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Volumn 28, Issue 2, 2000, Pages 167-173

Phenylarsine oxide inhibits nitric oxide synthase in pulmonary artery endothelial cells

Author keywords

Endothelial cell; Free radicals; Nitric oxide synthase; Phenylarsine oxide; Pulmonary

Indexed keywords

ARSENOSOBENZENE; FREE RADICAL; NITRIC OXIDE SYNTHASE; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE;

EID: 0033960738     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(99)00231-2     Document Type: Article
Times cited : (9)

References (24)
  • 1
    • 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. 100:1997;2146-2152.
    • (1997) J. Clin. Invest. , vol.100 , pp. 2146-2152
    • Michel, T.1    Feron, O.2
  • 2
    • 0029910141 scopus 로고    scopus 로고
    • Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-I
    • Garcia-Cardeña G., Fan R., Stern D.F., Liu J., Sessa W. Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-I. J. Biol. Chem. 271:1996;27237-27240.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27237-27240
    • Garcia-Cardeña, G.1    Fan, R.2    Stern, D.F.3    Liu, J.4    Sessa, W.5
  • 3
    • 0027414849 scopus 로고
    • Endothelial nitric oxide synthase N-terminal myristoylation determines subcellular localization
    • Busconi S., Michel T. Endothelial nitric oxide synthase N-terminal myristoylation determines subcellular localization. J. Biol. Chem. 268:1993;8410-8413.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8410-8413
    • Busconi, S.1    Michel, T.2
  • 4
    • 0029847608 scopus 로고    scopus 로고
    • Palmitoylation of endothelial nitric oxide synthase is necessary for optimal stimulated release of nitric oxide: Implications for caveolae localization
    • Liu J., Garcia-Cardeña G., Sessa W.C. Palmitoylation of endothelial nitric oxide synthase is necessary for optimal stimulated release of nitric oxide implications for caveolae localization . Biochemistry. 35:1996;13277-13281.
    • (1996) Biochemistry , vol.35 , pp. 13277-13281
    • Liu, J.1    Garcia-Cardeña, G.2    Sessa, W.C.3
  • 5
    • 0026712854 scopus 로고
    • Nitric oxide synthase regulatory sites. Phosphorylation by cyclic AMP-dependent protein kinase, protein kinase C, and calcium/calmodulin protein kinase; Identification of flavin and calmodulin binding sites
    • Bredt D.S., Ferris C.D., Snyder S.H. Nitric oxide synthase regulatory sites. Phosphorylation by cyclic AMP-dependent protein kinase, protein kinase C, and calcium/calmodulin protein kinase; identification of flavin and calmodulin binding sites. J. Biol. Chem. 267:1992;10976-10981.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10976-10981
    • Bredt, D.S.1    Ferris, C.D.2    Snyder, S.H.3
  • 6
    • 0030600392 scopus 로고    scopus 로고
    • Bradykinin-stimulated protein tyrosine phosphorylation promotes endothelial nitric oxide synthase translation to the cytoskeleton
    • Venema V.J., Marrero M.B., Venema R.C. Bradykinin-stimulated protein tyrosine phosphorylation promotes endothelial nitric oxide synthase translation to the cytoskeleton. Biochem. Biophys. Res. Commun. 226:1996;703-710.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 703-710
    • Venema, V.J.1    Marrero, M.B.2    Venema, R.C.3
  • 7
    • 0029914567 scopus 로고    scopus 로고
    • Intracellular pH and tyrosine phosphorylation but not calcium determine shear stress-induced nitric oxide production in native endothelial cells
    • Ayajiki K., Kindermann M., Hecker M., Fleming I., Busse R. Intracellular pH and tyrosine phosphorylation but not calcium determine shear stress-induced nitric oxide production in native endothelial cells. Circ. Res. 78:1996;750-758.
    • (1996) Circ. Res. , vol.78 , pp. 750-758
    • Ayajiki, K.1    Kindermann, M.2    Hecker, M.3    Fleming, I.4    Busse, R.5
  • 8
    • 0031561117 scopus 로고    scopus 로고
    • Caveolin-I detergent solubility and association with endothelial nitric oxide synthase is modulated by tyrosine phosphorylation
    • Venema V.J., Zou R., Ju H., Marrero M.B., Venema R.C. Caveolin-I detergent solubility and association with endothelial nitric oxide synthase is modulated by tyrosine phosphorylation. Biochem. Biophys. Res. Commun. 236:1997;155-161.
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 155-161
    • Venema, V.J.1    Zou, R.2    Ju, H.3    Marrero, M.B.4    Venema, R.C.5
  • 9
    • 0024440804 scopus 로고
    • Mechanism of hypoxic injury to pulmonary artery endothelial cell plasma membrane
    • Block E.R., Patel J.M., Edwards D.A. Mechanism of hypoxic injury to pulmonary artery endothelial cell plasma membrane. Am. J. Physiol. 257:1989;C223-C231.
    • (1989) Am. J. Physiol. , vol.257
    • Block, E.R.1    Patel, J.M.2    Edwards, D.A.3
  • 10
    • 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.H.W., Nakane M., 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.H.W.5    Nakane, M.6    Murad, F.7
  • 11
    • 0030238701 scopus 로고    scopus 로고
    • Nitric oxide induced inhibition of lung endothelial cell nitric oxide synthase via interaction with allosteric thiols: Role of thioredoxin in regulation of catalytic activity
    • Patel J.M., Zhang J., Block E.R. Nitric oxide induced inhibition of lung endothelial cell nitric oxide synthase via interaction with allosteric thiols role of thioredoxin in regulation of catalytic activity . Am. J. Respir. Cell. Mol. Biol. 15:1996;410-419.
    • (1996) Am. J. Respir. Cell. Mol. Biol. , vol.15 , pp. 410-419
    • Patel, J.M.1    Zhang, J.2    Block, E.R.3
  • 13
    • 0025967465 scopus 로고
    • Tissue-dependent regulation of protein tyrosine kinase activity during embryonic development
    • Maher P.A. Tissue-dependent regulation of protein tyrosine kinase activity during embryonic development. J. Cell. Biol. 112:1991;955-963.
    • (1991) J. Cell. Biol. , vol.112 , pp. 955-963
    • Maher, P.A.1
  • 14
  • 16
    • 0029376650 scopus 로고
    • Sulfhydryl-disulfide modulation and the role of disulfide oxidoreductases in regulation of the catalytic activity of nitric oxide synthase in pulmonary artery endothelial cells
    • Patel J.M., Block E.R. Sulfhydryl-disulfide modulation and the role of disulfide oxidoreductases in regulation of the catalytic activity of nitric oxide synthase in pulmonary artery endothelial cells. Am. J. Respir. Cell Mol. Biol. 13:1995;352-359.
    • (1995) Am. J. Respir. Cell Mol. Biol. , vol.13 , pp. 352-359
    • Patel, J.M.1    Block, E.R.2
  • 17
    • 0027255776 scopus 로고
    • Sulfhydryl reactive phenylarsine oxide inhibits signal transduction in NK and LAK cells: Effect on zeta-chain phosphorylation and phosphatidylinositol level
    • Bajpai A., Brahmi Z. Sulfhydryl reactive phenylarsine oxide inhibits signal transduction in NK and LAK cells Effect on zeta-chain phosphorylation and phosphatidylinositol level . Biochim. Biophys. Acta. 1177:1993;291-298.
    • (1993) Biochim. Biophys. Acta. , vol.1177 , pp. 291-298
    • Bajpai, A.1    Brahmi, Z.2
  • 18
    • 0028964674 scopus 로고
    • Protein tyrosine phosphatase inhibitors block tumor necrosis factor-dependent activation of the nuclear transcription factor NF-kB
    • Singh S., Aggarwal B.B. Protein tyrosine phosphatase inhibitors block tumor necrosis factor-dependent activation of the nuclear transcription factor NF-kB. J. Biol. Chem. 270:1995;10631-10639.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10631-10639
    • Singh, S.1    Aggarwal, B.B.2
  • 19
    • 0027725209 scopus 로고
    • Inhibition of endothelial nitric oxide synthase by ebselen: Prevention by thiols suggests the inactivation by ebselen of a critical thiol essential for the catalytic activity of nitric oxide synthase
    • Zembowicz A., Hatchett R.J., Radziszewski W., Gryglewski R.J. Inhibition of endothelial nitric oxide synthase by ebselen prevention by thiols suggests the inactivation by ebselen of a critical thiol essential for the catalytic activity of nitric oxide synthase . J. Pharmacol. Exp. Ther. 267:1993;1112-1118.
    • (1993) J. Pharmacol. Exp. Ther. , vol.267 , pp. 1112-1118
    • Zembowicz, A.1    Hatchett, R.J.2    Radziszewski, W.3    Gryglewski, R.J.4
  • 20
    • 0029987385 scopus 로고    scopus 로고
    • Phosphorylation of endothelial nitric oxide synthase in response to fluid shear stress
    • Corson M.A., James N.L., Latta S.E., Nerem R.M., Berk B.C., Harrison D.G. Phosphorylation of endothelial nitric oxide synthase in response to fluid shear stress. Circ. Res. 79:1996;984-991.
    • (1996) Circ. Res. , vol.79 , pp. 984-991
    • Corson, M.A.1    James, N.L.2    Latta, S.E.3    Nerem, R.M.4    Berk, B.C.5    Harrison, D.G.6
  • 21
    • 0025688139 scopus 로고
    • Tyrosine phosphorylation in T cells is regulated by phosphatase activity: Studies with phenylarsine oxide
    • Garcia-Morales P., Minami Y., Luong E., Klausner R.D., Samelson L.E. Tyrosine phosphorylation in T cells is regulated by phosphatase activity studies with phenylarsine oxide . Proc. Natl. Acad. Sci. USA. 87:1990;9255-9259.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9255-9259
    • Garcia-Morales, P.1    Minami, Y.2    Luong, E.3    Klausner, R.D.4    Samelson, L.E.5
  • 22
    • 15844382766 scopus 로고    scopus 로고
    • Interdependence of calcium signaling and protein tyrosine phosphorylation in human endothelial cells
    • Fleming I., Fisslthaler B., Busse R. Interdependence of calcium signaling and protein tyrosine phosphorylation in human endothelial cells. J. Biol. Chem. 271:1996;11009-11015.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11009-11015
    • Fleming, I.1    Fisslthaler, B.2    Busse, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.