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Volumn , Issue , 2009, Pages 261-285

Oxidant-Mediated Signaling and Injury in Pulmonary Endothelium

Author keywords

Cellular manifestations of oxidative stress; Cytochrome P450 pathway of endoplasmic reticulum; Endothelial injury hallmark of acute lung injury (ALI) pathology; NO synthase (nitric oxide synthase NOS); Oxidant stress with O2 based radicals and reactive oxygen species (ROS); Oxidant antioxidant balance; Oxidant mediated signaling and pulmonary endothelium injury; ROS as signaling molecules; SOD role in cellular defense against oxidative stress; Superoxide dismutases (SODs)

Indexed keywords


EID: 84889347084     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470747490.ch17     Document Type: Chapter
Times cited : (1)

References (198)
  • 2
    • 0033521006 scopus 로고    scopus 로고
    • Role of iron and superoxide for generation of hydroxyl radical, oxidative DNA lesions, and mutagenesis in Escherichia coli
    • Nunoshiba, T., Obata, F., Boss, A.C. et al. (1999) Role of iron and superoxide for generation of hydroxyl radical, oxidative DNA lesions, and mutagenesis in Escherichia coli. The Journal of Biological Chemistry, 274, 34832-37.
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 34832-34837
    • Nunoshiba, T.1    Obata, F.2    Boss, A.C.3
  • 3
    • 1942468123 scopus 로고    scopus 로고
    • Novel NAD(P)H oxidases in the cardiovascular system
    • Griendling, K.K. (2004) Novel NAD(P)H oxidases in the cardiovascular system. Heart, 90, 491-93.
    • (2004) Heart , vol.90 , pp. 491-493
    • Griendling, K.K.1
  • 4
    • 39949083961 scopus 로고    scopus 로고
    • NADPH oxidases in lung biology and pathology: host defense enzymes, and more
    • van der Vliet, A. (2008) NADPH oxidases in lung biology and pathology: host defense enzymes, and more. Free Radical Biology and Medicine, 44, 938-55.
    • (2008) Free Radical Biology and Medicine , vol.44 , pp. 938-955
    • Van Der Vliet, A.1
  • 6
    • 0032487361 scopus 로고    scopus 로고
    • Endothelial NADPH oxidase as the source of oxidants in lungs exposed to ischemia or high K+
    • Al-Mehdi, A.B., Zhao, G., Dodia, C. et al. (1998) Endothelial NADPH oxidase as the source of oxidants in lungs exposed to ischemia or high K+. Circulation Research, 83, 730-37.
    • (1998) Circulation Research , vol.83 , pp. 730-737
    • Al-Mehdi, A.B.1    Zhao, G.2    Dodia, C.3
  • 7
    • 0034677947 scopus 로고    scopus 로고
    • NAD(P)H oxidase: role in cardiovascular biology and disease
    • Griendling, K.K., Sorescu, D., and Ushio-Fukai, M. (2000) NAD(P)H oxidase: role in cardiovascular biology and disease. Circulation Research, 86, 494-501.
    • (2000) Circulation Research , vol.86 , pp. 494-501
    • Griendling, K.K.1    Sorescu, D.2    Ushio-Fukai, M.3
  • 9
    • 33750923857 scopus 로고    scopus 로고
    • NOX2 and NOX4 mediate proliferative response in endothelial cells
    • Petry, A., Djordjevic, T., Weitnauer, M. et al. (2006) NOX2 and NOX4 mediate proliferative response in endothelial cells. Antioxidants and Redox Signaling, 8, 1473-84.
    • (2006) Antioxidants and Redox Signaling , vol.8 , pp. 1473-1484
    • Petry, A.1    Djordjevic, T.2    Weitnauer, M.3
  • 10
    • 0037205457 scopus 로고    scopus 로고
    • Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells
    • Li, J.M. and Shah, A.M. (2002) Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells. The Journal of Biological Chemistry, 277, 19952-60.
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 19952-19960
    • Li, J.M.1    Shah, A.M.2
  • 11
    • 0024311743 scopus 로고
    • Xanthine oxidase activity in rat pulmonary artery endothelial cells and its alteration by activated neutrophils
    • Phan, S.H., Gannon, D.E., Varani, J. et al. (1989) Xanthine oxidase activity in rat pulmonary artery endothelial cells and its alteration by activated neutrophils. American Journal of Pathology, 134, 1201-11.
    • (1989) American Journal of Pathology , vol.134 , pp. 1201-1211
    • Phan, S.H.1    Gannon, D.E.2    Varani, J.3
  • 12
    • 41149100550 scopus 로고    scopus 로고
    • Production of reactive oxygen species by complex I (NADH: ubiquinone oxi-doreductase) from Escherichia coli and comparison to the enzyme from mitochondria
    • Esterhazy, D., King, M.S., Yakovlev, G., and Hirst, J. (2008) Production of reactive oxygen species by complex I (NADH: ubiquinone oxi-doreductase) from Escherichia coli and comparison to the enzyme from mitochondria. Biochemistry, 47, 3964-71.
    • (2008) Biochemistry , vol.47 , pp. 3964-3971
    • Esterhazy, D.1    King, M.S.2    Yakovlev, G.3    Hirst, J.4
  • 13
    • 0032924757 scopus 로고    scopus 로고
    • Mitochondrial damage induced by conditions of oxidative stress
    • Kowaltowski, A.J. and Vercesi, A.E. (1999) Mitochondrial damage induced by conditions of oxidative stress. Free Radical Biology and Medicine, 26, 463-71.
    • (1999) Free Radical Biology and Medicine , vol.26 , pp. 463-471
    • Kowaltowski, A.J.1    Vercesi, A.E.2
  • 15
    • 0014842505 scopus 로고
    • One-electron-transfer reactions in biochemical systems. V. Difference in the mechanism of quinone reduction by the NADH dehydrogenase and the NAD(P)H dehydrogenase (DT-diaphorase)
    • Iyanagi, T. and Yamazaki, I. (1970) One-electron-transfer reactions in biochemical systems. V. Difference in the mechanism of quinone reduction by the NADH dehydrogenase and the NAD(P)H dehydrogenase (DT-diaphorase). Biochimica et Biophysica Acta, 216, 282-94.
    • (1970) Biochimica et Biophysica Acta , vol.216 , pp. 282-294
    • Iyanagi, T.1    Yamazaki, I.2
  • 16
    • 0032002313 scopus 로고    scopus 로고
    • Mechanistic study of the autoxidation of reduced flavin and quinone compounds
    • Tatsumi, H., Nakase, H., Kano, K., and Ikeda, T. (1998) Mechanistic study of the autoxidation of reduced flavin and quinone compounds. Journal of Electroanalytical Chemistry, 443, 236-42.
    • (1998) Journal of Electroanalytical Chemistry , vol.443 , pp. 236-242
    • Tatsumi, H.1    Nakase, H.2    Kano, K.3    Ikeda, T.4
  • 17
    • 43049175139 scopus 로고    scopus 로고
    • Role of reactive oxygen species in the neurotoxicity of environmental agents implicated in Parkinson's disease
    • Drechsel, D. and Patel, M. (2008) Role of reactive oxygen species in the neurotoxicity of environmental agents implicated in Parkinson's disease. Free Radical Biology and Medicine, 44, 1873-86.
    • (2008) Free Radical Biology and Medicine , vol.44 , pp. 1873-1886
    • Drechsel, D.1    Patel, M.2
  • 18
    • 0016153291 scopus 로고
    • Superoxide-and singlet oxygen-catalyzed lipid peroxidation as a possible mechanism for paraquat (methyl viologen) toxicity
    • Bus, J.S., Aust, S.D., and Gibson, J.E. (1974) Superoxide-and singlet oxygen-catalyzed lipid peroxidation as a possible mechanism for paraquat (methyl viologen) toxicity. Biochemical and Biophysical Research Communications, 58, 749-55.
    • (1974) Biochemical and Biophysical Research Communications , vol.58 , pp. 749-755
    • Bus, J.S.1    Aust, S.D.2    Gibson, J.E.3
  • 19
    • 38349105900 scopus 로고    scopus 로고
    • Complex I is the major site of mitochondrial superoxide production by paraquat
    • Cocheme, H.M. and Murphy, M.P. (2008) Complex I is the major site of mitochondrial superoxide production by paraquat. The Journal of Biological Chemistry, 283, 1786-98.
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 1786-1798
    • Cocheme, H.M.1    Murphy, M.P.2
  • 22
    • 34548419654 scopus 로고    scopus 로고
    • Role of mitochondrial electron transport complex I in coenzyme Q1 reduction by intact pulmonary arterial endothelial cells and the effect of hyperoxia
    • Merker, M.P., Audi, S.H., Lindemer, B.J. et al. (2007) Role of mitochondrial electron transport complex I in coenzyme Q1 reduction by intact pulmonary arterial endothelial cells and the effect of hyperoxia. American Journal of Physiology: Lung Cellular and Molecular Physiology, 293, L809-19.
    • (2007) American Journal of Physiology: Lung Cellular and Molecular Physiology , vol.293
    • Merker, M.P.1    Audi, S.H.2    Lindemer, B.J.3
  • 25
    • 21744434507 scopus 로고    scopus 로고
    • Nitric oxide-induced nitrative stress involved in microbial pathogenesis
    • Zaki, M.H., Akuta, T., and Akaike, T. (2005) Nitric oxide-induced nitrative stress involved in microbial pathogenesis. Journal of Pharmacological Sciences, 98, 117-29.
    • (2005) Journal of Pharmacological Sciences , vol.98 , pp. 117-129
    • Zaki, M.H.1    Akuta, T.2    Akaike, T.3
  • 26
    • 0028105887 scopus 로고
    • Interactions of peroxynitrite with human plasma and its constituents: oxidative damage and antioxidant depletion
    • Van der Vliet, A., Smith, D., O'Neill, C.A. et al. (1994) Interactions of peroxynitrite with human plasma and its constituents: oxidative damage and antioxidant depletion. The Biochemical Journal, 303, 295-301.
    • (1994) The Biochemical Journal , vol.303 , pp. 295-301
    • Van Der Vliet, A.1    Smith, D.2    O'Neill, C.A.3
  • 28
    • 0037432615 scopus 로고    scopus 로고
    • Multiple pathways of perox-ynitrite cytotoxicity
    • 140-141
    • Szabo, C. (2003) Multiple pathways of perox-ynitrite cytotoxicity. Toxicology Letters, 140-141, 105-12.
    • (2003) Toxicology Letters , pp. 105-112
    • Szabo, C.1
  • 30
    • 2542455472 scopus 로고    scopus 로고
    • iNOS-mediated nitric oxide production and its regulation
    • Aktan, F. (2004) iNOS-mediated nitric oxide production and its regulation. Life Sciences, 75, 639-53.
    • (2004) Life Sciences , vol.75 , pp. 639-653
    • Aktan, F.1
  • 31
    • 0021745377 scopus 로고
    • Extracellular superoxide dismutase in human tissues and human cell lines
    • Marklund, S.L. (1984) Extracellular superoxide dismutase in human tissues and human cell lines. The Journal of Clinical Investigation, 74, 1398-403.
    • (1984) The Journal of Clinical Investigation , vol.74 , pp. 1398-1403
    • Marklund, S.L.1
  • 35
    • 0028170326 scopus 로고
    • Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress
    • Michiels, C., Raes, M., Toussaint, O., and Remacle, J. (1994) Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress. Free Radical Biology and Medicine, 17, 235-48.
    • (1994) Free Radical Biology and Medicine , vol.17 , pp. 235-248
    • Michiels, C.1    Raes, M.2    Toussaint, O.3    Remacle, J.4
  • 36
    • 0033597885 scopus 로고    scopus 로고
    • Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase
    • Fisher, A.B., Dodia, C., Manevich, Y. et al. (1999) Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase. The Journal of Biological Chemistry, 274, 21326-34.
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 21326-21334
    • Fisher, A.B.1    Dodia, C.2    Manevich, Y.3
  • 37
    • 38749094132 scopus 로고    scopus 로고
    • Peroxiredoxins in the lung with emphasis on peroxiredoxin VI
    • in, (eds L. Flohe and J.R. Harris), Springer, New York
    • Schremmer, B., Manevich, Y., Feinstein, S., and Fisher, A.B. (2007). Peroxiredoxins in the lung with emphasis on peroxiredoxin VI, in Perox-iredoxin Systems, (eds L. Flohe and J.R. Harris), Springer, New York, pp. 317-44.
    • (2007) Perox-iredoxin Systems , pp. 317-344
    • Schremmer, B.1    Manevich, Y.2    Feinstein, S.3    Fisher, A.B.4
  • 38
    • 18844400905 scopus 로고    scopus 로고
    • Perox-iredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism
    • Manevich, Y. and Fisher, A.B. (2005) Perox-iredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism. Free Radical Biology and Medicine, 38, 1422-32.
    • (2005) Free Radical Biology and Medicine , vol.38 , pp. 1422-1432
    • Manevich, Y.1    Fisher, A.B.2
  • 39
    • 7444247318 scopus 로고    scopus 로고
    • Lung injury and mortality with hyperoxia are increased in peroxiredoxin 6 gene-targeted mice
    • Wang, Y., Feinstein, S.I., Manevich, Y. et al. (2004) Lung injury and mortality with hyperoxia are increased in peroxiredoxin 6 gene-targeted mice. Free Radical Biology and Medicine, 37, 1736-43.
    • (2004) Free Radical Biology and Medicine , vol.37 , pp. 1736-1743
    • Wang, Y.1    Feinstein, S.I.2    Manevich, Y.3
  • 40
    • 33644662758 scopus 로고    scopus 로고
    • Peroxiredoxin 6 gene-targeted mice show increased lung injury with paraquat-induced oxidative stress
    • Wang, Y., Feinstein, S.I., Manevich, Y. et al. (2006) Peroxiredoxin 6 gene-targeted mice show increased lung injury with paraquat-induced oxidative stress. Antioxidants and Redox Signaling, 8, 229-37.
    • (2006) Antioxidants and Redox Signaling , vol.8 , pp. 229-237
    • Wang, Y.1    Feinstein, S.I.2    Manevich, Y.3
  • 41
    • 34250560940 scopus 로고
    • The oxidation of glutathione with formic acid and hydrogen peroxide
    • Utzinger, G.E., Strait, L.A., and Tuck, L.D. (1963) The oxidation of glutathione with formic acid and hydrogen peroxide. Experientia, 19, 324-27.
    • (1963) Experientia , vol.19 , pp. 324-327
    • Utzinger, G.E.1    Strait, L.A.2    Tuck, L.D.3
  • 42
    • 11844254800 scopus 로고    scopus 로고
    • --independent rescue from apoptosis by stil-bene derivatives in rat cardiomyocytes
    • --independent rescue from apoptosis by stil-bene derivatives in rat cardiomyocytes. FEBS Letters, 579, 517-22.
    • (2005) FEBS Letters , vol.579 , pp. 517-522
    • Tanabe, S.1    Wang, X.2    Takahashi, N.3
  • 43
    • 0037376674 scopus 로고    scopus 로고
    • Oxidant signals and oxidative stress
    • Finkel, T. (2003) Oxidant signals and oxidative stress. Current Opinion in Cell Biology, 15, 247-54.
    • (2003) Current Opinion in Cell Biology , vol.15 , pp. 247-254
    • Finkel, T.1
  • 44
    • 0035842896 scopus 로고    scopus 로고
    • VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release
    • Madesh, M. and Hajnoczky, G. (2001) VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release. The Journal of Cell Biology, 155, 1003-15.
    • (2001) The Journal of Cell Biology , vol.155 , pp. 1003-1015
    • Madesh, M.1    Hajnoczky, G.2
  • 45
    • 25444525139 scopus 로고    scopus 로고
    • Selective role for superoxide in InsP3 receptor-mediated mitochondrial dysfunction and endothelial apoptosis
    • Madesh, M., Hawkins, B.J., Milovanova, T. et al. (2005) Selective role for superoxide in InsP3 receptor-mediated mitochondrial dysfunction and endothelial apoptosis. The Journal ofCell Biology, 170, 1079-90.
    • (2005) The Journal ofCell Biology , vol.170 , pp. 1079-1090
    • Madesh, M.1    Hawkins, B.J.2    Milovanova, T.3
  • 46
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis
    • D'Autreaux, B. and Toledano, M.B. (2007) ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nature Reviews: Molecular Cell Biology, 8, 813-24.
    • (2007) Nature Reviews: Molecular Cell Biology , vol.8 , pp. 813-824
    • D'Autreaux, B.1    Toledano, M.B.2
  • 47
    • 34250349160 scopus 로고    scopus 로고
    • Superoxide flux in endothelial cells via the chloride channel-3 mediates intracellular signaling
    • Hawkins, B.J., Madesh, M., Kirkpatrick, C.J., and Fisher, A.B. (2007) Superoxide flux in endothelial cells via the chloride channel-3 mediates intracellular signaling. Molecular Biology of the Cell, 18, 2002-12.
    • (2007) Molecular Biology of the Cell , vol.18 , pp. 2002-2012
    • Hawkins, B.J.1    Madesh, M.2    Kirkpatrick, C.J.3    Fisher, A.B.4
  • 49
    • 3042682465 scopus 로고    scopus 로고
    • Low concentration of oxidant and nitric oxide donors stimulate proliferation of human endothelial cells in vitro
    • Luczak, K., Balcerczyk, A., Soszynski, M., and Bartosz, G. (2004) Low concentration of oxidant and nitric oxide donors stimulate proliferation of human endothelial cells in vitro. Cell Biology International, 28, 483-86.
    • (2004) Cell Biology International , vol.28 , pp. 483-486
    • Luczak, K.1    Balcerczyk, A.2    Soszynski, M.3    Bartosz, G.4
  • 50
    • 33644823952 scopus 로고    scopus 로고
    • Lung endothelial cell proliferation with decreased shear stress is mediated by reactive oxygen species
    • Milovanova, T., Chatterjee, S., Manevich, Y. et al. (2006) Lung endothelial cell proliferation with decreased shear stress is mediated by reactive oxygen species. American Journal of Physiology: Cell Physiology, 290, C66-76.
    • (2006) American Journal of Physiology: Cell Physiology , vol.290
    • Milovanova, T.1    Chatterjee, S.2    Manevich, Y.3
  • 51
    • 45149107474 scopus 로고    scopus 로고
    • Role of protein tyrosine phosphatase 1B in vascular endothelial growth factor signaling and cell-cell adhesions in endothelial cells
    • Nakamura, Y., Patrushev, N., Inomata, H. et al. (2008) Role of protein tyrosine phosphatase 1B in vascular endothelial growth factor signaling and cell-cell adhesions in endothelial cells. Circulation Research, 102, 1182-91.
    • (2008) Circulation Research , vol.102 , pp. 1182-1191
    • Nakamura, Y.1    Patrushev, N.2    Inomata, H.3
  • 52
    • 48849113980 scopus 로고    scopus 로고
    • Production of hydrogen peroxide and redox cycling can explain how sanguinarine and chelerythrine induce rapid apop-tosis
    • Matkar, S.S., Wrischnik, L.A., and Hellmann-Blumberg, U. (2008) Production of hydrogen peroxide and redox cycling can explain how sanguinarine and chelerythrine induce rapid apop-tosis. Archives of Biochemistry and Biophysics. 477, 43-52.
    • (2008) Archives of Biochemistry and Biophysics , vol.477 , pp. 43-52
    • Matkar, S.S.1    Wrischnik, L.A.2    Hellmann-Blumberg, U.3
  • 53
    • 0030014964 scopus 로고    scopus 로고
    • Involvement of the transcription factor NF-kappaB in tubular morphogenesis of human microvascu-lar endothelial cells by oxidative stress
    • Shono, T., Ono, M., Izumi, H. et al. (1996) Involvement of the transcription factor NF-kappaB in tubular morphogenesis of human microvascu-lar endothelial cells by oxidative stress. Molecular and Cellular Biology, 16, 4231-39.
    • (1996) Molecular and Cellular Biology , vol.16 , pp. 4231-4239
    • Shono, T.1    Ono, M.2    Izumi, H.3
  • 54
    • 0012449739 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways in redox signaling
    • Torres, M. (2003) Mitogen-activated protein kinase pathways in redox signaling. Frontiers in Bioscience, 8, d369-91.
    • (2003) Frontiers in Bioscience , vol.8
    • Torres, M.1
  • 55
    • 4143128938 scopus 로고    scopus 로고
    • Role of CaMKII in hydrogen peroxide activation of ERK1/2, p38 MAPK, HSP27 and actin reorganization in endothelial cells
    • Nguyen, A., Chen, P., and Cai, H. (2004) Role of CaMKII in hydrogen peroxide activation of ERK1/2, p38 MAPK, HSP27 and actin reorganization in endothelial cells. FEBS Letters, 572, 307-13.
    • (2004) FEBS Letters , vol.572 , pp. 307-313
    • Nguyen, A.1    Chen, P.2    Cai, H.3
  • 56
    • 14844327760 scopus 로고    scopus 로고
    • Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases
    • Kamata, H., Honda, S., Maeda, S. et al. (2005) Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell, 120, 649-61.
    • (2005) Cell , vol.120 , pp. 649-661
    • Kamata, H.1    Honda, S.2    Maeda, S.3
  • 60
    • 0344889206 scopus 로고    scopus 로고
    • Mechanisms involved in the contraction of endothelial cells by hydrogen peroxide
    • Lopez-Ongil, S., Torrecillas, G., Perez-Sala, D. et al. (1999) Mechanisms involved in the contraction of endothelial cells by hydrogen peroxide. Free Radical Biology and Medicine, 26, 501-10.
    • (1999) Free Radical Biology and Medicine , vol.26 , pp. 501-510
    • Lopez-Ongil, S.1    Torrecillas, G.2    Perez-Sala, D.3
  • 61
    • 0023690817 scopus 로고
    • Exogenous oxidants initiate hydrolysis of endothelial cell inositol phospholipids
    • Shasby, D.M., Yorek, M., and Shasby, S.S. (1988) Exogenous oxidants initiate hydrolysis of endothelial cell inositol phospholipids. Blood, 72, 491-99.
    • (1988) Blood , vol.72 , pp. 491-499
    • Shasby, D.M.1    Yorek, M.2    Shasby, S.S.3
  • 63
    • 0027459024 scopus 로고
    • Activation of endothelial cell phospholi-pase D by hydrogen peroxide and fatty acid hydroperoxide
    • Natarajan, V., Taher, M.M., Roehm, B. et al. (1993) Activation of endothelial cell phospholi-pase D by hydrogen peroxide and fatty acid hydroperoxide. The Journal of Biological Chemistry, 268, 930-37.
    • (1993) The Journal of Biological Chemistry , vol.268 , pp. 930-937
    • Natarajan, V.1    Taher, M.M.2    Roehm, B.3
  • 64
    • 0029074550 scopus 로고
    • Sublethal levels of oxidant stress stimulate multiple serine/threonine kinases and suppress protein phosphatases in Jurkat T cells
    • Whisler, R.L., Goyette, M.A., Grants, I.S., and Newhouse, Y.G. (1995) Sublethal levels of oxidant stress stimulate multiple serine/threonine kinases and suppress protein phosphatases in Jurkat T cells. Archives of Biochemistry and Biophysics, 319, 23-35.
    • (1995) Archives of Biochemistry and Biophysics , vol.319 , pp. 23-35
    • Whisler, R.L.1    Goyette, M.A.2    Grants, I.S.3    Newhouse, Y.G.4
  • 65
    • 0029860416 scopus 로고    scopus 로고
    • Effect of antioxidants on lipopolysaccharide-stimulated induction of mangano superoxide dismutase mRNA in bovine pulmonary artery endothelial cells
    • Mitchell, J., Jiang, H., Berry, L., and Meyrick, B. (1996) Effect of antioxidants on lipopolysaccharide-stimulated induction of mangano superoxide dismutase mRNA in bovine pulmonary artery endothelial cells. Journal of Cellular Physiology, 169, 333-40.
    • (1996) Journal of Cellular Physiology , vol.169 , pp. 333-340
    • Mitchell, J.1    Jiang, H.2    Berry, L.3    Meyrick, B.4
  • 66
    • 36749014121 scopus 로고    scopus 로고
    • Redox regulation of lung inflammation: role of NADPH oxidase and NF-kappaB signalling
    • Yao, H., Yang, S.R., Kode, A. et al. (2007) Redox regulation of lung inflammation: role of NADPH oxidase and NF-kappaB signalling. Biochemical Society Transactions, 35, 1151-55.
    • (2007) Biochemical Society Transactions , vol.35 , pp. 1151-1155
    • Yao, H.1    Yang, S.R.2    Kode, A.3
  • 67
    • 0033570031 scopus 로고    scopus 로고
    • Simulated ischemia in flow-adapted endothelial cells leads to generation of reactive oxygen species and cell signaling
    • Wei, Z., Costa, K., Al-Mehdi, A.B. et al. (1999) Simulated ischemia in flow-adapted endothelial cells leads to generation of reactive oxygen species and cell signaling. Circulation Research, 85, 682-89.
    • (1999) Circulation Research , vol.85 , pp. 682-689
    • Wei, Z.1    Costa, K.2    Al-Mehdi, A.B.3
  • 68
    • 33750523632 scopus 로고    scopus 로고
    • NF-kappaB activation by reactive oxygen species: fifteen years later
    • Gloire, G., Legrand-Poels, S., and Piette, J. (2006) NF-kappaB activation by reactive oxygen species: fifteen years later. Biochemical Pharmacology, 72, 1493-505.
    • (2006) Biochemical Pharmacology , vol.72 , pp. 1493-1505
    • Gloire, G.1    Legrand-Poels, S.2    Piette, J.3
  • 69
    • 0034830641 scopus 로고    scopus 로고
    • Impaired pulmonary NF-kappaB activation in response to lipopolysaccharide in NADPH oxidase-deficient mice
    • Koay, M.A., Christman, J.W., Segal, B.H. et al. (2001) Impaired pulmonary NF-kappaB activation in response to lipopolysaccharide in NADPH oxidase-deficient mice. Infection and Immunity, 69, 5991-96.
    • (2001) Infection and Immunity , vol.69 , pp. 5991-5996
    • Koay, M.A.1    Christman, J.W.2    Segal, B.H.3
  • 70
    • 1642525695 scopus 로고    scopus 로고
    • phox deficiency impairs activation and host defense in Pseudomonas pneumonia
    • phox deficiency impairs activation and host defense in Pseudomonas pneumonia. Journal of Immunology, 172, 1801-8.
    • (2004) Journal of Immunology , vol.172 , pp. 1801-1808
    • Sadikot, R.T.1    Zeng, H.2    Yull, F.E.3
  • 71
    • 0035877211 scopus 로고    scopus 로고
    • Surfactant protein D regulates NF-kappa B and matrix metalloproteinase production in alveolar macrophages via oxidant-sensitive pathways
    • Yoshida, M., Korfhagen, T.R., and Whitsett, J.A. (2001) Surfactant protein D regulates NF-kappa B and matrix metalloproteinase production in alveolar macrophages via oxidant-sensitive pathways. Journal of Immunology, 166, 7514-19.
    • (2001) Journal of Immunology , vol.166 , pp. 7514-7519
    • Yoshida, M.1    Korfhagen, T.R.2    Whitsett, J.A.3
  • 72
    • 29244473882 scopus 로고    scopus 로고
    • Nrf2-deficient mice are highly susceptible to cigarette smoke-induced emphysema
    • Iizuka, T., Ishii, Y., Itoh, K. et al. (2005) Nrf2-deficient mice are highly susceptible to cigarette smoke-induced emphysema. Genes to Cells, 10, 1113-25.
    • (2005) Genes to Cells , vol.10 , pp. 1113-1125
    • Iizuka, T.1    Ishii, Y.2    Itoh, K.3
  • 73
    • 22344438250 scopus 로고    scopus 로고
    • Disruption of Nrf2 enhances susceptibility to severe airway inflammation and asthma in mice
    • Rangasamy, T., Guo, J., Mitzner, W.A. et al. (2005) Disruption of Nrf2 enhances susceptibility to severe airway inflammation and asthma in mice. The Journal ofExperimental Medicine, 202, 47-59.
    • (2005) The Journal ofExperimental Medicine , vol.202 , pp. 47-59
    • Rangasamy, T.1    Guo, J.2    Mitzner, W.A.3
  • 74
    • 33750826092 scopus 로고    scopus 로고
    • Nrf2-dependent protection from LPS induced inflammatory response and mortality by CDDO-imidazolide
    • Thimmulappa, R.K., Scollick, C., Traore, K. et al. (2006) Nrf2-dependent protection from LPS induced inflammatory response and mortality by CDDO-imidazolide. Biochemical and Biophysical Research Communications, 351, 883-89.
    • (2006) Biochemical and Biophysical Research Communications , vol.351 , pp. 883-889
    • Thimmulappa, R.K.1    Scollick, C.2    Traore, K.3
  • 75
    • 18344416054 scopus 로고    scopus 로고
    • Nitrosative stress and transcription
    • Kroncke, K.D. (2003) Nitrosative stress and transcription. Biological Chemistry, 384, 1365-77.
    • (2003) Biological Chemistry , vol.384 , pp. 1365-1377
    • Kroncke, K.D.1
  • 76
    • 33847350668 scopus 로고    scopus 로고
    • Nitric oxide promotes endothelial cell survival signaling through S-nitrosylation and activation of dynamin-2
    • Kang-Decker, N., Cao, S., Chatterjee, S. et al. (2007) Nitric oxide promotes endothelial cell survival signaling through S-nitrosylation and activation of dynamin-2. Journal of Cell Science, 120, 492-501.
    • (2007) Journal of Cell Science , vol.120 , pp. 492-501
    • Kang-Decker, N.1    Cao, S.2    Chatterjee, S.3
  • 77
    • 44449119080 scopus 로고    scopus 로고
    • Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins
    • Benhar, M., Forrester, M.T., Hess, D.T., and Stam-ler, J.S. (2008) Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science, 320, 1050-54.
    • (2008) Science , vol.320 , pp. 1050-1054
    • Benhar, M.1    Forrester, M.T.2    Hess, D.T.3    Stam-Ler, J.S.4
  • 78
    • 0032972249 scopus 로고    scopus 로고
    • Urinary excretion of biomarkers for radical-induced damage in rats treated with NDMA or diquat and the effects of calcium carbimide co-administration
    • de Zwart, L.L., Vermeulen, N.P., Hermanns, R.C. et al. (1999) Urinary excretion of biomarkers for radical-induced damage in rats treated with NDMA or diquat and the effects of calcium carbimide co-administration. Chemico-Biological Interactions, 117, 151-72.
    • (1999) Chemico-Biological Interactions , vol.117 , pp. 151-172
    • De Zwart, L.L.1    Vermeulen, N.P.2    Hermanns, R.C.3
  • 79
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge, W. (2002) Free radicals in the physiological control of cell function. Physiological Reviews, 82, 47-95.
    • (2002) Physiological Reviews , vol.82 , pp. 47-95
    • Droge, W.1
  • 80
    • 0036274561 scopus 로고    scopus 로고
    • Reactive species mediated injury of human lung epithelial cells after hypoxia-reoxygenation
    • Li, C., Wright, M.M., and Jackson, R.M. (2002) Reactive species mediated injury of human lung epithelial cells after hypoxia-reoxygenation. Experimental Lung Research, 28, 373-89.
    • (2002) Experimental Lung Research , vol.28 , pp. 373-389
    • Li, C.1    Wright, M.M.2    Jackson, R.M.3
  • 82
    • 0026691086 scopus 로고
    • Role of oxygen in oxidation of lipid and protein during ischemia/reperfusion in isolated perfused rat lung
    • Ayene, I.S., Dodia, C., and Fisher, A.B. (1992) Role of oxygen in oxidation of lipid and protein during ischemia/reperfusion in isolated perfused rat lung. Archives of Biochemistry and Biophysics, 296, 183-89.
    • (1992) Archives of Biochemistry and Biophysics , vol.296 , pp. 183-189
    • Ayene, I.S.1    Dodia, C.2    Fisher, A.B.3
  • 83
    • 0027538063 scopus 로고
    • 2 inhibitor decreases generation of thiobarbituric acid reactive substance during lung ischemia-reperfusion
    • 2 inhibitor decreases generation of thiobarbituric acid reactive substance during lung ischemia-reperfusion. Biochimica et Biophysica Acta, 1167, 56-62.
    • (1993) Biochimica et Biophysica Acta , vol.1167 , pp. 56-62
    • Al-Mehdi, A.B.1    Dodia, C.2    Jain, M.K.3    Fisher, A.B.4
  • 85
    • 0034703973 scopus 로고    scopus 로고
    • 2+-and phosphatidylinosi-tol 3-kinase-dependent nitric oxide generation in lung endothelial cells in situ with ischemia
    • 2+-and phosphatidylinosi-tol 3-kinase-dependent nitric oxide generation in lung endothelial cells in situ with ischemia. The Journal ofBiological Chemistry, 275, 39807-10.
    • (2000) The Journal ofBiological Chemistry , vol.275 , pp. 39807-39810
    • Al-Mehdi, A.B.1    Song, C.2    Tozawa, K.3    Fisher, A.B.4
  • 86
    • 0037443708 scopus 로고    scopus 로고
    • Fluorescence imaging of lipid peroxidation in isolated rat lungs during nonhypoxic lung ischemia
    • Matot, I., Manevich, Y., Al-Mehdi, A.B. et al. (2003) Fluorescence imaging of lipid peroxidation in isolated rat lungs during nonhypoxic lung ischemia. Free Radical Biology and Medicine, 34, 785-90.
    • (2003) Free Radical Biology and Medicine , vol.34 , pp. 785-790
    • Matot, I.1    Manevich, Y.2    Al-Mehdi, A.B.3
  • 87
    • 0029915115 scopus 로고    scopus 로고
    • The selenoenzyme phospholipid hydroperoxide glutathione peroxidase controls the activity of the 15-lipoxygenase with complex substrates and preserves the specificity of the oxygenation products
    • Schnurr, K., Belkner, J., Ursini, F. et al. (1996) The selenoenzyme phospholipid hydroperoxide glutathione peroxidase controls the activity of the 15-lipoxygenase with complex substrates and preserves the specificity of the oxygenation products. The Journal of Biological Chemistry, 271, 4653-58.
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 4653-4658
    • Schnurr, K.1    Belkner, J.2    Ursini, F.3
  • 89
    • 0042664003 scopus 로고    scopus 로고
    • L-PhGPx expression can be suppressed by antisense oligodeoxynucleotides
    • Zhao, L., Wang, H.P., Zhang, H.J. et al. (2003) L-PhGPx expression can be suppressed by antisense oligodeoxynucleotides. Archives of Biochemistry and Biophysics, 417, 212-18.
    • (2003) Archives of Biochemistry and Biophysics , vol.417 , pp. 212-218
    • Zhao, L.1    Wang, H.P.2    Zhang, H.J.3
  • 91
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett, B.S. and Stadtman, E.R. (1997) Protein oxidation in aging, disease, and oxidative stress. The Journal of Biological Chemistry, 272, 20313-16.
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 92
    • 12844277331 scopus 로고    scopus 로고
    • Protein maintenance in aging and replicative senescence: a role for the peptide methionine sulfoxide reductases
    • Petropoulos, I. and Friguet, B. (2005) Protein maintenance in aging and replicative senescence: a role for the peptide methionine sulfoxide reductases. Biochimica et Biophysica Acta, 1703, 261-66.
    • (2005) Biochimica et Biophysica Acta , vol.1703 , pp. 261-266
    • Petropoulos, I.1    Friguet, B.2
  • 93
    • 34248583109 scopus 로고    scopus 로고
    • Protein oxidation, repair mechanisms and proteolysis in Saccharomyces cerevisiae
    • Costa, V., Quintanilha, A., and Moradas-Ferreira, P. (2007) Protein oxidation, repair mechanisms and proteolysis in Saccharomyces cerevisiae. IUBMB Life, 59, 293-98.
    • (2007) IUBMB Life , vol.59 , pp. 293-298
    • Costa, V.1    Quintanilha, A.2    Moradas-Ferreira, P.3
  • 95
    • 0038322044 scopus 로고    scopus 로고
    • Mode of inhibition of short-patch base excision repair by thymine glycol within clustered DNA lesions
    • Budworth, H. and Dianov, G.L. (2003) Mode of inhibition of short-patch base excision repair by thymine glycol within clustered DNA lesions. The Journal of Biological Chemistry, 278, 9378-81.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 9378-9381
    • Budworth, H.1    Dianov, G.L.2
  • 96
    • 0035174362 scopus 로고    scopus 로고
    • Regulation of bleomycin-induced DNA breakage and chromatin structure in lung endothelial cells by integrins and poly(ADP-ribose) polymerase
    • Jones, C.B., McIntosh, J., Huang, H. et al. (2001) Regulation of bleomycin-induced DNA breakage and chromatin structure in lung endothelial cells by integrins and poly(ADP-ribose) polymerase. Molecular Pharmacology, 59, 69-75.
    • (2001) Molecular Pharmacology , vol.59 , pp. 69-75
    • Jones, C.B.1    McIntosh, J.2    Huang, H.3
  • 98
    • 2942523593 scopus 로고    scopus 로고
    • Endogenous DNA damage in humans: a review of quantitative data
    • De Bont, R. and van Larebeke, N. (2004) Endogenous DNA damage in humans: a review of quantitative data. Mutagenesis, 19, 169-85.
    • (2004) Mutagenesis , vol.19 , pp. 169-185
    • De Bont, R.1    Van Larebeke, N.2
  • 99
    • 0035348181 scopus 로고    scopus 로고
    • Hypoxia promotes oxidative base modifications in the pulmonary artery endothelial cell VEGF gene
    • Grishko, V., Solomon, M., Breit, J.F. et al. (2001) Hypoxia promotes oxidative base modifications in the pulmonary artery endothelial cell VEGF gene. The FASEB Journal, 15, 1267-69.
    • (2001) The FASEB Journal , vol.15 , pp. 1267-1269
    • Grishko, V.1    Solomon, M.2    Breit, J.F.3
  • 102
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide
    • Radi, R., Beckman, J.S., Bush, K.M., and Freeman, B.A. (1991) Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide. The Journal of Biological Chemistry, 266, 4244-50.
    • (1991) The Journal of Biological Chemistry , vol.266 , pp. 4244-4250
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 106
    • 0032147208 scopus 로고    scopus 로고
    • Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species
    • Ischiropoulos, H. (1998) Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species. Archives of Biochemistry and Biophysics, 356, 1-11.
    • (1998) Archives of Biochemistry and Biophysics , vol.356 , pp. 1-11
    • Ischiropoulos, H.1
  • 108
    • 0034925593 scopus 로고    scopus 로고
    • Tyrosine nitration: localisation, quantification, consequences for protein function and signal transduction
    • Greenacre, S.A. and Ischiropoulos, H. (2001) Tyrosine nitration: localisation, quantification, consequences for protein function and signal transduction. Free Radical Research, 34, 541-81.
    • (2001) Free Radical Research , vol.34 , pp. 541-581
    • Greenacre, S.A.1    Ischiropoulos, H.2
  • 109
    • 0037177860 scopus 로고    scopus 로고
    • Nitric oxide (NO) induces nitration of protein kinase Cepsilon (PKCepsilon ), facilitating PKCepsilon translocation via enhanced PKCepsilon-RACK2 interactions: a novel mechanism of no-triggered activation of PKCepsilon
    • Balafanova, Z., Bolli, R., Zhang, J. et al. (2002) Nitric oxide (NO) induces nitration of protein kinase Cepsilon (PKCepsilon ), facilitating PKCepsilon translocation via enhanced PKCepsilon-RACK2 interactions: a novel mechanism of no-triggered activation of PKCepsilon. The Journal of Biological Chemistry, 277, 15021-27.
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 15021-15027
    • Balafanova, Z.1    Bolli, R.2    Zhang, J.3
  • 110
    • 0030002384 scopus 로고    scopus 로고
    • Effects of peroxynitrite-induced protein modifications on tyrosine phosphorylation and degradation
    • Gow, A.J., Duran, D., Malcolm, S., and Ischi-ropoulos, H. (1996) Effects of peroxynitrite-induced protein modifications on tyrosine phosphorylation and degradation. FEBS Letters, 385, 63-66.
    • (1996) FEBS Letters , vol.385 , pp. 63-66
    • Gow, A.J.1    Duran, D.2    Malcolm, S.3    Ischi-Ropoulos, H.4
  • 113
    • 0035902957 scopus 로고    scopus 로고
    • Nitrotyrosine mimics phosphotyrosine binding to the SH2 domain of the src family tyrosine kinase lyn
    • Mallozzi, C., Di Stasi, A.M., and Minetti, M. (2001) Nitrotyrosine mimics phosphotyrosine binding to the SH2 domain of the src family tyrosine kinase lyn. FEBS Letters, 503, 189-95.
    • (2001) FEBS Letters , vol.503 , pp. 189-195
    • Mallozzi, C.1    Di Stasi, A.M.2    Minetti, M.3
  • 116
    • 0018643205 scopus 로고
    • Indicator dilution measurement of 5-hydroxytryptamine clearance by human lung
    • Gillis, C.N., Cronau, L.H., Mandel, S., and Hammond, G.L. (1979) Indicator dilution measurement of 5-hydroxytryptamine clearance by human lung. Journal of Applied Physiology, 46, 1178-83.
    • (1979) Journal of Applied Physiology , vol.46 , pp. 1178-1183
    • Gillis, C.N.1    Cronau, L.H.2    Mandel, S.3    Hammond, G.L.4
  • 117
    • 0017595792 scopus 로고
    • Hyperoxia and lung serotonin clearance: a new observation
    • Block, E.R. and Fisher, A.B. (1977) Hyperoxia and lung serotonin clearance: a new observation. Chest, 71, 289-91.
    • (1977) Chest , vol.71 , pp. 289-291
    • Block, E.R.1    Fisher, A.B.2
  • 118
    • 0017752214 scopus 로고
    • Prevention of hyperoxic-induced depression of pulmonary serotonin clearance by pretreatment with superoxide dismutase
    • Block, E.R. and Fisher, A.B. (1977) Prevention of hyperoxic-induced depression of pulmonary serotonin clearance by pretreatment with superoxide dismutase. The American Review of Respiratory Disease, 116, 441-47.
    • (1977) The American Review of Respiratory Disease , vol.116 , pp. 441-447
    • Block, E.R.1    Fisher, A.B.2
  • 120
    • 0014217361 scopus 로고
    • Conversion of angiotensin I to angiotensin II
    • Ng, K.K. and Vane, J.R. (1967) Conversion of angiotensin I to angiotensin II. Nature, 216, 762-66.
    • (1967) Nature , vol.216 , pp. 762-766
    • Ng, K.K.1    Vane, J.R.2
  • 121
    • 0017234204 scopus 로고
    • Localization of angiotensin converting enzyme (kininase II). II. Immunocytochemistry and immunofluorescence
    • Ryan, U.S., Ryan, J.W., Whitaker, C., and Chiu, A. (1976) Localization of angiotensin converting enzyme (kininase II). II. Immunocytochemistry and immunofluorescence. Tissue and Cell, 8, 125-45.
    • (1976) Tissue and Cell , vol.8 , pp. 125-145
    • Ryan, U.S.1    Ryan, J.W.2    Whitaker, C.3    Chiu, A.4
  • 122
    • 0001722753 scopus 로고    scopus 로고
    • Angiotensin-1-converting enzyme (CD143) on endothelial cells in normal and in pathological conditions
    • in, (eds T. Kishimoto, H. Kikutani, A.E.G.Kr. von dem Borne et al.), Garland, New York
    • Metzger, F.F., Bohle, R., Kerkman, L. et al. (1997) Angiotensin-1-converting enzyme (CD143) on endothelial cells in normal and in pathological conditions, in Leukocyte Typing VI. White Cell Differentiation Antigens (eds T. Kishimoto, H. Kikutani, A.E.G.Kr. von dem Borne et al.), Garland, New York, pp. 749-51.
    • (1997) Leukocyte Typing VI. White Cell Differentiation Antigens , pp. 749-751
    • Metzger, F.F.1    Bohle, R.2    Kerkman, L.3
  • 124
    • 0026086627 scopus 로고
    • A new approach to the investigation of oxidative injury to the pulmonary endothelium: use of angiotensin-converting enzyme as a marker
    • Muzykantov, V.R. and Danilov, S.M. (1991) A new approach to the investigation of oxidative injury to the pulmonary endothelium: use of angiotensin-converting enzyme as a marker. Biomedical Science, 2, 11-21.
    • (1991) Biomedical Science , vol.2 , pp. 11-21
    • Muzykantov, V.R.1    Danilov, S.M.2
  • 125
    • 0030874071 scopus 로고    scopus 로고
    • Normoxic lung ischemia/ reperfusion accelerates shedding of angiotensin converting enzyme from the pulmonary endothelium
    • Atochina, E.N., Muzykantov, V.R., Al-Mehdi, A.B. et al. (1997) Normoxic lung ischemia/ reperfusion accelerates shedding of angiotensin converting enzyme from the pulmonary endothelium. American Journal of Respiratory and Critical Care Medicine, 156, 1114-19.
    • (1997) American Journal of Respiratory and Critical Care Medicine , vol.156 , pp. 1114-1119
    • Atochina, E.N.1    Muzykantov, V.R.2    Al-Mehdi, A.B.3
  • 126
    • 0034680306 scopus 로고    scopus 로고
    • Pulmonary capillary endothelium-bound angiotensin-converting enzyme activity in acute lung injury
    • Orfanos, S.E., Armaganidis, A., Glynos, C. et al. (2000) Pulmonary capillary endothelium-bound angiotensin-converting enzyme activity in acute lung injury. Circulation, 102, 2011-18.
    • (2000) Circulation , vol.102 , pp. 2011-2018
    • Orfanos, S.E.1    Armaganidis, A.2    Glynos, C.3
  • 128
    • 0030603783 scopus 로고    scopus 로고
    • Evidence for modulation of hydrogen peroxide-induced endothelial barrier dysfunction by nitric oxide in vitro
    • McQuaid, K.E., Smyth, E.M., and Keenan, A.K. (1996) Evidence for modulation of hydrogen peroxide-induced endothelial barrier dysfunction by nitric oxide in vitro. European Journal of Pharmacology, 307, 233-41.
    • (1996) European Journal of Pharmacology , vol.307 , pp. 233-241
    • McQuaid, K.E.1    Smyth, E.M.2    Keenan, A.K.3
  • 129
    • 0142242347 scopus 로고    scopus 로고
    • Effect of ischemia and reperfusion without airway occlusion on vascular barrier function in the in vivo mouse lung
    • Dodd-o, J.M., Hristopoulos, M.L., Faraday, N., and Pearse, D.B. (2003) Effect of ischemia and reperfusion without airway occlusion on vascular barrier function in the in vivo mouse lung. Journal of Applied Physiology, 95, 1971-78.
    • (2003) Journal of Applied Physiology , vol.95 , pp. 1971-1978
    • Dodd-O, J.M.1    Hristopoulos, M.L.2    Faraday, N.3    Pearse, D.B.4
  • 130
    • 0345258511 scopus 로고    scopus 로고
    • Redox regulation of reactive oxygen species-induced p38 MAP kinase activation and barrier dysfunction in lung microvascular endothelial cells
    • Usatyuk, P.V., Vepa, S., Watkins, T. et al. (2003) Redox regulation of reactive oxygen species-induced p38 MAP kinase activation and barrier dysfunction in lung microvascular endothelial cells. Antioxidants and Redox Signaling, 5, 723-30.
    • (2003) Antioxidants and Redox Signaling , vol.5 , pp. 723-730
    • Usatyuk, P.V.1    Vepa, S.2    Watkins, T.3
  • 132
    • 33645688912 scopus 로고    scopus 로고
    • Hyperoxia-induced reactive oxygen species formation in pulmonary capillary endothelial cells in situ
    • Brueckl, C., Kaestle, S., Kerem, A. et al. (2006) Hyperoxia-induced reactive oxygen species formation in pulmonary capillary endothelial cells in situ. American Journal of Respiratory Cell and Molecular Biology, 34, 453-63.
    • (2006) American Journal of Respiratory Cell and Molecular Biology , vol.34 , pp. 453-463
    • Brueckl, C.1    Kaestle, S.2    Kerem, A.3
  • 133
    • 33745223933 scopus 로고    scopus 로고
    • Reactive oxygen species in vascular endothelial cell motility. Roles of NAD(P)H oxidase and Rac1
    • Moldovan, L., Mythreye, K., Goldschmidt-Clermont, P.J., and Satterwhite, L.L. (2006) Reactive oxygen species in vascular endothelial cell motility. Roles of NAD(P)H oxidase and Rac1. Cardiovascular Research, 71, 236-46.
    • (2006) Cardiovascular Research , vol.71 , pp. 236-246
    • Moldovan, L.1    Mythreye, K.2    Goldschmidt-Clermont, P.J.3    Satterwhite, L.L.4
  • 135
    • 0026059929 scopus 로고
    • Oxygen radicals induce human endothelial cells to express GMP-140 and bind neutrophils
    • Patel, K.D., Zimmerman, G.A., Prescott, S.M. et al. (1991) Oxygen radicals induce human endothelial cells to express GMP-140 and bind neutrophils. The Journal of Cell Biology, 112, 749-59.
    • (1991) The Journal of Cell Biology , vol.112 , pp. 749-759
    • Patel, K.D.1    Zimmerman, G.A.2    Prescott, S.M.3
  • 138
    • 0028978703 scopus 로고
    • 2 and tumor necrosis factor-alpha activate intercellular adhesion molecule 1 (ICAM-1) gene transcription through distinct cis-regulatory elements within the ICAM-1 promoter
    • 2 and tumor necrosis factor-alpha activate intercellular adhesion molecule 1 (ICAM-1) gene transcription through distinct cis-regulatory elements within the ICAM-1 promoter. The Journal of Biological Chemistry, 270, 18966-74.
    • (1995) The Journal of Biological Chemistry , vol.270 , pp. 18966-18974
    • Roebuck, K.A.1    Rahman, A.2    Lakshminarayanan, V.3
  • 139
    • 0033583116 scopus 로고    scopus 로고
    • Molecular mechanisms of neutrophil-endothelial cell adhesion induced by redox imbalance
    • Kokura, S., Wolf, R.E., Yoshikawa, T. et al. (1999) Molecular mechanisms of neutrophil-endothelial cell adhesion induced by redox imbalance. Circulation Research, 84, 516-24.
    • (1999) Circulation Research , vol.84 , pp. 516-524
    • Kokura, S.1    Wolf, R.E.2    Yoshikawa, T.3
  • 140
    • 15644369365 scopus 로고    scopus 로고
    • Differential contribution of various adhesion molecules to leukocyte kinetics in pulmonary microvessels of hyperoxia-exposed rat lungs
    • Nishio, K., Suzuki, Y., Aoki, T. et al. (1998) Differential contribution of various adhesion molecules to leukocyte kinetics in pulmonary microvessels of hyperoxia-exposed rat lungs. American Journal of Respiratory and Critical Care Medicine, 157, 599-609.
    • (1998) American Journal of Respiratory and Critical Care Medicine , vol.157 , pp. 599-609
    • Nishio, K.1    Suzuki, Y.2    Aoki, T.3
  • 141
    • 0031950444 scopus 로고    scopus 로고
    • In vivo regulation of PECAM-1 activity during acute endothelial dysfunction in the rat mesenteric microvasculature
    • Scalia, R. and Lefer, A.M. (1998) In vivo regulation of PECAM-1 activity during acute endothelial dysfunction in the rat mesenteric microvasculature. Journal of Leukocyte Biology, 64, 163-69.
    • (1998) Journal of Leukocyte Biology , vol.64 , pp. 163-169
    • Scalia, R.1    Lefer, A.M.2
  • 142
    • 0033059141 scopus 로고    scopus 로고
    • Differential activation of some transcription factors during rat liver ischemia, reperfusion, and heat shock
    • Tacchini, L., Radice, L., and Bernelli-Zazzera, A. (1999) Differential activation of some transcription factors during rat liver ischemia, reperfusion, and heat shock. Journal of Cellular Physiology, 180, 255-62.
    • (1999) Journal of Cellular Physiology , vol.180 , pp. 255-262
    • Tacchini, L.1    Radice, L.2    Bernelli-Zazzera, A.3
  • 144
    • 0036829765 scopus 로고    scopus 로고
    • Oxidative stress and neutrophil activation-the two keystones of ischemia/reperfusion injury
    • Kaminski, K.A., Bonda, T.A., Korecki, J., and Musial, W.J. (2002) Oxidative stress and neutrophil activation-the two keystones of ischemia/reperfusion injury. International Journal of Cardiology, 86, 41-59.
    • (2002) International Journal of Cardiology , vol.86 , pp. 41-59
    • Kaminski, K.A.1    Bonda, T.A.2    Korecki, J.3    Musial, W.J.4
  • 145
    • 33847291917 scopus 로고    scopus 로고
    • Carbon monoxide protects against hyperoxia-induced endothelial cell apoptosis by inhibiting reactive oxygen species formation
    • Wang, X., Wang, Y., Kim, H.P. et al. (2007) Carbon monoxide protects against hyperoxia-induced endothelial cell apoptosis by inhibiting reactive oxygen species formation. The Journal of Biological Chemistry, 282, 1718-26.
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 1718-1726
    • Wang, X.1    Wang, Y.2    Kim, H.P.3
  • 146
    • 27144528184 scopus 로고    scopus 로고
    • Wood smoke extract induces oxidative stress-mediated caspase-independent apoptosis in human lung endothelial cells: role of AIF and En-doG
    • Liu, P.L., Chen, Y.L., Chen, Y.H. et al. (2005) Wood smoke extract induces oxidative stress-mediated caspase-independent apoptosis in human lung endothelial cells: role of AIF and En-doG. American Journal of Physiology: Lung Cellular and Molecular Physiology, 289, L739-49.
    • (2005) American Journal of Physiology: Lung Cellular and Molecular Physiology , vol.289
    • Liu, P.L.1    Chen, Y.L.2    Chen, Y.H.3
  • 148
    • 34548168822 scopus 로고    scopus 로고
    • Regulation of hyperoxia-induced NADPH oxidase activation in human lung endothelial cells by the actin cytoskeleton and cortactin
    • Usatyuk, P.V., Romer, L.H., He, D. et al. (2007) Regulation of hyperoxia-induced NADPH oxidase activation in human lung endothelial cells by the actin cytoskeleton and cortactin. The Journal of Biological Chemistry, 282, 23284-95.
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 23284-23295
    • Usatyuk, P.V.1    Romer, L.H.2    He, D.3
  • 149
    • 0022559220 scopus 로고
    • Morphologic changes in pulmonary oxygen toxicity
    • Crapo, J.D. (1986) Morphologic changes in pulmonary oxygen toxicity. Annual Review of Physiology, 48, 721-31.
    • (1986) Annual Review of Physiology , vol.48 , pp. 721-731
    • Crapo, J.D.1
  • 150
    • 84944487992 scopus 로고
    • The pathological effects due to increase of oxygen tension in air breathed
    • Smith, J.L. (1899) The pathological effects due to increase of oxygen tension in air breathed. The Journal of Physiology, 24, 19-35.
    • (1899) The Journal of Physiology , vol.24 , pp. 19-35
    • Smith, J.L.1
  • 151
    • 0021143804 scopus 로고
    • Mechanisms of pulmonary oxygen toxicity
    • Fisher, A.B., Forman, H.J., and Glass, M. (1984) Mechanisms of pulmonary oxygen toxicity. Lung, 162, 255-59.
    • (1984) Lung , vol.162 , pp. 255-259
    • Fisher, A.B.1    Forman, H.J.2    Glass, M.3
  • 154
    • 0024266108 scopus 로고
    • Role of polymorphonuclear leukocytes in hyperoxic lung injury. Prevention of neutrophil influx into the lung endothelium during oxygen exposure by ibuprofen
    • Das, D.K., Bandyopadhyay, D., Hoory, S., and Steinberg, H. (1988) Role of polymorphonuclear leukocytes in hyperoxic lung injury. Prevention of neutrophil influx into the lung endothelium during oxygen exposure by ibuprofen. Biomedica Biochimica Acta, 47, 1023-36.
    • (1988) Biomedica Biochimica Acta , vol.47 , pp. 1023-1036
    • Das, D.K.1    Bandyopadhyay, D.2    Hoory, S.3    Steinberg, H.4
  • 155
    • 0023257360 scopus 로고
    • The physiology of intestinal oxygenation and the pathophysiology of intestinal ileus
    • Malone, P.C. (1987) The physiology of intestinal oxygenation and the pathophysiology of intestinal ileus. Medical Hypotheses, 22, 111-57.
    • (1987) Medical Hypotheses , vol.22 , pp. 111-157
    • Malone, P.C.1
  • 156
    • 33644957463 scopus 로고    scopus 로고
    • Hypoxia-induced reactive oxygen species down-regulate ETB receptor-mediated contraction of rat pulmonary arteries
    • Wang, X., Tong, M., Chinta, S. et al. (2006) Hypoxia-induced reactive oxygen species down-regulate ETB receptor-mediated contraction of rat pulmonary arteries. American Journal of Physiology: Lung Cellular and Molecular Physiology, 290, L570-78.
    • (2006) American Journal of Physiology: Lung Cellular and Molecular Physiology , vol.290
    • Wang, X.1    Tong, M.2    Chinta, S.3
  • 157
    • 36249010820 scopus 로고    scopus 로고
    • Sequence-specific oxidative base modifications in hypoxia-inducible genes
    • Pastukh, V., Ruchko, M., Gorodnya, O. et al. (2007) Sequence-specific oxidative base modifications in hypoxia-inducible genes. Free Radical Biology and Medicine, 43, 1616-26.
    • (2007) Free Radical Biology and Medicine , vol.43 , pp. 1616-1626
    • Pastukh, V.1    Ruchko, M.2    Gorodnya, O.3
  • 158
    • 0021984681 scopus 로고
    • Oxygen-derived free radicals in postischemic tissue injury
    • McCord, J.M. (1985) Oxygen-derived free radicals in postischemic tissue injury. The New England Journal of Medicine, 312, 159-63.
    • (1985) The New England Journal of Medicine , vol.312 , pp. 159-163
    • McCord, J.M.1
  • 159
    • 45549094799 scopus 로고    scopus 로고
    • Bench-to-bedside review: mitochondrial injury, oxidative stress and apoptosis-there is nothing more practical than a good theory
    • Bayir, H. and Kagan, V.E. (2008) Bench-to-bedside review: mitochondrial injury, oxidative stress and apoptosis-there is nothing more practical than a good theory. Critical Care, 12, 206.
    • (2008) Critical Care , vol.12 , pp. 206
    • Bayir, H.1    Kagan, V.E.2
  • 160
    • 0019921584 scopus 로고
    • The role of lipid peroxidation in pathogenesis of ischemic damage and the antioxidant protection of the heart
    • Meerson, F.Z., Kagan, V.E., Kozlov, Y.P. et al. (1982) The role of lipid peroxidation in pathogenesis of ischemic damage and the antioxidant protection of the heart. Basic Research in Cardiology, 77, 465-85.
    • (1982) Basic Research in Cardiology , vol.77 , pp. 465-485
    • Meerson, F.Z.1    Kagan, V.E.2    Kozlov, Y.P.3
  • 163
    • 33646382128 scopus 로고    scopus 로고
    • Prevention of ischemia reperfusion injury by positive pulmonary venous pressure in isolated rat lung
    • Georgieva, G.S., Kurata, S., Ikeda, S. et al. (2006) Prevention of ischemia reperfusion injury by positive pulmonary venous pressure in isolated rat lung. Shock, 25, 66-72.
    • (2006) Shock , vol.25 , pp. 66-72
    • Georgieva, G.S.1    Kurata, S.2    Ikeda, S.3
  • 164
    • 0029072762 scopus 로고
    • Flow-mediated endothelial mechanotransduction
    • Davies, P.F. (1995) Flow-mediated endothelial mechanotransduction. Physiological Reviews, 75, 519-60.
    • (1995) Physiological Reviews , vol.75 , pp. 519-560
    • Davies, P.F.1
  • 165
  • 166
    • 0037402442 scopus 로고    scopus 로고
    • Cellular mechanics and gene expression in blood vessels
    • Lehoux, S. and Tedgui, A. (2003) Cellular mechanics and gene expression in blood vessels. Journal of Biomechanics, 36, 631-43.
    • (2003) Journal of Biomechanics , vol.36 , pp. 631-643
    • Lehoux, S.1    Tedgui, A.2
  • 167
    • 50849143789 scopus 로고    scopus 로고
    • Caveolae are an essential component of the pathway for endothelial cell signaling associated with abrupt reduction of shear stress
    • Milovanova, T., Chatterjee, S., Hawkins, B.J. et al. (2008) Caveolae are an essential component of the pathway for endothelial cell signaling associated with abrupt reduction of shear stress. Biochimica et Biophysica Acta, 1783, 1866-75.
    • (2008) Biochimica et Biophysica Acta , vol.1783 , pp. 1866-1875
    • Milovanova, T.1    Chatterjee, S.2    Hawkins, B.J.3
  • 168
    • 33750629317 scopus 로고    scopus 로고
    • KATP channels are an important component of the shear-sensing mechanism in the pulmonary microvasculature
    • Chatterjee, S., Levitan, I., Wei, Z., and Fisher, A.B. (2006) KATP channels are an important component of the shear-sensing mechanism in the pulmonary microvasculature. Microcirculation, 13, 633-44.
    • (2006) Microcirculation , vol.13 , pp. 633-644
    • Chatterjee, S.1    Levitan, I.2    Wei, Z.3    Fisher, A.B.4
  • 170
    • 38949181060 scopus 로고    scopus 로고
    • Rac and P13 kinase mediate endothelial cell-reactive oxygen species generation during normoxic lung ischemia
    • Zhang, Q., Chatterjee, S., Wei, Z. et al. (2008) Rac and P13 kinase mediate endothelial cell-reactive oxygen species generation during normoxic lung ischemia. Antioxidants and Redox Signaling, 10, 679-89.
    • (2008) Antioxidants and Redox Signaling , vol.10 , pp. 679-689
    • Zhang, Q.1    Chatterjee, S.2    Wei, Z.3
  • 171
    • 10244251533 scopus 로고    scopus 로고
    • 2+ flux through voltage-gated channels with flow cessation in pulmonary microvascular endothelial cells
    • 2+ flux through voltage-gated channels with flow cessation in pulmonary microvascular endothelial cells. Microcirculation, 11, 517-26.
    • (2004) Microcirculation , vol.11 , pp. 517-526
    • Wei, Z.1    Manevich, Y.2    Al-Mehdi, A.B.3
  • 173
    • 0031885891 scopus 로고    scopus 로고
    • Increase of reactive oxygen species (ROS) in endothelial cells by shear flow and involvement of ROS in shear-induced c-fos expression
    • Hsieh, H.J., Cheng, C.C., Wu, S.T. et al. (1998) Increase of reactive oxygen species (ROS) in endothelial cells by shear flow and involvement of ROS in shear-induced c-fos expression. Journal of Cellular Physiology, 175, 156-62.
    • (1998) Journal of Cellular Physiology , vol.175 , pp. 156-162
    • Hsieh, H.J.1    Cheng, C.C.2    Wu, S.T.3
  • 174
    • 0023937536 scopus 로고
    • High inflation pressure pulmonary edema. Respective effects of high airway pressure, high tidal volume, and positive end-expiratory pressure
    • Dreyfuss, D., Soler, P., Basset, G., and Saumon, G. (1988) High inflation pressure pulmonary edema. Respective effects of high airway pressure, high tidal volume, and positive end-expiratory pressure. The American Review of Respiratory Disease, 137, 1159-64.
    • (1988) The American Review of Respiratory Disease , vol.137 , pp. 1159-1164
    • Dreyfuss, D.1    Soler, P.2    Basset, G.3    Saumon, G.4
  • 176
    • 22444448911 scopus 로고    scopus 로고
    • Cyclic stretch increases VEGF expression in pulmonary arterial smooth muscle cells via TGF-beta1 and reactive oxygen species: arequire-ment for NAD(P)H oxidase
    • Mata-Greenwood, E., Grobe, A., Kumar, S. et al. (2005) Cyclic stretch increases VEGF expression in pulmonary arterial smooth muscle cells via TGF-beta1 and reactive oxygen species: arequire-ment for NAD(P)H oxidase. American Journal of Physiology: Lung Cellular and Molecular Physiology, 289, L288-89.
    • (2005) American Journal of Physiology: Lung Cellular and Molecular Physiology , vol.289
    • Mata-Greenwood, E.1    Grobe, A.2    Kumar, S.3
  • 177
    • 33846109765 scopus 로고    scopus 로고
    • Hyper-oxia in the intensive care unit: why more is not always better
    • Altemeier, W.A. and Sinclair, S.E. (2007) Hyper-oxia in the intensive care unit: why more is not always better. Current Opinion in Critical Care, 13, 73-78.
    • (2007) Current Opinion in Critical Care , vol.13 , pp. 73-78
    • Altemeier, W.A.1    Sinclair, S.E.2
  • 179
    • 0029555770 scopus 로고
    • A metalloporphyrin superoxide dismu-tase mimetic protects against paraquat-induced endothelial cell injury, in vitro
    • Day, B.J., Shawen, S., Liochev, S.I., and Crapo, J.D. (1995) A metalloporphyrin superoxide dismu-tase mimetic protects against paraquat-induced endothelial cell injury, in vitro. The Journal ofPhar-macology and Experimental Therapeutics, 275, 1227-32.
    • (1995) The Journal ofPhar-macology and Experimental Therapeutics , vol.275 , pp. 1227-1232
    • Day, B.J.1    Shawen, S.2    Liochev, S.I.3    Crapo, J.D.4
  • 180
    • 40949107656 scopus 로고    scopus 로고
    • Structure, function, and mechanism of cytosolic quinone reductases
    • Bianchet, M.A., Erdemli, S.B., and Amzel, L.M. (2008) Structure, function, and mechanism of cytosolic quinone reductases. Vitamins and Hormones, 78, 63-84.
    • (2008) Vitamins and Hormones , vol.78 , pp. 63-84
    • Bianchet, M.A.1    Erdemli, S.B.2    Amzel, L.M.3
  • 181
    • 0034827655 scopus 로고    scopus 로고
    • Bleomycin-induced pneumonitis
    • Sleijfer, S. (2001) Bleomycin-induced pneumonitis. Chest, 120, 617-24.
    • (2001) Chest , vol.120 , pp. 617-624
    • Sleijfer, S.1
  • 182
    • 0024379958 scopus 로고
    • Bleomycin hydrolase: molecular cloning, sequencing, and biochemical studies reveal membership in the cysteine proteinase family
    • Sebti, S.M., Mignano, J.E., Jani, J.P. et al. (1989) Bleomycin hydrolase: molecular cloning, sequencing, and biochemical studies reveal membership in the cysteine proteinase family. Biochemistry, 28, 6544-48.
    • (1989) Biochemistry , vol.28 , pp. 6544-6548
    • Sebti, S.M.1    Mignano, J.E.2    Jani, J.P.3
  • 184
    • 13444257678 scopus 로고    scopus 로고
    • Bleomycins: towards better therapeutics
    • Chen, J. and Stubbe, J. (2005) Bleomycins: towards better therapeutics. Nature Reviews: Cancer, 5, 102-12.
    • (2005) Nature Reviews: Cancer , vol.5 , pp. 102-112
    • Chen, J.1    Stubbe, J.2
  • 185
    • 0020058095 scopus 로고
    • Effect of deoxyribonucleic acid on the production of reduced oxygen by bleomycin and iron
    • Caspary, W.J., Lanzo, D.A., and Niziak, C. (1982) Effect of deoxyribonucleic acid on the production of reduced oxygen by bleomycin and iron. Biochemistry, 21, 334-38.
    • (1982) Biochemistry , vol.21 , pp. 334-338
    • Caspary, W.J.1    Lanzo, D.A.2    Niziak, C.3
  • 187
    • 33644633955 scopus 로고    scopus 로고
    • The anti-cancer drug, doxorubicin, causes oxidant stress-induced endothelial dysfunction
    • Wolf, M.B. and Baynes, J.W. (2006) The anti-cancer drug, doxorubicin, causes oxidant stress-induced endothelial dysfunction. Biochimica et Biophysica Acta, 1760, 267-71.
    • (2006) Biochimica et Biophysica Acta , vol.1760 , pp. 267-271
    • Wolf, M.B.1    Baynes, J.W.2
  • 188
    • 0034660629 scopus 로고    scopus 로고
    • Neutrophil-induced changes in the biomechanical properties of endothelial cells: roles of ICAM-1 and reactive oxygen species
    • Wang, Q. and Doerschuk, C.M. (2000) Neutrophil-induced changes in the biomechanical properties of endothelial cells: roles of ICAM-1 and reactive oxygen species. Journal of Immunology, 164, 6487-94.
    • (2000) Journal of Immunology , vol.164 , pp. 6487-6494
    • Wang, Q.1    Doerschuk, C.M.2
  • 189
    • 0035109840 scopus 로고    scopus 로고
    • Oxidants and antioxidant therapy
    • Rotstein, O.D. (2001) Oxidants and antioxidant therapy. Critical Care Clinics, 17, 239-47.
    • (2001) Critical Care Clinics , vol.17 , pp. 239-247
    • Rotstein, O.D.1
  • 190
    • 0037418938 scopus 로고    scopus 로고
    • Increased superoxide generation is associated with pulmonary hypertension in fetal lambs: a role for NADPH oxidase
    • Brennan, L.A., Steinhorn, R.H., Wedgwood, S. et al. (2003) Increased superoxide generation is associated with pulmonary hypertension in fetal lambs: a role for NADPH oxidase. Circulation Research, 92, 683-91.
    • (2003) Circulation Research , vol.92 , pp. 683-691
    • Brennan, L.A.1    Steinhorn, R.H.2    Wedgwood, S.3
  • 191
    • 25444442602 scopus 로고    scopus 로고
    • Increased hydrogen peroxide down-regulates soluble guanylate cyclase in the lungs of lambs with persistent pulmonary hypertension of the newborn
    • Wedgwood, S., Steinhorn, R.H., Bunderson, M. et al. (2005) Increased hydrogen peroxide down-regulates soluble guanylate cyclase in the lungs of lambs with persistent pulmonary hypertension of the newborn. American Journal of Physiology: Lung Cellular and Molecular Physiology, 289, L660-66.
    • (2005) American Journal of Physiology: Lung Cellular and Molecular Physiology , vol.289
    • Wedgwood, S.1    Steinhorn, R.H.2    Bunderson, M.3
  • 192
    • 43049099358 scopus 로고    scopus 로고
    • Prevalence and risk of hypertension in renal disease-data from the Czech Registry of Renal Biopsies
    • Jancova, E., Vankova, Z., Honsova, E. et al. (2008) Prevalence and risk of hypertension in renal disease-data from the Czech Registry of Renal Biopsies. Kidney and Blood Pressure Research, 31, 135-42.
    • (2008) Kidney and Blood Pressure Research , vol.31 , pp. 135-142
    • Jancova, E.1    Vankova, Z.2    Honsova, E.3
  • 193
    • 0035869592 scopus 로고    scopus 로고
    • Reactive oxygen species and substance P in monocrotaline-induced pulmonary hypertension
    • Chen, M.J., Chiang, L.Y., and Lai, Y.L. (2001) Reactive oxygen species and substance P in monocrotaline-induced pulmonary hypertension. Toxicology and Applied Pharmacology, 171, 165-73.
    • (2001) Toxicology and Applied Pharmacology , vol.171 , pp. 165-173
    • Chen, M.J.1    Chiang, L.Y.2    Lai, Y.L.3
  • 194
    • 0035100461 scopus 로고    scopus 로고
    • Generation of oxidative stress contributes to the development of pulmonary hypertension induced by hypoxia
    • Hoshikawa, Y., Ono, S., Suzuki, S. et al. (2001) Generation of oxidative stress contributes to the development of pulmonary hypertension induced by hypoxia. Journal of Applied Physiology, 90, 1299-306.
    • (2001) Journal of Applied Physiology , vol.90 , pp. 1299-1306
    • Hoshikawa, Y.1    Ono, S.2    Suzuki, S.3
  • 197
    • 0028838749 scopus 로고
    • Free radical-mediated vascular injury in lungs preserved at moderate hypothermia
    • Haniuda, M., Dresler, C.M., Mizuta, T. et al. (1995) Free radical-mediated vascular injury in lungs preserved at moderate hypothermia. Annals of Thoracic and Cardiovascular Surgery, 60, 1376-81.
    • (1995) Annals of Thoracic and Cardiovascular Surgery , vol.60 , pp. 1376-1381
    • Haniuda, M.1    Dresler, C.M.2    Mizuta, T.3
  • 198
    • 0037974800 scopus 로고    scopus 로고
    • Low potassium dextran lung preservation solution reduces reactive oxygen species production
    • Kelly, R.F., Murar, J., Hong, Z. et al. (2003) Low potassium dextran lung preservation solution reduces reactive oxygen species production. Annals of Thoracic and Cardiovascular Surgery, 75, 1705-10.
    • (2003) Annals of Thoracic and Cardiovascular Surgery , vol.75 , pp. 1705-1710
    • Kelly, R.F.1    Murar, J.2    Hong, Z.3


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