메뉴 건너뛰기




Volumn 394, Issue 3, 2010, Pages 448-452

Arginase activity in mitochondria - An interfering factor in nitric oxide synthase activity assays

Author keywords

Arginase; Mitochondria; Nitric oxide synthase

Indexed keywords

ACETONE; ARGINASE; ARGININE; CARBON 14; CITRULLINE; NITRIC OXIDE SYNTHASE; UREA;

EID: 77950516393     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.10.169     Document Type: Article
Times cited : (10)

References (39)
  • 1
    • 67749147469 scopus 로고    scopus 로고
    • Absence of nitric-oxide synthase in sequentially purified rat liver mitochondria
    • Venkatakrishnan P., Nakayasu E.S., Almeida I.C., and Miller R.T. Absence of nitric-oxide synthase in sequentially purified rat liver mitochondria. J. Biol. Chem. 284 (2009) 19843-19855
    • (2009) J. Biol. Chem. , vol.284 , pp. 19843-19855
    • Venkatakrishnan, P.1    Nakayasu, E.S.2    Almeida, I.C.3    Miller, R.T.4
  • 2
    • 0024537028 scopus 로고
    • Endothelium-derived nitric oxide: actions and properties
    • Ignarro L.J. Endothelium-derived nitric oxide: actions and properties. FASEB J. 3 (1989) 31-36
    • (1989) FASEB J. , vol.3 , pp. 31-36
    • Ignarro, L.J.1
  • 3
    • 0023676959 scopus 로고
    • Endothelium-derived relaxing factor and nitric oxide possess identical pharmacologic properties as relaxants of bovine arterial and venous smooth muscle
    • Ignarro L.J., Buga G.M., Byrns R.E., Wood K.S., and Chaudhuri G. Endothelium-derived relaxing factor and nitric oxide possess identical pharmacologic properties as relaxants of bovine arterial and venous smooth muscle. J. Pharmacol. Exp. Ther. 246 (1988) 218-226
    • (1988) J. Pharmacol. Exp. Ther. , vol.246 , pp. 218-226
    • Ignarro, L.J.1    Buga, G.M.2    Byrns, R.E.3    Wood, K.S.4    Chaudhuri, G.5
  • 4
    • 0024390169 scopus 로고
    • Endothelium-derived relaxing and contracting factors
    • Furchgott R.F., and Vanhoutte P.M. Endothelium-derived relaxing and contracting factors. FASEB J. 3 (1989) 2007-2018
    • (1989) FASEB J. , vol.3 , pp. 2007-2018
    • Furchgott, R.F.1    Vanhoutte, P.M.2
  • 5
    • 0026071876 scopus 로고
    • Calmodulin-dependent endothelium-derived relaxing factor/nitric oxide synthase activity is present in the particulate and cytosolic fractions of bovine aortic endothelial cells
    • Forstermann U., Pollock J.S., Schmidt H.H., Heller M., and Murad F. Calmodulin-dependent endothelium-derived relaxing factor/nitric oxide synthase activity is present in the particulate and cytosolic fractions of bovine aortic endothelial cells. Proc. Natl. Acad. Sci. USA 88 (1991) 1788-1792
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1788-1792
    • Forstermann, U.1    Pollock, J.S.2    Schmidt, H.H.3    Heller, M.4    Murad, F.5
  • 7
    • 0025750850 scopus 로고
    • Purification and characterization of particulate endothelium-derived relaxing factor synthase from cultured and native bovine aortic endothelial cells
    • Pollock J.S., Forstermann U., Mitchell J.A., Warner T.D., Schmidt H.H., Nakane M., and Murad F. Purification and characterization of particulate endothelium-derived relaxing factor synthase from cultured and native bovine aortic endothelial cells. Proc. Natl. Acad. Sci. USA 88 (1991) 10480-10484
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10480-10484
    • Pollock, J.S.1    Forstermann, U.2    Mitchell, J.A.3    Warner, T.D.4    Schmidt, H.H.5    Nakane, M.6    Murad, F.7
  • 8
    • 0343046540 scopus 로고
    • Formation of nitric oxide from l-arginine in the central nervous system: a transduction mechanism for stimulation of the soluble guanylate cyclase
    • Knowles R.G., Palacios M., Palmer R.M., and Moncada S. Formation of nitric oxide from l-arginine in the central nervous system: a transduction mechanism for stimulation of the soluble guanylate cyclase. Proc. Natl. Acad. Sci. USA 86 (1989) 5159-5162
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5159-5162
    • Knowles, R.G.1    Palacios, M.2    Palmer, R.M.3    Moncada, S.4
  • 10
    • 0025191219 scopus 로고
    • Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme
    • Bredt D.S., and Snyder S.H. Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme. Proc. Natl. Acad. Sci. USA 87 (1990) 682-685
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 682-685
    • Bredt, D.S.1    Snyder, S.H.2
  • 11
    • 0023518452 scopus 로고
    • Endothelium-derived relaxing factor from pulmonary artery and vein possesses pharmacologic and chemical properties identical to those of nitric oxide radical
    • Ignarro L.J., Byrns R.E., Buga G.M., and Wood K.S. Endothelium-derived relaxing factor from pulmonary artery and vein possesses pharmacologic and chemical properties identical to those of nitric oxide radical. Circ. Res. 61 (1987) 866-879
    • (1987) Circ. Res. , vol.61 , pp. 866-879
    • Ignarro, L.J.1    Byrns, R.E.2    Buga, G.M.3    Wood, K.S.4
  • 12
    • 0025719538 scopus 로고
    • Synthesis of nitric oxide from l-arginine: a recently discovered pathway induced by cytokines with antitumour and antimicrobial activity
    • (discussion 596-8)
    • Hibbs Jr. J.B. Synthesis of nitric oxide from l-arginine: a recently discovered pathway induced by cytokines with antitumour and antimicrobial activity. Res. Immunol. 142 (1991) 565-569 (discussion 596-8)
    • (1991) Res. Immunol. , vol.142 , pp. 565-569
    • Hibbs Jr., J.B.1
  • 13
    • 0032079851 scopus 로고    scopus 로고
    • Purification and characterization of a nitric-oxide synthase from rat liver mitochondria
    • Tatoyan A., and Giulivi C. Purification and characterization of a nitric-oxide synthase from rat liver mitochondria. J. Biol. Chem. 273 (1998) 11044-11048
    • (1998) J. Biol. Chem. , vol.273 , pp. 11044-11048
    • Tatoyan, A.1    Giulivi, C.2
  • 15
    • 0030697859 scopus 로고    scopus 로고
    • Nitric oxide synthase activity in mitochondria
    • Ghafourifar P., and Richter C. Nitric oxide synthase activity in mitochondria. FEBS Lett. 418 (1997) 291-296
    • (1997) FEBS Lett. , vol.418 , pp. 291-296
    • Ghafourifar, P.1    Richter, C.2
  • 16
    • 0032882857 scopus 로고    scopus 로고
    • Ultrastructural localization of neuronal nitric oxide synthase in the laterodorsal tegmental nucleus of wild-type and knockout mice
    • Rothe F., Huang P.L., and Wolf G. Ultrastructural localization of neuronal nitric oxide synthase in the laterodorsal tegmental nucleus of wild-type and knockout mice. Neuroscience 94 (1999) 193-201
    • (1999) Neuroscience , vol.94 , pp. 193-201
    • Rothe, F.1    Huang, P.L.2    Wolf, G.3
  • 18
    • 0034979539 scopus 로고    scopus 로고
    • Nitric oxide synthase in porcine heart mitochondria: evidence for low physiological activity
    • French S., Giulivi C., and Balaban R.S. Nitric oxide synthase in porcine heart mitochondria: evidence for low physiological activity. Am. J. Physiol. Heart Circ. Physiol. 280 (2001) H2863-H2867
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.280
    • French, S.1    Giulivi, C.2    Balaban, R.S.3
  • 19
    • 0035893981 scopus 로고    scopus 로고
    • Mitochondrial nitric oxide synthase is constitutively active and is functionally upregulated in hypoxia
    • Lacza Z., Puskar M., Figueroa J.P., Zhang J., Rajapakse N., and Busija D.W. Mitochondrial nitric oxide synthase is constitutively active and is functionally upregulated in hypoxia. Free Radic. Biol. Med. 31 (2001) 1609-1615
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1609-1615
    • Lacza, Z.1    Puskar, M.2    Figueroa, J.P.3    Zhang, J.4    Rajapakse, N.5    Busija, D.W.6
  • 20
    • 0037381787 scopus 로고    scopus 로고
    • Interactions among nitric oxide and Bcl-family proteins after MPP+ exposure of SH-SY5Y neural cells. I. MPP+ increases mitochondrial NO and Bax protein
    • Dennis J., and Bennett Jr. J.P. Interactions among nitric oxide and Bcl-family proteins after MPP+ exposure of SH-SY5Y neural cells. I. MPP+ increases mitochondrial NO and Bax protein. J. Neurosci. Res. 72 (2003) 76-88
    • (2003) J. Neurosci. Res. , vol.72 , pp. 76-88
    • Dennis, J.1    Bennett Jr., J.P.2
  • 22
    • 0036330994 scopus 로고    scopus 로고
    • Sequential NO production by mitochondria and endoplasmic reticulum during induced apoptosis
    • Bustamante J., Bersier G., Badin R.A., Cymeryng C., Parodi A., and Boveris A. Sequential NO production by mitochondria and endoplasmic reticulum during induced apoptosis. Nitric Oxide 6 (2002) 333-341
    • (2002) Nitric Oxide , vol.6 , pp. 333-341
    • Bustamante, J.1    Bersier, G.2    Badin, R.A.3    Cymeryng, C.4    Parodi, A.5    Boveris, A.6
  • 23
    • 0038661151 scopus 로고    scopus 로고
    • Melatonin counteracts lipopolysaccharide-induced expression and activity of mitochondrial nitric oxide synthase in rats
    • Escames G., Leon J., Macias M., Khaldy H., and Acuna-Castroviejo D. Melatonin counteracts lipopolysaccharide-induced expression and activity of mitochondrial nitric oxide synthase in rats. FASEB J. 17 (2003) 932-934
    • (2003) FASEB J. , vol.17 , pp. 932-934
    • Escames, G.1    Leon, J.2    Macias, M.3    Khaldy, H.4    Acuna-Castroviejo, D.5
  • 24
    • 1342282382 scopus 로고    scopus 로고
    • Mitochondrial nitric oxide synthase
    • Brookes P.S. Mitochondrial nitric oxide synthase. Mitochondrion 3 (2004) 187-204
    • (2004) Mitochondrion , vol.3 , pp. 187-204
    • Brookes, P.S.1
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation 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
  • 28
    • 33644781686 scopus 로고    scopus 로고
    • Cryopreservation of brain mitochondria: a novel methodology for functional studies
    • Nukala V.N., Singh I.N., Davis L.M., and Sullivan P.G. Cryopreservation of brain mitochondria: a novel methodology for functional studies. J. Neurosci. Methods 152 (2006) 48-54
    • (2006) J. Neurosci. Methods , vol.152 , pp. 48-54
    • Nukala, V.N.1    Singh, I.N.2    Davis, L.M.3    Sullivan, P.G.4
  • 29
    • 0033605383 scopus 로고    scopus 로고
    • The stimulatory effects of Hofmeister ions on the activities of neuronal nitric-oxide synthase. Apparent substrate inhibition by l-arginine is overcome in the presence of protein-destabilizing agents
    • Nishimura J.S., Narayanasami R., Miller R.T., Roman L.J., Panda S., and Masters B.S. The stimulatory effects of Hofmeister ions on the activities of neuronal nitric-oxide synthase. Apparent substrate inhibition by l-arginine is overcome in the presence of protein-destabilizing agents. J. Biol. Chem. 274 (1999) 5399-5406
    • (1999) J. Biol. Chem. , vol.274 , pp. 5399-5406
    • Nishimura, J.S.1    Narayanasami, R.2    Miller, R.T.3    Roman, L.J.4    Panda, S.5    Masters, B.S.6
  • 30
    • 0035996331 scopus 로고    scopus 로고
    • Dinitrobenzene-mediated production of peroxynitrite by neuronal nitric oxide synthase
    • Miller R.T. Dinitrobenzene-mediated production of peroxynitrite by neuronal nitric oxide synthase. Chem. Res. Toxicol. 15 (2002) 927-934
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 927-934
    • Miller, R.T.1
  • 31
    • 0028314083 scopus 로고
    • Synthesis of l-thiocitrulline, l-homothiocitrulline, and S-methyl-l-thiocitrulline: a new class of potent nitric oxide synthase inhibitors
    • Narayanan K., and Griffith O.W. Synthesis of l-thiocitrulline, l-homothiocitrulline, and S-methyl-l-thiocitrulline: a new class of potent nitric oxide synthase inhibitors. J. Med. Chem. 37 (1994) 885-887
    • (1994) J. Med. Chem. , vol.37 , pp. 885-887
    • Narayanan, K.1    Griffith, O.W.2
  • 32
    • 0018221205 scopus 로고
    • Radiochemical assays for creatine kinase and arginine kinase using rapid ion exchange separations
    • Leech A.R., Beis I., and Newsholme E.A. Radiochemical assays for creatine kinase and arginine kinase using rapid ion exchange separations. Anal. Biochem. 90 (1978) 561-575
    • (1978) Anal. Biochem. , vol.90 , pp. 561-575
    • Leech, A.R.1    Beis, I.2    Newsholme, E.A.3
  • 33
  • 35
    • 0019418579 scopus 로고
    • Arginine, mitochondrial arginase, and the control of carbamyl phosphate synthesis
    • Cheung C.W., and Raijman L. Arginine, mitochondrial arginase, and the control of carbamyl phosphate synthesis. Arch Biochem. Biophys. 209 (1981) 643-649
    • (1981) Arch Biochem. Biophys. , vol.209 , pp. 643-649
    • Cheung, C.W.1    Raijman, L.2
  • 36
    • 33645704767 scopus 로고    scopus 로고
    • Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver
    • Forner F., Foster L.J., Campanaro S., Valle G., and Mann M. Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver. Mol. Cell. Proteomics 5 (2006) 608-619
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 608-619
    • Forner, F.1    Foster, L.J.2    Campanaro, S.3    Valle, G.4    Mann, M.5
  • 38
    • 33744494822 scopus 로고    scopus 로고
    • Critical overview of mitochondrial nitric-oxide synthase
    • Kato K., and Giulivi C. Critical overview of mitochondrial nitric-oxide synthase. Front. Biosci. 11 (2006) 2725-2738
    • (2006) Front. Biosci. , vol.11 , pp. 2725-2738
    • Kato, K.1    Giulivi, C.2
  • 39
    • 0032528524 scopus 로고    scopus 로고
    • An improved assay for measurement of nitric oxide synthase activity in biological tissues
    • Giraldez R.R., and Zweier J.L. An improved assay for measurement of nitric oxide synthase activity in biological tissues. Anal. Biochem. 261 (1998) 29-35
    • (1998) Anal. Biochem. , vol.261 , pp. 29-35
    • Giraldez, R.R.1    Zweier, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.