메뉴 건너뛰기




Volumn 583, Issue 13, 2009, Pages 2276-2280

NAD(P)H- and superoxide-dependent nitric oxide degradation by rat liver mitochondria

Author keywords

NAD(P)H oxidase; Nitric oxide; Rat liver mitochondria; Superoxide anion

Indexed keywords

NITRIC OXIDE; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SUCCINATE DEHYDROGENASE; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 67649378399     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.06.012     Document Type: Article
Times cited : (1)

References (23)
  • 1
    • 64749103648 scopus 로고    scopus 로고
    • The formation of peroxynitrite in the applied physiology of mitochondrial nitric oxide
    • Poderoso J.J. The formation of peroxynitrite in the applied physiology of mitochondrial nitric oxide. Arch. Biochem. Biophys. 484 (2009) 214-220
    • (2009) Arch. Biochem. Biophys. , vol.484 , pp. 214-220
    • Poderoso, J.J.1
  • 2
    • 0028134892 scopus 로고
    • Nanomolar concentrations of nitric oxide reversibly inhibits synaptosomal respiration by competing with oxygen at cytochrome oxidase
    • Brown G.C., and Cooper C.E. Nanomolar concentrations of nitric oxide reversibly inhibits synaptosomal respiration by competing with oxygen at cytochrome oxidase. FEBS Lett. 356 (1994) 295-298
    • (1994) FEBS Lett. , vol.356 , pp. 295-298
    • Brown, G.C.1    Cooper, C.E.2
  • 3
    • 0032560572 scopus 로고    scopus 로고
    • Persistent inhibition of cell respiration by nitric oxide: crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione
    • Clementi E., Brown G.C., Feelisch M., and Moncada S. Persistent inhibition of cell respiration by nitric oxide: crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione. Proc. Natl. Acad. Sci. USA 95 (1998) 7631-7636
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7631-7636
    • Clementi, E.1    Brown, G.C.2    Feelisch, M.3    Moncada, S.4
  • 4
    • 0035912784 scopus 로고    scopus 로고
    • Nitric oxide partitioning into mitochondrial membranes and the control of respiration at cytochrome c oxidase
    • Shiva S., Brookes P.S., Patel R.P., Anderson P.G., and Darley-Usmar V.M. Nitric oxide partitioning into mitochondrial membranes and the control of respiration at cytochrome c oxidase. Proc. Natl. Acad. Sci. USA 98 (2001) 7212-7217
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7212-7217
    • Shiva, S.1    Brookes, P.S.2    Patel, R.P.3    Anderson, P.G.4    Darley-Usmar, V.M.5
  • 5
    • 0036162636 scopus 로고    scopus 로고
    • Nitric oxide and cytochrome oxidase: substrate, inhibitor or effector?
    • Cooper C.E. Nitric oxide and cytochrome oxidase: substrate, inhibitor or effector?. Trends Biochem. Sci. 27 (2002) 33-39
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 33-39
    • Cooper, C.E.1
  • 6
    • 0029986691 scopus 로고    scopus 로고
    • Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles
    • Poderoso J.J., Carreras M.C., Lisdero C., Riobó N., Schöpfer F., and Boveris A. Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles. Arch. Biochem. Biophys. 328 (1996) 85-92
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 85-92
    • Poderoso, J.J.1    Carreras, M.C.2    Lisdero, C.3    Riobó, N.4    Schöpfer, F.5    Boveris, A.6
  • 7
    • 0033621429 scopus 로고    scopus 로고
    • The regulation of mitochondrial oxygen uptake by redox reactions involving nitric oxide and ubiquinol
    • Poderoso J.J., Lisdero C., Schöpfer F., Riobó N., Carreras M.C., Cadenas E., and Boveris A. The regulation of mitochondrial oxygen uptake by redox reactions involving nitric oxide and ubiquinol. J. Biol. Chem. 274 (1999) 37709-337716
    • (1999) J. Biol. Chem. , vol.274 , pp. 37709-337716
    • Poderoso, J.J.1    Lisdero, C.2    Schöpfer, F.3    Riobó, N.4    Carreras, M.C.5    Cadenas, E.6    Boveris, A.7
  • 8
    • 33744963444 scopus 로고    scopus 로고
    • Direct and indirect roles of cytochrome b in the mediation of superoxide generation and NO catabolism by mitochondrial succinate-cytochrome c reductase
    • Chen Y.R., Chen C.L., Yeh A., Liu X., and Zweier J.L. Direct and indirect roles of cytochrome b in the mediation of superoxide generation and NO catabolism by mitochondrial succinate-cytochrome c reductase. J. Biol. Chem. 281 (2006) 13159-13168
    • (2006) J. Biol. Chem. , vol.281 , pp. 13159-13168
    • Chen, Y.R.1    Chen, C.L.2    Yeh, A.3    Liu, X.4    Zweier, J.L.5
  • 9
    • 43049095110 scopus 로고    scopus 로고
    • Nitric oxide degradation by potato tuber mitochondria: evidence for the involvement of external NAD(P)H dehydrogenases
    • de Oliveira H.C., Wulff A., Saviani E.E., and Salgado I. Nitric oxide degradation by potato tuber mitochondria: evidence for the involvement of external NAD(P)H dehydrogenases. Biochim. Biophys. Acta 1777 (2008) 470-476
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 470-476
    • de Oliveira, H.C.1    Wulff, A.2    Saviani, E.E.3    Salgado, I.4
  • 10
    • 17144422877 scopus 로고    scopus 로고
    • Mitochondrial metabolism of reactive oxygen species
    • Andreyev A.Y., Kushnareva Y.E., and Starkov A.A. Mitochondrial metabolism of reactive oxygen species. Biochemistry 70 (2005) 200-214
    • (2005) Biochemistry , vol.70 , pp. 200-214
    • Andreyev, A.Y.1    Kushnareva, Y.E.2    Starkov, A.A.3
  • 11
    • 0036134932 scopus 로고    scopus 로고
    • Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases
    • Lambeth J.D. Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases. Curr. Opin. Hematol. 9 (2002) 11-17
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 11-17
    • Lambeth, J.D.1
  • 12
    • 31144469322 scopus 로고    scopus 로고
    • Cross talk between mitochondria and superoxide generating NADPH oxidase in breast and ovarian tumors
    • Desouki M.M., Kulawiec M., Bansal S., Das G.M., and Singh K.K. Cross talk between mitochondria and superoxide generating NADPH oxidase in breast and ovarian tumors. Cancer Biol. Ther. 4 (2005) 1367-1373
    • (2005) Cancer Biol. Ther. , vol.4 , pp. 1367-1373
    • Desouki, M.M.1    Kulawiec, M.2    Bansal, S.3    Das, G.M.4    Singh, K.K.5
  • 13
    • 65349088460 scopus 로고    scopus 로고
    • Cross-talk between mitochondria and NADPH oxidase: effects of mild mitochondrial dysfunction on angiotensin II-mediated increase in Nox isoform expression and activity in vascular smooth muscle cells
    • Wosniak J.J., Santos C.X., Kowaltowski A.J., and Laurindo F. Cross-talk between mitochondria and NADPH oxidase: effects of mild mitochondrial dysfunction on angiotensin II-mediated increase in Nox isoform expression and activity in vascular smooth muscle cells. Antioxid. Redox Signal. 11 (2009) 1265-1278
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 1265-1278
    • Wosniak, J.J.1    Santos, C.X.2    Kowaltowski, A.J.3    Laurindo, F.4
  • 14
    • 33846247968 scopus 로고    scopus 로고
    • Cyclosporin A inhibits calcium uptake by Citrus sinensis mitochondria
    • de Oliveira H.C., Saviani E.E., de Oliveira J.F.P., and Salgado I. Cyclosporin A inhibits calcium uptake by Citrus sinensis mitochondria. Plant Sci. 172 (2007) 665-670
    • (2007) Plant Sci. , vol.172 , pp. 665-670
    • de Oliveira, H.C.1    Saviani, E.E.2    de Oliveira, J.F.P.3    Salgado, I.4
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 0027762128 scopus 로고
    • Biological activity of S-nitrosothiols: the role of nitric oxide
    • Mathews W.R., and Kerr S.W. Biological activity of S-nitrosothiols: the role of nitric oxide. J. Pharmacol. Exp. Ther. 267 (1993) 1529-1537
    • (1993) J. Pharmacol. Exp. Ther. , vol.267 , pp. 1529-1537
    • Mathews, W.R.1    Kerr, S.W.2
  • 19
    • 0022973182 scopus 로고
    • Subcellular distribution of OM cytochrome b-mediated NADH-semidehydroascorbate reductase activity in rat liver
    • Nishino H., and Ito A. Subcellular distribution of OM cytochrome b-mediated NADH-semidehydroascorbate reductase activity in rat liver. J. Biochem. 100 (1986) 1523-1531
    • (1986) J. Biochem. , vol.100 , pp. 1523-1531
    • Nishino, H.1    Ito, A.2
  • 20
    • 0031781878 scopus 로고    scopus 로고
    • Superoxide, neuroleptics and the ubiquinone and cytochrome b5 reductases in brain and lymphocytes from normals and schizophrenic patients
    • Whatley S.A., Curti D., Das Gupta F., Ferrier I.N., Jones S., Taylor C., and Marchbanks R.M. Superoxide, neuroleptics and the ubiquinone and cytochrome b5 reductases in brain and lymphocytes from normals and schizophrenic patients. Mol. Psychiatr. 3 (1998) 227-237
    • (1998) Mol. Psychiatr. , vol.3 , pp. 227-237
    • Whatley, S.A.1    Curti, D.2    Das Gupta, F.3    Ferrier, I.N.4    Jones, S.5    Taylor, C.6    Marchbanks, R.M.7
  • 21
    • 57149125691 scopus 로고    scopus 로고
    • Clustering of plasma membrane-bound cytochrome b5 reductase within 'lipid raft' microdomains of the neuronal plasma membrane
    • Samhan-Arias A.K., Garcia-Bereguiain M.A., Martin-Romero F.J., and Gutierrez-Merino C. Clustering of plasma membrane-bound cytochrome b5 reductase within 'lipid raft' microdomains of the neuronal plasma membrane. Mol. Cell. Neurosci. 40 (2009) 14-26
    • (2009) Mol. Cell. Neurosci. , vol.40 , pp. 14-26
    • Samhan-Arias, A.K.1    Garcia-Bereguiain, M.A.2    Martin-Romero, F.J.3    Gutierrez-Merino, C.4
  • 22
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology
    • Bedard K., and Krause K.H. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol. Rev. 87 (2007) 245-313
    • (2007) Physiol. Rev. , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.