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Volumn 14, Issue 11, 1998, Pages 1185-1195

Biosynthesis of NO: Mechanism, regulation and control;Biosynthese du monoxyde d'azote (NO): mecanisme, regulation et controle

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CITRULLINE; CYTOCHROME P450 REDUCTASE; HEME; ISOENZYME; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; OXYGEN; PEROXIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TETRAHYDROBIOPTERIN; VASODILATOR AGENT;

EID: 0031742832     PISSN: 07670974     EISSN: None     Source Type: Journal    
DOI: 10.4267/10608/936     Document Type: Article
Times cited : (10)

References (48)
  • 1
    • 0028815563 scopus 로고
    • Nitric oxide : A new paradigm for second messengers
    • Kerwin JF, Lancaster JR, Feldman PL. Nitric oxide : a new paradigm for second messengers. J Med Chem 1995; 38: 4343-62.
    • (1995) J Med Chem , vol.38 , pp. 4343-4362
    • Kerwin, J.F.1    Lancaster, J.R.2    Feldman, P.L.3
  • 2
    • 0027992219 scopus 로고
    • Simulation of the diffusion and reaction of endogenously produced nitric oxide
    • Lancaster JR. Simulation of the diffusion and reaction of endogenously produced nitric oxide. Proc Natl Acad Sci USA 1994; 91: 8137-41.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8137-8141
    • Lancaster, J.R.1
  • 4
    • 0030988217 scopus 로고    scopus 로고
    • Structure-function aspects in the nitric oxide synthases
    • Stuehr DJ. Structure-function aspects in the nitric oxide synthases. Ann Rev Pharmacol Toxicol 1997; 37: 339-59.
    • (1997) Ann Rev Pharmacol Toxicol , vol.37 , pp. 339-359
    • Stuehr, D.J.1
  • 5
    • 0029149471 scopus 로고
    • Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy
    • Brenman JE, Chao DS, Xia H, Aldape K, Bredt DS. Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy. Cell 1995; 82: 743-52.
    • (1995) Cell , vol.82 , pp. 743-752
    • Brenman, J.E.1    Chao, D.S.2    Xia, H.3    Aldape, K.4    Bredt, D.S.5
  • 6
    • 0028810841 scopus 로고
    • Isoforms of nitric oxide synthase. Properties, cellular distribution and expressional control
    • Forstermann U, Gath I, Schwarz P, Closs EI, Kleinert H. Isoforms of nitric oxide synthase. Properties, cellular distribution and expressional control. Biochem Pharmacol 1995; 50: 1321-32.
    • (1995) Biochem Pharmacol , vol.50 , pp. 1321-1332
    • Forstermann, U.1    Gath, I.2    Schwarz, P.3    Closs, E.I.4    Kleinert, H.5
  • 7
    • 0030711558 scopus 로고    scopus 로고
    • Nitric oxide synthases : Which, where, how, and why?
    • Michel T, Feron O. Nitric oxide synthases : which, where, how, and why? J Clin Invest 1997; 100: 2146-52.
    • (1997) J Clin Invest , vol.100 , pp. 2146-2152
    • Michel, T.1    Feron, O.2
  • 8
    • 0026660191 scopus 로고
    • Spectral characterization of brain and macrophage nitric-oxide synthases - Cytochrome-P-450-like hemeproteins that contain a flavin semiquinone radical
    • Stuehr DJ, Ikeda-Saito M. Spectral characterization of brain and macrophage nitric-oxide synthases - cytochrome-P-450-like hemeproteins that contain a flavin semiquinone radical. J Biol Chem 1992; 267: 20547-50.
    • (1992) J Biol Chem , vol.267 , pp. 20547-20550
    • Stuehr, D.J.1    Ikeda-Saito, M.2
  • 9
    • 0027320848 scopus 로고
    • Particular ability of liver P450s3A to catalyze the oxidation of Nω-hydroxyarginine to citrulline and nitrogen oxides and occurence in NO synthases of a sequence very similar to the heme-binding sequence in P450s
    • Renaud JP, Boucher JL, Vadon S, Delaforge M, Mansuy D. Particular ability of liver P450s3A to catalyze the oxidation of Nω-hydroxyarginine to citrulline and nitrogen oxides and occurence in NO synthases of a sequence very similar to the heme-binding sequence in P450s. Biochem Biophys Res Commun 1993; 192: 53-60.
    • (1993) Biochem Biophys Res Commun , vol.192 , pp. 53-60
    • Renaud, J.P.1    Boucher, J.L.2    Vadon, S.3    Delaforge, M.4    Mansuy, D.5
  • 10
    • 0029664605 scopus 로고    scopus 로고
    • Domains of macrophage NO synthase have divergent roles in forming and stabilizing the active dimeric enzyme
    • Ghosh DK, Abu-Soud HM, Stuehr DJ. Domains of macrophage NO synthase have divergent roles in forming and stabilizing the active dimeric enzyme. Biochemistry 1996; 35: 1444-9.
    • (1996) Biochemistry , vol.35 , pp. 1444-1449
    • Ghosh, D.K.1    Abu-Soud, H.M.2    Stuehr, D.J.3
  • 11
    • 0031030864 scopus 로고    scopus 로고
    • Subunit interactions of endothelial nitric-oxide synthase. Comparisons to the neuronal and inducible nitric-oxide synthase isoforms
    • Venema RC, Ju H, Zou R, Ryan JW, Venema VJ. Subunit interactions of endothelial nitric-oxide synthase. Comparisons to the neuronal and inducible nitric-oxide synthase isoforms. J Biol Chem 1997; 272: 1276-82.
    • (1997) J Biol Chem , vol.272 , pp. 1276-1282
    • Venema, R.C.1    Ju, H.2    Zou, R.3    Ryan, J.W.4    Venema, V.J.5
  • 12
    • 0030973425 scopus 로고    scopus 로고
    • Calmodulin promotes dimerization of the oxygenase domain of human endothelial nitric-oxide synthase
    • Hellermann GR, Solomonson LP. Calmodulin promotes dimerization of the oxygenase domain of human endothelial nitric-oxide synthase. J Biol Chem 1997; 272: 12030-4.
    • (1997) J Biol Chem , vol.272 , pp. 12030-12034
    • Hellermann, G.R.1    Solomonson, L.P.2
  • 13
    • 0032488596 scopus 로고    scopus 로고
    • Comparative functioning of dihydro- and tetrahydrobiopterins in supporting electron transfer, catalysis and subunit dimerization in inducible NO synthase
    • Presta A, Siddhanta U, Wu C, et al. Comparative functioning of dihydro- and tetrahydrobiopterins in supporting electron transfer, catalysis and subunit dimerization in inducible NO synthase. Biochemistry 1998; 37: 298-310.
    • (1998) Biochemistry , vol.37 , pp. 298-310
    • Presta, A.1    Siddhanta, U.2    Wu, C.3
  • 14
    • 0029975203 scopus 로고    scopus 로고
    • Analysis of substrate-induced electronic, catalytic, and structural changes in inducible NO synthase
    • Sennequier N, Stuehr DJ. Analysis of substrate-induced electronic, catalytic, and structural changes in inducible NO synthase. Biochemistry 1996; 35: 5883-92.
    • (1996) Biochemistry , vol.35 , pp. 5883-5892
    • Sennequier, N.1    Stuehr, D.J.2
  • 15
    • 0029983264 scopus 로고    scopus 로고
    • Identification, characterization, and comparison of the calmodulin-binding domains of the endothelial and inducible nitric oxide synthases
    • Venema RC, Sayegh HS, Kent JD, Harrison DG. Identification, characterization, and comparison of the calmodulin-binding domains of the endothelial and inducible nitric oxide synthases. J Biol Chem 1996; 271: 6435-40.
    • (1996) J Biol Chem , vol.271 , pp. 6435-6440
    • Venema, R.C.1    Sayegh, H.S.2    Kent, J.D.3    Harrison, D.G.4
  • 16
    • 0029929385 scopus 로고    scopus 로고
    • Characterization of heme-deficient neuronal nitricoxide synthase reveals a role for heme in subunit dimerization and binding of the amino acid substrate and tetrahydrobiopterin
    • Klatt P, Pfeiffer S, List BM, et al. Characterization of heme-deficient neuronal nitricoxide synthase reveals a role for heme in subunit dimerization and binding of the amino acid substrate and tetrahydrobiopterin. J Biol Chem 1996; 271: 7336-42.
    • (1996) J Biol Chem , vol.271 , pp. 7336-7342
    • Klatt, P.1    Pfeiffer, S.2    List, B.M.3
  • 17
    • 0030464496 scopus 로고    scopus 로고
    • Tetrahydrobiopterin-free neuronal nitric oxide synthase: Evidence for two identical highly anticooperative pteridine binding sites
    • Gorren AC, List BM, Schrammel A, et al. Tetrahydrobiopterin-free neuronal nitric oxide synthase: evidence for two identical highly anticooperative pteridine binding sites. Biochemistry 1996; 35: 16735-45.
    • (1996) Biochemistry , vol.35 , pp. 16735-16745
    • Gorren, A.C.1    List, B.M.2    Schrammel, A.3
  • 18
    • 0030723329 scopus 로고    scopus 로고
    • The structure of nitric oxide synthase oxygenase domain and inhibitor complexes
    • Crane BR, Arvai AS, Gachhui R, et al. The structure of nitric oxide synthase oxygenase domain and inhibitor complexes. Sciene 1997; 278: 425-31.
    • (1997) Sciene , vol.278 , pp. 425-431
    • Crane, B.R.1    Arvai, A.S.2    Gachhui, R.3
  • 19
    • 0032571411 scopus 로고    scopus 로고
    • Structure of nitric oxide synthase oxygenase dimer with pterin and substrate
    • Crane BR, Arvai AS, Ghosh DK, et al. Structure of nitric oxide synthase oxygenase dimer with pterin and substrate. Science 1998; 279: 2121-6.
    • (1998) Science , vol.279 , pp. 2121-2126
    • Crane, B.R.1    Arvai, A.S.2    Ghosh, D.K.3
  • 21
    • 0030766384 scopus 로고    scopus 로고
    • Analysis of neuronal NO synthase under single-turnover conditions: Conversion of Nω-hydroxyarginine to nitric oxide and citrulline
    • Abu-Soud HM, Presta A, Mayer B, Stuehr DJ. Analysis of neuronal NO synthase under single-turnover conditions: conversion of Nω-hydroxyarginine to nitric oxide and citrulline. Biochemistry 1997; 36: 10811-6.
    • (1997) Biochemistry , vol.36 , pp. 10811-10816
    • Abu-Soud, H.M.1    Presta, A.2    Mayer, B.3    Stuehr, D.J.4
  • 23
    • 0029156528 scopus 로고
    • Superoxide anion efficiently performs the oxidative cleavage of C = NOH bonds of amidoximes and N-hydroxyguanidines with formation of nitrogen oxides
    • Sennequier N, Boucher JL, Battioni P, Mansuy D. Superoxide anion efficiently performs the oxidative cleavage of C = NOH bonds of amidoximes and N-hydroxyguanidines with formation of nitrogen oxides. Tetrahedron Lett 1995; 36: 6059-62.
    • (1995) Tetrahedron Lett , vol.36 , pp. 6059-6062
    • Sennequier, N.1    Boucher, J.L.2    Battioni, P.3    Mansuy, D.4
  • 24
    • 0028821761 scopus 로고
    • On the mechanism of nitric oxide formation upon oxidative cleavage of C = N (OH) bonds by NO-synthases and cytochromes P450
    • Mansuy D, Boucher JL, Clement B. On the mechanism of nitric oxide formation upon oxidative cleavage of C = N (OH) bonds by NO-synthases and cytochromes P450. Biochimie 1995; 77: 661-7.
    • (1995) Biochimie , vol.77 , pp. 661-667
    • Mansuy, D.1    Boucher, J.L.2    Clement, B.3
  • 25
    • 0029592040 scopus 로고
    • Inhibition des synthases de monoxyde d'azote dans la défaillance circulatoire: Effet bénéfique ou délétère
    • Thiemermann C. Inhibition des synthases de monoxyde d'azote dans la défaillance circulatoire: effet bénéfique ou délétère Med Sci 1995; 11: 1643-51.
    • (1995) Med Sci , vol.11 , pp. 1643-1651
    • Thiemermann, C.1
  • 26
    • 0028582164 scopus 로고
    • Calmodulin controls neuronal nitric-oxide synthase by a dual mechanism - Activation of intra- and interdomain electron transfer
    • Abu-Soud HM, Yoho LL, Stuehr DJ. Calmodulin controls neuronal nitric-oxide synthase by a dual mechanism - activation of intra- and interdomain electron transfer. J Biol Chem 1994; 269: 32047-50.
    • (1994) J Biol Chem , vol.269 , pp. 32047-32050
    • Abu-Soud, H.M.1    Yoho, L.L.2    Stuehr, D.J.3
  • 27
    • 0029858301 scopus 로고    scopus 로고
    • PIN: An associated protein inhibitor of neuronal nitric oxide synthase
    • Jaffrey SR, Snyder SH. PIN: an associated protein inhibitor of neuronal nitric oxide synthase. Science 1996; 274: 774-7.
    • (1996) Science , vol.274 , pp. 774-777
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 28
    • 0031915818 scopus 로고    scopus 로고
    • Arginase modulates nitric oxide production in activated macrophages
    • Chang CI, Liao JC, Kuo L. Arginase modulates nitric oxide production in activated macrophages. Am J Physiol 1998; 43: H342-8.
    • (1998) Am J Physiol , vol.43
    • Chang, C.I.1    Liao, J.C.2    Kuo, L.3
  • 29
    • 0028170690 scopus 로고
    • N-omega-hydroxy-L-arginine, an intermediate in the L-arginine to nitric oxide pathway, is a strong inhibitor of liver and macrophage arginase
    • Boucher JL, Custot J, Vadon S, et al. N-omega-hydroxy-L-arginine, an intermediate in the L-arginine to nitric oxide pathway, is a strong inhibitor of liver and macrophage arginase. Biochem Biophys Res Commun 1994; 203: 1614-21.
    • (1994) Biochem Biophys Res Commun , vol.203 , pp. 1614-1621
    • Boucher, J.L.1    Custot, J.2    Vadon, S.3
  • 30
    • 0032005770 scopus 로고    scopus 로고
    • Nitric oxide synthesis in the lung. Regulation by oxygen through a kinetic mechanism
    • Dweik RA, Laskowski D, Abu-Soud HM, et al. Nitric oxide synthesis in the lung. Regulation by oxygen through a kinetic mechanism. J Clin Invest 1998; 101: 660-6.
    • (1998) J Clin Invest , vol.101 , pp. 660-666
    • Dweik, R.A.1    Laskowski, D.2    Abu-Soud, H.M.3
  • 31
    • 0030711684 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of endothelial cell dysfunction
    • Harrison DG. Cellular and molecular mechanisms of endothelial cell dysfunction. J Clin Invest 1997; 100: 2153-7.
    • (1997) J Clin Invest , vol.100 , pp. 2153-2157
    • Harrison, D.G.1
  • 32
    • 0030780758 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase: What difference does it make?
    • Nathan C. Inducible nitric oxide synthase: what difference does it make? J Clin Invest 1997; 100: 2417-23.
    • (1997) J Clin Invest , vol.100 , pp. 2417-2423
    • Nathan, C.1
  • 33
    • 0030734267 scopus 로고    scopus 로고
    • Nitric oxide in excitable tissues: Physiological roles and disease
    • Christopherson KS, Bredt DS. Nitric oxide in excitable tissues: Physiological roles and disease. J Clin Invest 1997; 100: 2424-9.
    • (1997) J Clin Invest , vol.100 , pp. 2424-2429
    • Christopherson, K.S.1    Bredt, D.S.2
  • 34
    • 0030758234 scopus 로고    scopus 로고
    • Formation of olfactory memories mediated by nitric oxide
    • Kendrick KM, Guevara-Guzman R, Zorrilla J, et al. Formation of olfactory memories mediated by nitric oxide. Nature 1997; 388: 670-4.
    • (1997) Nature , vol.388 , pp. 670-674
    • Kendrick, K.M.1    Guevara-Guzman, R.2    Zorrilla, J.3
  • 35
    • 0031254183 scopus 로고    scopus 로고
    • Induction of NO and prostaglandin E-2 in osteoblasts by wall-shear stress but not mechanical strain
    • Smalt R, Mitchell FT, Howard RL, Chambers TJ. Induction of NO and prostaglandin E-2 in osteoblasts by wall-shear stress but not mechanical strain. Am J Physiol 1997; 36: E751-8.
    • (1997) Am J Physiol , vol.36
    • Smalt, R.1    Mitchell, F.T.2    Howard, R.L.3    Chambers, T.J.4
  • 36
    • 15844403223 scopus 로고    scopus 로고
    • Nitrite/nitrate oxide (NOx) and cytokine levels in patients with septic shock
    • Endo S, Inada K, Nakae H, et al. Nitrite/nitrate oxide (NOx) and cytokine levels in patients with septic shock. Res Commun Mol Pathol Pharmacol 1996; 91: 347-56.
    • (1996) Res Commun Mol Pathol Pharmacol , vol.91 , pp. 347-356
    • Endo, S.1    Inada, K.2    Nakae, H.3
  • 37
    • 0028999596 scopus 로고
    • Altered responses to bacterial infection and endotoxic shock in mice lacking inducible nitric oxide synthase
    • Mac Micking JD, Nathan C, Hom G, et al. Altered responses to bacterial infection and endotoxic shock in mice lacking inducible nitric oxide synthase. Cell 1995; 81: 641-50.
    • (1995) Cell , vol.81 , pp. 641-650
    • Mac Micking, J.D.1    Nathan, C.2    Hom, G.3
  • 38
    • 0031431194 scopus 로고    scopus 로고
    • Differential effects of nonselective nitric oxide synthase (NOS) and selective inducible NOS inhibition on hepatic necrosis, apoptosis, ICAM-1 expression, and neutrophil accumulation during endotoxemia
    • Ou J, Carlos TM, Watkins SC, et al. Differential effects of nonselective nitric oxide synthase (NOS) and selective inducible NOS inhibition on hepatic necrosis, apoptosis, ICAM-1 expression, and neutrophil accumulation during endotoxemia. Nitric Oxide Biol Chem 1997; 1: 404-16.
    • (1997) Nitric Oxide Biol Chem , vol.1 , pp. 404-416
    • Ou, J.1    Carlos, T.M.2    Watkins, S.C.3
  • 39
    • 0031891318 scopus 로고    scopus 로고
    • Selective iNOS inhibition is superior to norepinephrine in the treatment of rat endotoxic shock
    • Rosselet A, Feihl F, Markert M, et al. Selective iNOS inhibition is superior to norepinephrine in the treatment of rat endotoxic shock. Am J Respir Crit Care Med 1998; 157: 162-70.
    • (1998) Am J Respir Crit Care Med , vol.157 , pp. 162-170
    • Rosselet, A.1    Feihl, F.2    Markert, M.3
  • 40
    • 0031985033 scopus 로고    scopus 로고
    • Nonselective versus selective inhibition of inducible nitric oxide synthase in experimental endotoxic shock
    • Liaudet L, Rosselet A, Schaller MD, et al. Nonselective versus selective inhibition of inducible nitric oxide synthase in experimental endotoxic shock. J Infect Dis 1998; 177: 127-32.
    • (1998) J Infect Dis , vol.177 , pp. 127-132
    • Liaudet, L.1    Rosselet, A.2    Schaller, M.D.3
  • 41
    • 0028987869 scopus 로고
    • Inhibition of constitutive and inducible nitric oxide synthase: Potential selective inhibition
    • Fukuto JM, Chaudhuri G. Inhibition of constitutive and inducible nitric oxide synthase: potential selective inhibition. Annu Rev Pharmacol Toxicol 1995; 35: 165-94.
    • (1995) Annu Rev Pharmacol Toxicol , vol.35 , pp. 165-194
    • Fukuto, J.M.1    Chaudhuri, G.2
  • 42
    • 0028838821 scopus 로고
    • The calmodulin-nitric oxide synthase interaction. Critical role of the calmodulin latch domain in enzyme activation
    • Su Z, Blazing MA, Fan D, George SE. The calmodulin-nitric oxide synthase interaction. Critical role of the calmodulin latch domain in enzyme activation. J Biol Chem 1995; 270: 29117-22.
    • (1995) J Biol Chem , vol.270 , pp. 29117-29122
    • Su, Z.1    Blazing, M.A.2    Fan, D.3    George, S.E.4
  • 43
    • 0028301505 scopus 로고
    • The inhibition of the constitutive and inducible nitric oxide synthase isoforms by indazole agents
    • Wolff DJ, Gribin BJ. The inhibition of the constitutive and inducible nitric oxide synthase isoforms by indazole agents. Arch Biochem Biophys 1994; 311: 300-6.
    • (1994) Arch Biochem Biophys , vol.311 , pp. 300-306
    • Wolff, D.J.1    Gribin, B.J.2
  • 45
    • 0028893884 scopus 로고
    • Aminoguanidine is an isolorm-selective, mechanism-based inactivator of nitric oxide synthase
    • Wolff DJ, Lubeskie A. Aminoguanidine is an isolorm-selective, mechanism-based inactivator of nitric oxide synthase. Arch Biochem Biophys 1995; 316: 290-301.
    • (1995) Arch Biochem Biophys , vol.316 , pp. 290-301
    • Wolff, D.J.1    Lubeskie, A.2
  • 46
    • 0028089793 scopus 로고
    • Potent and selective inhibition of human nitric oxide synthases. Inhibition by non-amino acid isothioureas
    • Garvey EP, Oplinger JA, Tanoury GJ, et al. Potent and selective inhibition of human nitric oxide synthases. Inhibition by non-amino acid isothioureas. J Biol Chem 1994; 269: 26669-76.
    • (1994) J Biol Chem , vol.269 , pp. 26669-26676
    • Garvey, E.P.1    Oplinger, J.A.2    Tanoury, G.J.3
  • 47
    • 0031040613 scopus 로고    scopus 로고
    • 1400W is a slow, tight binding and highly selective inhibitor of inducible nitric-oxide synthase in vitro and in vivo
    • Garvey EP, Oplinger JA, Furfine ES, et al. 1400W is a slow, tight binding and highly selective inhibitor of inducible nitric-oxide synthase in vitro and in vivo. J Biol Chem 1997; 272: 4959-63.
    • (1997) J Biol Chem , vol.272 , pp. 4959-4963
    • Garvey, E.P.1    Oplinger, J.A.2    Furfine, E.S.3
  • 48
    • 0030731240 scopus 로고    scopus 로고
    • Potent and selective inhibition of neuronal nitric oxide synthase by Nω-propyl-L-arginine
    • Zhang HQ, Fast W, Marletta MA, Martasek P, Silverman RB. Potent and selective inhibition of neuronal nitric oxide synthase by Nω-propyl-L-arginine. J Med Chem 1997; 40: 3869-70.
    • (1997) J Med Chem , vol.40 , pp. 3869-3870
    • Zhang, H.Q.1    Fast, W.2    Marletta, M.A.3    Martasek, P.4    Silverman, R.B.5


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