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Volumn 277, Issue 6 21-6, 1999, Pages

NADPH and heme redox modulate pulmonary artery relaxation and guanylate cyclase activation by NO

Author keywords

NADPH oxidoreductase; Nitric oxide; Pentose phosphate pathway

Indexed keywords

1H 1,2,4 OXADIAZOLO[4,3 A]QUINOXALIN 1 ONE; DIPHENYLIODONIUM SALT; EPIANDROSTERONE; FERRICYANIDE; FORSKOLIN; GLUTATHIONE PEROXIDASE; GUANYLATE CYCLASE; HEME; NITRIC OXIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0033387868     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1999.277.6.l1124     Document Type: Article
Times cited : (41)

References (33)
  • 1
    • 0000707453 scopus 로고
    • Nitric oxide activates guanylate cyclase and increases guanosine 3′:5′-cyclic monophosphate
    • Arnold, W. P., C. K. Mittal, S. Katsuki, and F. Murad. Nitric oxide activates guanylate cyclase and increases guanosine 3′:5′-cyclic monophosphate. Proc. Natl. Acad. Sci. USA 74: 3203-3207, 1977.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3203-3207
    • Arnold, W.P.1    Mittal, C.K.2    Katsuki, S.3    Murad, F.4
  • 2
    • 0019409050 scopus 로고
    • Reversible inactivation of guanylate cyclase by mixed disulfide formation
    • Brandwein, H. J., J. A. Lewicki, and F. Murad. Reversible inactivation of guanylate cyclase by mixed disulfide formation. J. Biol. Chem. 256: 2958-2962, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2958-2962
    • Brandwein, H.J.1    Lewicki, J.A.2    Murad, F.3
  • 3
    • 0030424372 scopus 로고    scopus 로고
    • Novel guanyl cyclase inhibitor potently inhibits cyclic GMP accumulation in endothelial cells and relaxation of bovine pulmonary artery
    • Brunner, F., K. Schmidt, E. B. Nielsen, and B. Mayer. Novel guanyl cyclase inhibitor potently inhibits cyclic GMP accumulation in endothelial cells and relaxation of bovine pulmonary artery. J. Pharmacol. Exp. Ther. 277: 48-53, 1996.
    • (1996) J. Pharmacol. Exp. Ther. , vol.277 , pp. 48-53
    • Brunner, F.1    Schmidt, K.2    Nielsen, E.B.3    Mayer, B.4
  • 4
    • 0023234054 scopus 로고
    • Hydrogen peroxide elicits pulmonary arterial relaxation and guanylate cyclase activation
    • Heart Circ. Physiol. 21
    • Burke, T. M., and M. S. Wolin. Hydrogen peroxide elicits pulmonary arterial relaxation and guanylate cyclase activation. Am. J. Physiol. 252 (Heart Circ. Physiol. 21): H721-H732, 1987.
    • (1987) Am. J. Physiol. , vol.252
    • Burke, T.M.1    Wolin, M.S.2
  • 5
    • 0025044065 scopus 로고
    • Superoxide anion inhibits cGMP-associated bovine pulmonary arterial relaxation
    • Heart Circ. Physiol. 28
    • Cherry, P. D., H. A. Omar, K. A. Farrell, J. S. Stuart, and M. S. Wolin. Superoxide anion inhibits cGMP-associated bovine pulmonary arterial relaxation. Am. J. Physiol. 259 (Heart Circ. Physiol. 28): H1056-H1062, 1990.
    • (1990) Am. J. Physiol. , vol.259
    • Cherry, P.D.1    Omar, H.A.2    Farrell, K.A.3    Stuart, J.S.4    Wolin, M.S.5
  • 8
    • 0018216365 scopus 로고
    • Restoration of the responsiveness of purified guanylate cyclase to nitrosoguanidine, nitric oxide, and related activators by heme and hemoproteins. Evidence for involvement of the paramagnetic nitrosyl-heme complex in enzyme activation
    • Craven, P. A., and F. R. DeRubertis. Restoration of the responsiveness of purified guanylate cyclase to nitrosoguanidine, nitric oxide, and related activators by heme and hemoproteins. Evidence for involvement of the paramagnetic nitrosyl-heme complex in enzyme activation. J. Biol. Chem. 253: 8433-8443, 1978.
    • (1978) J. Biol. Chem. , vol.253 , pp. 8433-8443
    • Craven, P.A.1    DeRubertis, F.R.2
  • 9
    • 0030809625 scopus 로고    scopus 로고
    • Nitric oxide elicits prolonged relaxation of bovine pulmonary arteries via endogenous peroxynitrite generation
    • Lung Cell. Mol. Physiol. 17
    • Davidson, C. A., P. M. Kaminski, and M. S. Wolin. Nitric oxide elicits prolonged relaxation of bovine pulmonary arteries via endogenous peroxynitrite generation. Am. J. Physiol. 273 (Lung Cell. Mol. Physiol. 17): L437-L444, 1997.
    • (1997) Am. J. Physiol. , vol.273
    • Davidson, C.A.1    Kaminski, P.M.2    Wolin, M.S.3
  • 10
    • 0032030178 scopus 로고    scopus 로고
    • The deactivation of soluble guanylate cyclase by redox-active agents
    • Dierks, E. A., and J. N. Burstyn. The deactivation of soluble guanylate cyclase by redox-active agents. Arch. Biochem. Biophys. 351: 1-7, 1998.
    • (1998) Arch. Biochem. Biophys. , vol.351 , pp. 1-7
    • Dierks, E.A.1    Burstyn, J.N.2
  • 11
    • 0019879880 scopus 로고
    • Soluble guanylate cyclase purified from bovine lung contains heme and copper
    • Gerzer, R., E. Bohme, F. Hofmann, and G. Schultz. Soluble guanylate cyclase purified from bovine lung contains heme and copper. FEBS Lett. 132: 71-74, 1981.
    • (1981) FEBS Lett. , vol.132 , pp. 71-74
    • Gerzer, R.1    Bohme, E.2    Hofmann, F.3    Schultz, G.4
  • 12
    • 0029045610 scopus 로고
    • Dapsone-induced hemolytic anemia: Role of glucose-6-phosphate dehydrogenase in the hemolytic response of rat erythrocytes to N-hydroxydapsone
    • Grossman, S., R. Budinsky, and D. Jollow. Dapsone-induced hemolytic anemia: role of glucose-6-phosphate dehydrogenase in the hemolytic response of rat erythrocytes to N-hydroxydapsone. J. Pharmacol. Exp. Ther. 273: 870-877, 1995.
    • (1995) J. Pharmacol. Exp. Ther. , vol.273 , pp. 870-877
    • Grossman, S.1    Budinsky, R.2    Jollow, D.3
  • 13
    • 0032989452 scopus 로고    scopus 로고
    • Regulation of NO-elicited pulmonary artery relaxation and guanylate cyclase activation by NADH oxidase and SOD
    • Heart Circ. Physiol. 45
    • Gupte, S., T. Rupawalla, K. M. Mohazzab-H., and M. S. Wolin. Regulation of NO-elicited pulmonary artery relaxation and guanylate cyclase activation by NADH oxidase and SOD. Am. J. Physiol. 276 (Heart Circ. Physiol. 45): H1535-H1542, 1999.
    • (1999) Am. J. Physiol. , vol.276
    • Gupte, S.1    Rupawalla, T.2    Mohazzab-H, K.M.3    Wolin, M.S.4
  • 14
    • 0030711684 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of endothelial cell dysfunction
    • Harrison, D. G. Cellular and molecular mechanisms of endothelial cell dysfunction. J. Clin. Invest. 100: 2153-2157, 1997.
    • (1997) J. Clin. Invest. , vol.100 , pp. 2153-2157
    • Harrison, D.G.1
  • 15
    • 0017831701 scopus 로고
    • Methemoglobin reduction system of erythrocytes
    • edited by S. Fleischer and L. Packer. New York: Academic
    • Hultquist, D. E. Methemoglobin reduction system of erythrocytes. In: Methods of Enzymology, edited by S. Fleischer and L. Packer. New York: Academic, 1978, vol. 52, p. 463-475.
    • (1978) Methods of Enzymology , vol.52 , pp. 463-475
    • Hultquist, D.E.1
  • 17
    • 0024706628 scopus 로고
    • Biological actions and properties of endothelium-derived nitric oxide formed and released from artery and vein
    • Ignarro, L. J. Biological actions and properties of endothelium-derived nitric oxide formed and released from artery and vein. Circ. Res. 65: 1-21, 1989.
    • (1989) Circ. Res. , vol.65 , pp. 1-21
    • Ignarro, L.J.1
  • 18
    • 0019388174 scopus 로고
    • Mechanism of vascular smooth muscle relaxation by organic nitrates, nitrites, nitroprusside and nitric oxide: Evidence for the involvement of S-nitrosothiols as active intermediates
    • Ignarro, L. J., H. Lippton, J. C. Edwards, W. H. Baricos, A. L. Hyman, P. J. Kadowitz, and C. A. Gruetter. Mechanism of vascular smooth muscle relaxation by organic nitrates, nitrites, nitroprusside and nitric oxide: evidence for the involvement of S-nitrosothiols as active intermediates. J. Pharmacol. Exp. Ther. 218: 739-749, 1981.
    • (1981) J. Pharmacol. Exp. Ther. , vol.218 , pp. 739-749
    • Ignarro, L.J.1    Lippton, H.2    Edwards, J.C.3    Baricos, W.H.4    Hyman, A.L.5    Kadowitz, P.J.6    Gruetter, C.A.7
  • 19
    • 0021306536 scopus 로고
    • Regulation of purified soluble guanylate cyclase by porphyrins and metalloporphyrins: A unifying concept
    • Ignarro, L. J., K. S. Wood, and M. S. Wolin. Regulation of purified soluble guanylate cyclase by porphyrins and metalloporphyrins: a unifying concept. Adv. Cyclic Nucleotide Res. 17: 267-274, 1984.
    • (1984) Adv. Cyclic Nucleotide Res. , vol.17 , pp. 267-274
    • Ignarro, L.J.1    Wood, K.S.2    Wolin, M.S.3
  • 20
    • 0019778223 scopus 로고
    • Determination of pyridine dinucleotide in cell extracts by high-performance liquid chromatography
    • Jones, D. P. Determination of pyridine dinucleotide in cell extracts by high-performance liquid chromatography. J. Chromatogr. 225: 446-449, 1981.
    • (1981) J. Chromatogr. , vol.225 , pp. 446-449
    • Jones, D.P.1
  • 21
    • 0000281046 scopus 로고
    • Inhibition of NADP dependent oxidoreductases by the 6-aminonicotinamide
    • Kohler, E., H.-J. Barrach, and D. Neubert. Inhibition of NADP dependent oxidoreductases by the 6-aminonicotinamide. FEBS Lett. 6: 225-228, 1970.
    • (1970) FEBS Lett. , vol.6 , pp. 225-228
    • Kohler, E.1    Barrach, H.-J.2    Neubert, D.3
  • 22
    • 0033524687 scopus 로고    scopus 로고
    • Potential role of a membrane bound NADH oxidoreductase in nitric oxide release and arterial relaxation to nitroprusside
    • Mohazzab-H., K. M., P. M. Kaminski, R. Agarwal, and M. S. Wolin. Potential role of a membrane bound NADH oxidoreductase in nitric oxide release and arterial relaxation to nitroprusside. Circ. Res. 84: 220-228, 1999.
    • (1999) Circ. Res. , vol.84 , pp. 220-228
    • Mohazzab-H, K.M.1    Kaminski, P.M.2    Agarwal, R.3    Wolin, M.S.4
  • 23
    • 0028596392 scopus 로고
    • Sites of superoxide anion production detected by lucigenin in calf pulmonary artery smooth muscle
    • Lung Cell. Mol. Physiol. 11
    • Mohazzab-H., K. M., and M. S. Wolin. Sites of superoxide anion production detected by lucigenin in calf pulmonary artery smooth muscle. Am. J. Physiol. 267 (Lung Cell. Mol. Physiol. 11): L815-L822, 1994.
    • (1994) Am. J. Physiol. , vol.267
    • Mohazzab-H, K.M.1    Wolin, M.S.2
  • 24
    • 0019795076 scopus 로고
    • Resolution of 52 ninhydrin-positive compounds with a high-speed amino acid analyzer
    • Murayama, K., and T. Sugawara. Resolution of 52 ninhydrin-positive compounds with a high-speed amino acid analyzer. J. Chromatogr. 224: 315-321, 1981.
    • (1981) J. Chromatogr. , vol.224 , pp. 315-321
    • Murayama, K.1    Sugawara, T.2
  • 25
    • 0002769601 scopus 로고
    • The assay of intermediates and enzymes involved in the synthesis of the nicotinamide nucleotide in mammalian tissue
    • Pinder, S., B. J. Clark, and A. L. Greenbaum. The assay of intermediates and enzymes involved in the synthesis of the nicotinamide nucleotide in mammalian tissue. Methods Enzymol. 18: 20-32, 1971.
    • (1971) Methods Enzymol. , vol.18 , pp. 20-32
    • Pinder, S.1    Clark, B.J.2    Greenbaum, A.L.3
  • 27
    • 0022104472 scopus 로고
    • Effect of 6-aminonicotianide on renin release in isolated rat kidney: Possible role of the pentose phosphate pathway
    • Renal Fluid Electrolyte Physiol. 18
    • Rostand, S. G., and J. Work. Effect of 6-aminonicotianide on renin release in isolated rat kidney: possible role of the pentose phosphate pathway. Am. J. Physiol. 249 (Renal Fluid Electrolyte Physiol. 18): F213-F219, 1985.
    • (1985) Am. J. Physiol. , vol.249
    • Rostand, S.G.1    Work, J.2
  • 28
    • 0029938767 scopus 로고    scopus 로고
    • Characterization of 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one as a heme-site inhibitor of nitric oxide-sensitive guanyl cyclase
    • Schrammel, A., S. Behrends, K. Schmidt, D. Koesling, and B. Mayer. Characterization of 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one as a heme-site inhibitor of nitric oxide-sensitive guanyl cyclase. Mol. Pharmacol. 50: 1-5, 1996.
    • (1996) Mol. Pharmacol. , vol.50 , pp. 1-5
    • Schrammel, A.1    Behrends, S.2    Schmidt, K.3    Koesling, D.4    Mayer, B.5
  • 29
    • 0028228808 scopus 로고
    • Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states
    • Stone, J. R., and M. A. Marletta. Soluble guanylate cyclase from bovine lung: activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states. Biochemistry 33: 5636-5640, 1994.
    • (1994) Biochemistry , vol.33 , pp. 5636-5640
    • Stone, J.R.1    Marletta, M.A.2
  • 30
    • 0029015864 scopus 로고
    • Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation
    • Thomas, J. A., B. Poland, and R. Honzatko. Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Arch. Biochem. Biophys. 319: 1-9, 1995.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 1-9
    • Thomas, J.A.1    Poland, B.2    Honzatko, R.3
  • 32
    • 0020491331 scopus 로고
    • Guanylate cyclase from bovine lung: A kinetic analysis of the regulation of the purified soluble enzyme by protoporphyrin IX, heme and nitrosylheme
    • Wolin, M. S., K. S. Wood, and L. J. Ignarro. Guanylate cyclase from bovine lung: a kinetic analysis of the regulation of the purified soluble enzyme by protoporphyrin IX, heme and nitrosylheme. J. Biol. Chem. 257: 13312-13320, 1982.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13312-13320
    • Wolin, M.S.1    Wood, K.S.2    Ignarro, L.J.3
  • 33
    • 0028137347 scopus 로고
    • Raman resonance spectroscopy of soluble guanyl cyclase reveals displacement of distal and proximal heme ligands by NO
    • Yu, A. E., S. Hu, T. G. Spiro, and J. N. Burstyn. Raman resonance spectroscopy of soluble guanyl cyclase reveals displacement of distal and proximal heme ligands by NO. J. Am. Chem. Soc. 116: 4117-4118, 1994.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 4117-4118
    • Yu, A.E.1    Hu, S.2    Spiro, T.G.3    Burstyn, J.N.4


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