivative of biosynthetic human growth hormone produced in Escherichia coli
    • Jespersen, A. M. et al. Characterization of a trisulphide derivative of biosynthetic human growth hormone produced in Escherichia coli. Eur J Biochem 219, 365-373 (1994).
    • (1994) Eur J Biochem , vol.219 , pp. 365-373
    • Jespersen, A.M.1
  • 9
    • 76749156792 scopus 로고    scopus 로고
    • Characterization of a covalent polysulfane bridge in copper-zinc superoxide dismutase
    • You, Z. et al. Characterization of a covalent polysulfane bridge in copper-zinc superoxide dismutase. Biochemistry 49, 1191-1198 (2010).
    • (2010) Biochemistry , vol.49 , pp. 1191-1198
    • You, Z.1
  • 10
    • 10544244908 scopus 로고
    • Enzymatic formation of polysulfides from mercaptopyruvate
    • Hylin, J. W., Wood, J. L. Enzymatic formation of polysulfides from mercaptopyruvate. J Biol Chem 234, 2141-2144 (1959).
    • (1959) J Biol Chem , vol.234 , pp. 2141-2144
    • Hylin, J.W.1    Wood, J.L.2
  • 11
    • 84878758877 scopus 로고    scopus 로고
    • Polysulfides induce calcium waves in rat hippocampal astrocytes
    • Nagai, Y., Tsugane, M., Oka, J.-I., Kimura, H. Polysulfides induce calcium waves in rat hippocampal astrocytes. J Pharmacol Sci 100, 200 (2006).
    • (2006) J Pharmacol Sci , vol.100 , pp. 200
    • Nagai, Y.1    Tsugane, M.2    Oka, J.-I.3    Kimura, H.4
  • 12
    • 84911948141 scopus 로고    scopus 로고
    • Polysulfide activates TRP channels and increases intracellular Ca2+ in astrocytes
    • Oosumi, K., et al. Polysulfide activates TRP channels and increases intracellular Ca2+ in astrocytes. Neurosci Res 685, e109-e222 (2010).
    • (2010) Neurosci Res , vol.685 , pp. e109-e222
    • Oosumi, K.1
  • 13
    • 84878764595 scopus 로고    scopus 로고
    • Polysulfides are possible H2S-derived signaling molecules in rat brain
    • Kimura, Y. et al. Polysulfides are possible H2S-derived signaling molecules in rat brain. FASEB J 27, 2451-2457 (2013).
    • (2013) FASEB J , vol.27 , pp. 2451-2457
    • Kimura, Y.1
  • 14
    • 84879651400 scopus 로고    scopus 로고
    • Antioxidant enzyme, 3-mercaptopyruvate sulfurtransferase-knockout mice exhibit increased anxiety-like behaviors: A model for human mercaptolactate-cysteine disulfiduria
    • Nagahara, N. et al. Antioxidant enzyme, 3-mercaptopyruvate sulfurtransferase-knockout mice exhibit increased anxiety-like behaviors: a model for human mercaptolactate-cysteine disulfiduria. Scientific Reports 3, 1986 (2013).
    • (2013) Scientific Reports , vol.3 , pp. 1986
    • Nagahara, N.1
  • 15
    • 84906830179 scopus 로고    scopus 로고
    • The blockade of transient receptor potential ankirin 1 (TRPA1) signaling mediates antidepressantand anxiolytic-like actions in mice
    • Cavalcante de Moura, J. et al. The blockade of transient receptor potential ankirin 1 (TRPA1) signaling mediates antidepressantand anxiolytic-like actions in mice. Br J Pharm 171, 4289-4299 (2014).
    • (2014) Br J Pharm , vol.171 , pp. 4289-4299
    • Cavalcante De Moura, J.1
  • 16
    • 84886243717 scopus 로고    scopus 로고
    • Polysulfide exerts a protective effect against cytotoxicity caused by t-buthylhydroperoxide through Nrf2 signaling in neuroblastoma cells
    • Koike, S. et al. Polysulfide exerts a protective effect against cytotoxicity caused by t-buthylhydroperoxide through Nrf2 signaling in neuroblastoma cells. FEBS lett 587, 3548-3555 (2013).
    • (2013) FEBS Lett , vol.587 , pp. 3548-3555
    • Koike, S.1
  • 17
    • 84886255283 scopus 로고    scopus 로고
    • Polysulfides link H2S to protein thiol oxidation
    • Greiner, R. et al. Polysulfides link H2S to protein thiol oxidation. Antioxid Redox Signal 19, 1749-1765 (2013).
    • (2013) Antioxid Redox Signal , vol.19 , pp. 1749-1765
    • Greiner, R.1
  • 18
    • 84927785706 scopus 로고    scopus 로고
    • Protein kinase G Ialpha oxidation paradoxically underlies blood pressure lowering by the reductant hydrogen sulfide
    • Stubbert, D. et al. Protein kinase G Ialpha oxidation paradoxically underlies blood pressure lowering by the reductant hydrogen sulfide. Hypertension 64, 1344-1351 (2014).
    • (2014) Hypertension , vol.64 , pp. 1344-1351
    • Stubbert, D.1
  • 19
    • 60749088329 scopus 로고    scopus 로고
    • 3-Mercaptopyruvate sulfurtransferease produces hydrogen sulfide and bound sulfane sulfur in the brain
    • Shibuya, N. et al. 3-Mercaptopyruvate sulfurtransferease produces hydrogen sulfide and bound sulfane sulfur in the brain. Antioxid Redox Signal 11, 703-714 (2009).
    • (2009) Antioxid Redox Signal , vol.11 , pp. 703-714
    • Shibuya, N.1
  • 20
    • 84905247104 scopus 로고    scopus 로고
    • Controversies and conundrums in hydrogen sulfide biology
    • Olson, K. R., DeLeon E. R., Liu, F. Controversies and conundrums in hydrogen sulfide biology. Nitric Oxide 41, 11-26 (2014).
    • (2014) Nitric Oxide , vol.41 , pp. 11-26
    • Olson, K.R.1    DeLeon, E.R.2    Liu, F.3
  • 21
    • 84929031571 scopus 로고    scopus 로고
    • Hydrogen sulfide-based therapeutics: Exploiting a unique but ubiquitous gasotransmitter
    • Wallace, J. L., Wang, R. Hydrogen sulfide-based therapeutics: exploiting a unique but ubiquitous gasotransmitter. Nat. Rev. Drug Discov. 14, 329-345 (2015).
    • (2015) Nat. Rev. Drug Discov. , vol.14 , pp. 329-345
    • Wallace, J.L.1    Wang, R.2
  • 22
    • 84907597056 scopus 로고    scopus 로고
    • Hydrogen sulfide measurement using sulfide dibimane: Critical evalutation with electrospray ion trap mass spectrometry
    • Shen, X. et al. Hydrogen sulfide measurement using sulfide dibimane: Critical evalutation with electrospray ion trap mass spectrometry. Nitric Oxide 41, 97-104 (2014).
    • (2014) Nitric Oxide , vol.41 , pp. 97-104
    • Shen, X.1
  • 23
    • 0029003927 scopus 로고
    • Cytosolic mercaptopyruvate sulfurtransferase is evolutionarily related to mitochondrial rhodanese. Striking similarity in active site amino acid sequence and the increase in the mercaptopyruvate sulfurtransferase activity of rhodanese by site-directed mutagenesis
    • Nagahara, N., Okazaki, T., Nishino, T. Cytosolic mercaptopyruvate sulfurtransferase is evolutionarily related to mitochondrial rhodanese. Striking similarity in active site amino acid sequence and the increase in the mercaptopyruvate sulfurtransferase activity of rhodanese by site-directed mutagenesis. J Biol Chem 270, 16230-16235 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 16230-16235
    • Nagahara, N.1    Okazaki, T.2    Nishino, T.3
  • 24
    • 80054015725 scopus 로고    scopus 로고
    • Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide
    • Mikami, Y. et al. Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide. Biochm J 439, 479-485 (2011).
    • (2011) Biochm J , vol.439 , pp. 479-485
    • Mikami, Y.1
  • 25
    • 84878793080 scopus 로고    scopus 로고
    • New fluorescent probes for sulfane sulfurs and the application in bioimaging
    • Chen, W. et al. New fluorescent probes for sulfane sulfurs and the application in bioimaging. Chem. Sci. 4, 2892-2896 (2013).
    • (2013) Chem. Sci. , vol.4 , pp. 2892-2896
    • Chen, W.1
  • 26
    • 77958095282 scopus 로고    scopus 로고
    • Rapid reaction of hydrogen sulfide with the neutrophil oxidant hypochlorous acid to generate polysulfides
    • Nagy, P., Winterbourn, C. C. Rapid reaction of hydrogen sulfide with the neutrophil oxidant hypochlorous acid to generate polysulfides. Chem Res Toxicol 23, 1541-1543 (2010).
    • (2010) Chem Res Toxicol , vol.23 , pp. 1541-1543
    • Nagy, P.1    Winterbourn, C.C.2
  • 27
    • 74949103637 scopus 로고    scopus 로고
    • H2S signals through protein S-sulfhydration
    • Mustafa, A. K. et al. H2S signals through protein S-sulfhydration. Sci Signal 2, ra72 (2009).
    • (2009) Sci Signal , vol.2 , pp. 72
    • Mustafa, A.K.1
  • 28
    • 79953712285 scopus 로고    scopus 로고
    • Sulfur signaling: Is the agent sulfide or sulfane
    • Toohey, J. I. Sulfur signaling: Is the agent sulfide or sulfane? Anal Biochem 413, 1-7 (2011).
    • (2011) Anal Biochem , vol.413 , pp. 1-7
    • Toohey, J.I.1
  • 29
    • 0013868205 scopus 로고
    • Control mechanism in the rat liver enzyme system converting L-methionine to L-cystine. 3. Noncompetitive inhibition of cystathionine synthetase-serine dehydratase by elemental sulfur and competitive inhibition of cystathionine-homoserine dehydratase by L-cysteine and L-cystine
    • Kato, A., Ogura, M., Suda, M. Control mechanism in the rat liver enzyme system converting L-methionine to L-cystine. 3. Noncompetitive inhibition of cystathionine synthetase-serine dehydratase by elemental sulfur and competitive inhibition of cystathionine-homoserine dehydratase by L-cysteine and L-cystine. J Biochem 59, 40-48 (1966).
    • (1966) J Biochem , vol.59 , pp. 40-48
    • Kato, A.1    Ogura, M.2    Suda, M.3
  • 30
    • 0016156485 scopus 로고
    • Evidence for an active site persulfide residue in rabbit liver aldehyde oxidase
    • Branzoli, U., Massey, V. Evidence for an active site persulfide residue in rabbit liver aldehyde oxidase. J Biol Chem 249, 4346-4349 (1974).
    • (1974) J Biol Chem , vol.249 , pp. 4346-4349
    • Branzoli, U.1    Massey, V.2
  • 31
    • 0021116479 scopus 로고
    • Elemental sulfur: A novel inhibitor of adenylate kinase
    • Conner, J., Russell, P. J. Elemental sulfur: a novel inhibitor of adenylate kinase. Biochem Biophys Res Commun 113, 348-352 (1983).
    • (1983) Biochem Biophys Res Commun , vol.113 , pp. 348-352
    • Conner, J.1    Russell, P.J.2
  • 32
    • 81355127489 scopus 로고    scopus 로고
    • Hydrogen sulfide as endothelium-derived hyperpolarizing factor sulfhydrates potassium channels
    • Mustafa, A. K. et al. Hydrogen sulfide as endothelium-derived hyperpolarizing factor sulfhydrates potassium channels. Circ Res 109, 1259-1268 (2011).
    • (2011) Circ Res , vol.109 , pp. 1259-1268
    • Mustafa, A.K.1
  • 33
    • 83655165310 scopus 로고    scopus 로고
    • H2S-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response
    • Krishnan, N., Fu, C., Pappin, D. J., Tonks, N. K. H2S-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response. Sci Signal 4, ra86 (2011).
    • (2011) Sci Signal , vol.4 , pp. 86
    • Krishnan, N.1    Fu, C.2    Pappin, D.J.3    Tonks, N.K.4
  • 34
    • 84875910694 scopus 로고    scopus 로고
    • Sulfhydration mediates neuroprotective actions of parkin
    • Vandiver, M. S. et al. Sulfhydration mediates neuroprotective actions of parkin. Nat Commun 4, 1626 (2013).
    • (2013) Nat Commun , vol.4 , pp. 1626
    • Vandiver, M.S.1
  • 35
    • 84921904030 scopus 로고    scopus 로고
    • Signaling molecules: Hydrogen sulfide and polysulfides
    • Kimura, H. Signaling molecules: hydrogen sulfide and polysulfides. Antioxid. Redox. Signal. 22, 362-376 (2015).
    • (2015) Antioxid. Redox. Signal. , vol.22 , pp. 362-376
    • Kimura, H.1
  • 36
    • 84921918209 scopus 로고    scopus 로고
    • S-Glutathionylation enhances human cystathionine ?-synthase activity under oxidative stress conditions
    • Niu, W. N. et al. S-Glutathionylation enhances human cystathionine ?-synthase activity under oxidative stress conditions. Antioxid Redox Signal 22, 350-361 (2015).
    • (2015) Antioxid Redox Signal , vol.22 , pp. 350-361
    • Niu, W.N.1
  • 37
    • 84929146397 scopus 로고    scopus 로고
    • Polysulfide evokes acute pain through the activation of nociceptive TRPA1 in mouse sensory neurons
    • Hatakeyama, Y. et al. Polysulfide evokes acute pain through the activation of nociceptive TRPA1 in mouse sensory neurons. Mol. Pain 11, 24 (2015).
    • (2015) Mol. Pain , vol.11 , pp. 24
    • Hatakeyama, Y.1
  • 38
    • 84934905709 scopus 로고    scopus 로고
    • Biogenesis of reactive sulfur species for signaling by hydrogen sulfide oxidation pathways
    • Mishanina, T. V., Libiad, M., Banerjee, R. Biogenesis of reactive sulfur species for signaling by hydrogen sulfide oxidation pathways. Nat. Chem. Biol. 11, 457-464 (2015).
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 457-464
    • Mishanina, T.V.1    Libiad, M.2    Banerjee, R.3
  • 39
    • 84874575518 scopus 로고    scopus 로고
    • VEGFR2 functions as an H2S-targeting receptor protein kinase with its novel Cys1045-Cys1024 disulfide bond serving as a specific molecular switch for hydrogen sulfide actions in vascular endothelial cells
    • Tao, B. B. et al. VEGFR2 functions as an H2S-targeting receptor protein kinase with its novel Cys1045-Cys1024 disulfide bond serving as a specific molecular switch for hydrogen sulfide actions in vascular endothelial cells. Antioxid Redox Signal 19, 448-464 (2013).
    • (2013) Antioxid Redox Signal , vol.19 , pp. 448-464
    • Tao, B.B.1
  • 40
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D. B., Johnson, K. S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67, 31-40 (1988).
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 41
    • 0019866781 scopus 로고
    • An improved method for the bulk isolation of viable perikarya from postnatal cerebellum
    • Dutton, G. R. et al. An improved method for the bulk isolation of viable perikarya from postnatal cerebellum. J. Neurosci. Methods 3, 421-427 (1981).
    • (1981) J. Neurosci. Methods , vol.3 , pp. 421-427
    • Dutton, G.R.1


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