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Volumn 23, Issue 7, 2012, Pages 745-757

Redox balance dynamically regulates vascular growth and remodeling

Author keywords

Angiogenesis; Antioxidant; Hydrogen peroxide; Nitric oxide; Superoxide

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; ENDOTHELIAL NITRIC OXIDE SYNTHASE; GLUTATHIONE; INDUCIBLE NITRIC OXIDE SYNTHASE; MANGANESE SUPEROXIDE DISMUTASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; N(G) NITROARGININE METHYL ESTER; NEURONAL NITRIC OXIDE SYNTHASE; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; PEROXIREDOXIN; PHOSPHATASE; PHOSPHOLIPASE C; PROTEIN KINASE C; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 4; THIOREDOXIN; TRANSCRIPTION FACTOR; UNINDEXED DRUG; VASCULOTROPIN; VASCULOTROPIN RECEPTOR 1; VASCULOTROPIN RECEPTOR 2; XANTHINE DEHYDROGENASE; XANTHINE OXIDASE;

EID: 84866634415     PISSN: 10849521     EISSN: 10963634     Source Type: Journal    
DOI: 10.1016/j.semcdb.2012.05.003     Document Type: Review
Times cited : (58)

References (189)
  • 1
    • 33644683263 scopus 로고    scopus 로고
    • Endothelial extracellular matrix: biosynthesis, remodeling, and functions during vascular morphogenesis and neovessel stabilization
    • Davis G.E., Senger D.R. Endothelial extracellular matrix: biosynthesis, remodeling, and functions during vascular morphogenesis and neovessel stabilization. Circulation Research 2005, 97:1093-1107.
    • (2005) Circulation Research , vol.97 , pp. 1093-1107
    • Davis, G.E.1    Senger, D.R.2
  • 2
    • 0028929803 scopus 로고
    • Angiogenesis in cancer, vascular, rheumatoid and other disease
    • Folkman J. Angiogenesis in cancer, vascular, rheumatoid and other disease. Nature Medicine 1995, 1:27-31.
    • (1995) Nature Medicine , vol.1 , pp. 27-31
    • Folkman, J.1
  • 4
    • 34249071326 scopus 로고    scopus 로고
    • VEGF signaling through NADPH oxidase-derived ROS
    • Ushio-Fukai M. VEGF signaling through NADPH oxidase-derived ROS. Antioxidants & Redox Signaling 2007, 9:731-739.
    • (2007) Antioxidants & Redox Signaling , vol.9 , pp. 731-739
    • Ushio-Fukai, M.1
  • 6
    • 8544270180 scopus 로고    scopus 로고
    • Direct interaction of the novel Nox proteins with p22phox is required for the formation of a functionally active NADPH oxidase
    • Ambasta R.K., Kumar P., Griendling K.K., Schmidt H.H., Busse R., Brandes R.P. Direct interaction of the novel Nox proteins with p22phox is required for the formation of a functionally active NADPH oxidase. The Journal of Biological Chemistry 2004, 279:45935-45941.
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 45935-45941
    • Ambasta, R.K.1    Kumar, P.2    Griendling, K.K.3    Schmidt, H.H.4    Busse, R.5    Brandes, R.P.6
  • 7
    • 0025114585 scopus 로고
    • Human neutrophil cytochrome b light chain (p22-phox). Gene structure, chromosomal location, and mutations in cytochrome-negative autosomal recessive chronic granulomatous disease
    • Dinauer M.C., Pierce E.A., Bruns G.A., Curnutte J.T., Orkin S.H. Human neutrophil cytochrome b light chain (p22-phox). Gene structure, chromosomal location, and mutations in cytochrome-negative autosomal recessive chronic granulomatous disease. Journal of Clinical Investigation 1990, 86:1729-1737.
    • (1990) Journal of Clinical Investigation , vol.86 , pp. 1729-1737
    • Dinauer, M.C.1    Pierce, E.A.2    Bruns, G.A.3    Curnutte, J.T.4    Orkin, S.H.5
  • 8
    • 0033609785 scopus 로고    scopus 로고
    • Tetratricopeptide repeat (TPR) motifs of p67(phox) participate in interaction with the small GTPase Rac and activation of the phagocyte NADPH oxidase
    • Koga H., Terasawa H., Nunoi H., Takeshige K., Inagaki F., Sumimoto H. Tetratricopeptide repeat (TPR) motifs of p67(phox) participate in interaction with the small GTPase Rac and activation of the phagocyte NADPH oxidase. The Journal of Biological Chemistry 1999, 274:25051-25060.
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 25051-25060
    • Koga, H.1    Terasawa, H.2    Nunoi, H.3    Takeshige, K.4    Inagaki, F.5    Sumimoto, H.6
  • 9
    • 79151477025 scopus 로고    scopus 로고
    • Direct interaction between Tks proteins and the N-terminal proline-rich region (PRR) of NoxA1 mediates Nox1-dependent ROS generation
    • Gianni D., DerMardirossian C., Bokoch G.M. Direct interaction between Tks proteins and the N-terminal proline-rich region (PRR) of NoxA1 mediates Nox1-dependent ROS generation. European Journal of Cell Biology 2011, 90:164-171.
    • (2011) European Journal of Cell Biology , vol.90 , pp. 164-171
    • Gianni, D.1    DerMardirossian, C.2    Bokoch, G.M.3
  • 12
    • 9144255403 scopus 로고    scopus 로고
    • Nox4 as the major catalytic component of an endothelial NAD(P)H oxidase
    • Ago T., Kitazono T., Ooboshi H., Iyama T., Han Y.H., Takada J., et al. Nox4 as the major catalytic component of an endothelial NAD(P)H oxidase. Circulation 2004, 109:227-233.
    • (2004) Circulation , vol.109 , pp. 227-233
    • Ago, T.1    Kitazono, T.2    Ooboshi, H.3    Iyama, T.4    Han, Y.H.5    Takada, J.6
  • 14
    • 83455185433 scopus 로고    scopus 로고
    • Reactive oxygen species and endothelial function-role of nitric oxide synthase uncoupling and Nox family nicotinamide adenine dinucleotide phosphate oxidases
    • Montezano A.C., Touyz R.M. Reactive oxygen species and endothelial function-role of nitric oxide synthase uncoupling and Nox family nicotinamide adenine dinucleotide phosphate oxidases. Basic & Clinical Pharmacology & Toxicology 2012, 110:87-94.
    • (2012) Basic & Clinical Pharmacology & Toxicology , vol.110 , pp. 87-94
    • Montezano, A.C.1    Touyz, R.M.2
  • 15
    • 18144447696 scopus 로고    scopus 로고
    • Protein kinase C-dependent increase in reactive oxygen species (ROS) production in vascular tissues of diabetes: role of vascular NAD(P)H oxidase
    • Inoguchi T., Sonta T., Tsubouchi H., Etoh T., Kakimoto M., Sonoda N., et al. Protein kinase C-dependent increase in reactive oxygen species (ROS) production in vascular tissues of diabetes: role of vascular NAD(P)H oxidase. Journal of the American Society of Nephrology 2003, 14:S227-S232.
    • (2003) Journal of the American Society of Nephrology , vol.14
    • Inoguchi, T.1    Sonta, T.2    Tsubouchi, H.3    Etoh, T.4    Kakimoto, M.5    Sonoda, N.6
  • 18
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology
    • Bedard K., Krause K.H. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiological Reviews 2007, 87:245-313.
    • (2007) Physiological Reviews , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 19
    • 64749111284 scopus 로고    scopus 로고
    • Protein disulfide isomerase overexpression in vascular smooth muscle cells induces spontaneous preemptive NADPH oxidase activation and Nox1 mRNA expression: effects of nitrosothiol exposure
    • Fernandes D.C., Manoel A.H., Wosniak J., Laurindo F.R. Protein disulfide isomerase overexpression in vascular smooth muscle cells induces spontaneous preemptive NADPH oxidase activation and Nox1 mRNA expression: effects of nitrosothiol exposure. Archives of Biochemistry and Biophysics 2009, 484:197-204.
    • (2009) Archives of Biochemistry and Biophysics , vol.484 , pp. 197-204
    • Fernandes, D.C.1    Manoel, A.H.2    Wosniak, J.3    Laurindo, F.R.4
  • 20
    • 0037205457 scopus 로고    scopus 로고
    • Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells
    • Li J.M., Shah A.M. Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells. The Journal of Biological Chemistry 2002, 277:19952-19960.
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 19952-19960
    • Li, J.M.1    Shah, A.M.2
  • 22
    • 36348938884 scopus 로고    scopus 로고
    • Reactive oxygen species regulate angiogenesis and tumor growth through vascular endothelial growth factor
    • Xia C., Meng Q., Liu L.Z., Rojanasakul Y., Wang X.R., Jiang B.H. Reactive oxygen species regulate angiogenesis and tumor growth through vascular endothelial growth factor. Cancer Research 2007, 67:10823-10830.
    • (2007) Cancer Research , vol.67 , pp. 10823-10830
    • Xia, C.1    Meng, Q.2    Liu, L.Z.3    Rojanasakul, Y.4    Wang, X.R.5    Jiang, B.H.6
  • 23
    • 33745728157 scopus 로고    scopus 로고
    • Hydrogen peroxide produced by angiopoietin-1 mediates angiogenesis
    • Kim Y.M., Kim K.E., Koh G.Y., Ho Y.S., Lee K.J. Hydrogen peroxide produced by angiopoietin-1 mediates angiogenesis. Cancer Research 2006, 66:6167-6174.
    • (2006) Cancer Research , vol.66 , pp. 6167-6174
    • Kim, Y.M.1    Kim, K.E.2    Koh, G.Y.3    Ho, Y.S.4    Lee, K.J.5
  • 27
    • 0028288342 scopus 로고
    • Inducible nitric oxide synthase in vascular smooth muscle
    • Schini V.B., Busse R., Vanhoutte P.M. Inducible nitric oxide synthase in vascular smooth muscle. Arzneimittel-Forschung 1994, 44:432-435.
    • (1994) Arzneimittel-Forschung , vol.44 , pp. 432-435
    • Schini, V.B.1    Busse, R.2    Vanhoutte, P.M.3
  • 28
    • 0028100605 scopus 로고
    • Indirect angiogenic cytokines upregulate VEGF and bFGF gene expression in vascular smooth muscle cells, whereas hypoxia upregulates VEGF expression only
    • Brogi E., Wu T., Namiki A., Isner J.M. Indirect angiogenic cytokines upregulate VEGF and bFGF gene expression in vascular smooth muscle cells, whereas hypoxia upregulates VEGF expression only. Circulation 1994, 90:649-652.
    • (1994) Circulation , vol.90 , pp. 649-652
    • Brogi, E.1    Wu, T.2    Namiki, A.3    Isner, J.M.4
  • 30
    • 0032948123 scopus 로고    scopus 로고
    • Vascular endothelial growth factor and basic fibroblast growth factor induce expression of CXCR4 on human endothelial cells: In vivo neovascularization induced by stromal-derived factor-1alpha
    • Salcedo R., Wasserman K., Young H.A., Grimm M.C., Howard O.M., Anver M.R., et al. Vascular endothelial growth factor and basic fibroblast growth factor induce expression of CXCR4 on human endothelial cells: In vivo neovascularization induced by stromal-derived factor-1alpha. The American Journal of Pathology 1999, 154:1125-1135.
    • (1999) The American Journal of Pathology , vol.154 , pp. 1125-1135
    • Salcedo, R.1    Wasserman, K.2    Young, H.A.3    Grimm, M.C.4    Howard, O.M.5    Anver, M.R.6
  • 34
    • 77954217626 scopus 로고    scopus 로고
    • Endothelial nitric oxide synthase deficiency causes collateral vessel rarefaction and impairs activation of a cell cycle gene network during arteriogenesis
    • Dai X., Faber J.E. Endothelial nitric oxide synthase deficiency causes collateral vessel rarefaction and impairs activation of a cell cycle gene network during arteriogenesis. Circulation Research 2010, 106:1870-1881.
    • (2010) Circulation Research , vol.106 , pp. 1870-1881
    • Dai, X.1    Faber, J.E.2
  • 36
    • 0035814951 scopus 로고    scopus 로고
    • Endothelial regulation of vasomotion in apoE-deficient mice: implications for interactions between peroxynitrite and tetrahydrobiopterin
    • Laursen J.B., Somers M., Kurz S., McCann L., Warnholtz A., Freeman B.A., et al. Endothelial regulation of vasomotion in apoE-deficient mice: implications for interactions between peroxynitrite and tetrahydrobiopterin. Circulation 2001, 103:1282-1288.
    • (2001) Circulation , vol.103 , pp. 1282-1288
    • Laursen, J.B.1    Somers, M.2    Kurz, S.3    McCann, L.4    Warnholtz, A.5    Freeman, B.A.6
  • 37
    • 0037399439 scopus 로고    scopus 로고
    • Oxidation of tetrahydrobiopterin leads to uncoupling of endothelial cell nitric oxide synthase in hypertension
    • Landmesser U., Dikalov S., Price S.R., McCann L., Fukai T., Holland S.M., et al. Oxidation of tetrahydrobiopterin leads to uncoupling of endothelial cell nitric oxide synthase in hypertension. Journal of Clinical Investigation 2003, 111:1201-1209.
    • (2003) Journal of Clinical Investigation , vol.111 , pp. 1201-1209
    • Landmesser, U.1    Dikalov, S.2    Price, S.R.3    McCann, L.4    Fukai, T.5    Holland, S.M.6
  • 38
    • 0037105296 scopus 로고    scopus 로고
    • Structure and function of xanthine oxidoreductase: where are we now?
    • Harrison R. Structure and function of xanthine oxidoreductase: where are we now?. Free Radical Biology & Medicine 2002, 33:774-797.
    • (2002) Free Radical Biology & Medicine , vol.33 , pp. 774-797
    • Harrison, R.1
  • 39
    • 0028678762 scopus 로고
    • Xanthine oxidoreductase. Biochemical, biological and pathogenic functions
    • Stipek S., Novak L., Crkovska J., Zima T., Platenik J. Xanthine oxidoreductase. Biochemical, biological and pathogenic functions. Sbornik Lekarsky 1994, 95:289-295.
    • (1994) Sbornik Lekarsky , vol.95 , pp. 289-295
    • Stipek, S.1    Novak, L.2    Crkovska, J.3    Zima, T.4    Platenik, J.5
  • 40
    • 0037954564 scopus 로고    scopus 로고
    • Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology
    • Garattini E., Mendel R., Romao M.J., Wright R., Terao M. Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology. Biochemical Journal 2003, 372:15-32.
    • (2003) Biochemical Journal , vol.372 , pp. 15-32
    • Garattini, E.1    Mendel, R.2    Romao, M.J.3    Wright, R.4    Terao, M.5
  • 41
    • 46449131251 scopus 로고    scopus 로고
    • Xanthine oxidase interaction with vascular endothelial growth factor in human endothelial cell angiogenesis
    • Kou B., Ni J., Vatish M., Singer D.R. Xanthine oxidase interaction with vascular endothelial growth factor in human endothelial cell angiogenesis. Microcirculation 2008, 15:251-267.
    • (2008) Microcirculation , vol.15 , pp. 251-267
    • Kou, B.1    Ni, J.2    Vatish, M.3    Singer, D.R.4
  • 43
    • 0034625073 scopus 로고    scopus 로고
    • Investigation into the sources of superoxide in human blood vessels: angiotensin II increases superoxide production in human internal mammary arteries
    • Berry C., Hamilton C.A., Brosnan M.J., Magill F.G., Berg G.A., McMurray J.J., et al. Investigation into the sources of superoxide in human blood vessels: angiotensin II increases superoxide production in human internal mammary arteries. Circulation 2000, 101:2206-2212.
    • (2000) Circulation , vol.101 , pp. 2206-2212
    • Berry, C.1    Hamilton, C.A.2    Brosnan, M.J.3    Magill, F.G.4    Berg, G.A.5    McMurray, J.J.6
  • 45
    • 0036954803 scopus 로고    scopus 로고
    • Novel role of gp91(phox)-containing NAD(P)H oxidase in vascular endothelial growth factor-induced signaling and angiogenesis
    • Ushio-Fukai M., Tang Y., Fukai T., Dikalov S.I., Ma Y., Fujimoto M., et al. Novel role of gp91(phox)-containing NAD(P)H oxidase in vascular endothelial growth factor-induced signaling and angiogenesis. Circulation Research 2002, 91:1160-1167.
    • (2002) Circulation Research , vol.91 , pp. 1160-1167
    • Ushio-Fukai, M.1    Tang, Y.2    Fukai, T.3    Dikalov, S.I.4    Ma, Y.5    Fujimoto, M.6
  • 47
    • 0142055950 scopus 로고    scopus 로고
    • Oxidative stress and cardiovascular injury: part I: basic mechanisms and in vivo monitoring of ROS
    • Griendling K.K., FitzGerald G.A. Oxidative stress and cardiovascular injury: part I: basic mechanisms and in vivo monitoring of ROS. Circulation 2003, 108:1912-1916.
    • (2003) Circulation , vol.108 , pp. 1912-1916
    • Griendling, K.K.1    FitzGerald, G.A.2
  • 48
    • 70349314327 scopus 로고    scopus 로고
    • Angiogenic properties of sustained release platelet-rich plasma: characterization in vitro and in the ischemic hind limb of the mouse
    • e872
    • Bir S.C., Esaki J., Marui A., Yamahara K., Tsubota H., Ikeda T., et al. Angiogenic properties of sustained release platelet-rich plasma: characterization in vitro and in the ischemic hind limb of the mouse. Journal of Vascular Surgery 2009, 50:870-879. e872.
    • (2009) Journal of Vascular Surgery , vol.50 , pp. 870-879
    • Bir, S.C.1    Esaki, J.2    Marui, A.3    Yamahara, K.4    Tsubota, H.5    Ikeda, T.6
  • 49
    • 0038363443 scopus 로고    scopus 로고
    • Angiogenic synergism, vascular stability and improvement of hind-limb ischemia by a combination of PDGF-BB and FGF-2
    • Cao R., Brakenhielm E., Pawliuk R., Wariaro D., Post M.J., Wahlberg E., et al. Angiogenic synergism, vascular stability and improvement of hind-limb ischemia by a combination of PDGF-BB and FGF-2. Nature Medicine 2003, 9:604-613.
    • (2003) Nature Medicine , vol.9 , pp. 604-613
    • Cao, R.1    Brakenhielm, E.2    Pawliuk, R.3    Wariaro, D.4    Post, M.J.5    Wahlberg, E.6
  • 50
    • 80052015813 scopus 로고    scopus 로고
    • Molecular control of endothelial cell behaviour during blood vessel morphogenesis
    • Herbert S.P., Stainier D.Y. Molecular control of endothelial cell behaviour during blood vessel morphogenesis. Nature Reviews Molecular Cell Biology 2011, 12:551-564.
    • (2011) Nature Reviews Molecular Cell Biology , vol.12 , pp. 551-564
    • Herbert, S.P.1    Stainier, D.Y.2
  • 51
    • 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., Bartosz G. Low concentration of oxidant and nitric oxide donors stimulate proliferation of human endothelial cells in vitro. Cell Biology International 2004, 28:483-486.
    • (2004) Cell Biology International , vol.28 , pp. 483-486
    • Luczak, K.1    Balcerczyk, A.2    Soszynski, M.3    Bartosz, G.4
  • 53
    • 0036910386 scopus 로고    scopus 로고
    • The role of hydrogen peroxide in endothelial proliferative responses
    • Stone J.R., Collins T. The role of hydrogen peroxide in endothelial proliferative responses. Endothelium 2002, 9:231-238.
    • (2002) Endothelium , vol.9 , pp. 231-238
    • Stone, J.R.1    Collins, T.2
  • 55
    • 0032545526 scopus 로고    scopus 로고
    • Stimulation of in vitro angiogenesis by hydrogen peroxide and the relation with ETS-1 in endothelial cells
    • Yasuda M., Ohzeki Y., Shimizu S., Naito S., Ohtsuru A., Yamamoto T., et al. Stimulation of in vitro angiogenesis by hydrogen peroxide and the relation with ETS-1 in endothelial cells. Life Sciences 1999, 64:249-258.
    • (1999) Life Sciences , vol.64 , pp. 249-258
    • Yasuda, M.1    Ohzeki, Y.2    Shimizu, S.3    Naito, S.4    Ohtsuru, A.5    Yamamoto, T.6
  • 56
    • 33745217132 scopus 로고    scopus 로고
    • Redox signaling in angiogenesis: role of NADPH oxidase
    • Ushio-Fukai M. Redox signaling in angiogenesis: role of NADPH oxidase. Cardiovascular Research 2006, 71:226-235.
    • (2006) Cardiovascular Research , vol.71 , pp. 226-235
    • Ushio-Fukai, M.1
  • 57
    • 44449125132 scopus 로고    scopus 로고
    • Reactive oxygen species and angiogenesis: NADPH oxidase as target for cancer therapy
    • Ushio-Fukai M., Nakamura Y. Reactive oxygen species and angiogenesis: NADPH oxidase as target for cancer therapy. Cancer Letters 2008, 266:37-52.
    • (2008) Cancer Letters , vol.266 , pp. 37-52
    • Ushio-Fukai, M.1    Nakamura, Y.2
  • 59
    • 0034177682 scopus 로고    scopus 로고
    • Endogenous oxygen radicals modulate protein tyrosine phosphorylation and JNK-1 activation in lectin-stimulated thymocytes
    • Pani G., Colavitti R., Borrello S., Galeotti T. Endogenous oxygen radicals modulate protein tyrosine phosphorylation and JNK-1 activation in lectin-stimulated thymocytes. Biochemical Journal 2000, 347(Pt 1):173-181.
    • (2000) Biochemical Journal , vol.347 , Issue.PART. 1 , pp. 173-181
    • Pani, G.1    Colavitti, R.2    Borrello, S.3    Galeotti, T.4
  • 60
    • 18244408857 scopus 로고    scopus 로고
    • Involvement of VEGFR-2 (kdr/flk-1) but not VEGFR-1 (flt-1) in VEGF-A and VEGF-C-induced tube formation by human microvascular endothelial cells in fibrin matrices in vitro
    • Koolwijk P., Peters E., van der Vecht B., Hornig C., Weich H.A., Alitalo K., et al. Involvement of VEGFR-2 (kdr/flk-1) but not VEGFR-1 (flt-1) in VEGF-A and VEGF-C-induced tube formation by human microvascular endothelial cells in fibrin matrices in vitro. Angiogenesis 2001, 4:53-60.
    • (2001) Angiogenesis , vol.4 , pp. 53-60
    • Koolwijk, P.1    Peters, E.2    van der Vecht, B.3    Hornig, C.4    Weich, H.A.5    Alitalo, K.6
  • 61
    • 0029071065 scopus 로고
    • Activation of mitogen-activated protein kinases by vascular endothelial growth factor and basic fibroblast growth factor in capillary endothelial cells is inhibited by the antiangiogenic factor 16-kDa N-terminal fragment of prolactin
    • D'Angelo G., Struman I., Martial J., Weiner R.I. Activation of mitogen-activated protein kinases by vascular endothelial growth factor and basic fibroblast growth factor in capillary endothelial cells is inhibited by the antiangiogenic factor 16-kDa N-terminal fragment of prolactin. Proceedings of the National Academy of Sciences of the United States of America 1995, 92:6374-6378.
    • (1995) Proceedings of the National Academy of Sciences of the United States of America , vol.92 , pp. 6374-6378
    • D'Angelo, G.1    Struman, I.2    Martial, J.3    Weiner, R.I.4
  • 62
    • 0028899424 scopus 로고
    • Vascular endothelial cell growth factor promotes tyrosine phosphorylation of mediators of signal transduction that contain SH2 domains Association with endothelial cell proliferation
    • Guo D., Jia Q., Song H.Y., Warren R.S., Donner D.B. Vascular endothelial cell growth factor promotes tyrosine phosphorylation of mediators of signal transduction that contain SH2 domains Association with endothelial cell proliferation. The Journal of Biological Chemistry 1995, 270:6729-6733.
    • (1995) The Journal of Biological Chemistry , vol.270 , pp. 6729-6733
    • Guo, D.1    Jia, Q.2    Song, H.Y.3    Warren, R.S.4    Donner, D.B.5
  • 63
    • 0031466232 scopus 로고    scopus 로고
    • The vascular endothelial growth factor receptor KDR activates multiple signal transduction pathways in porcine aortic endothelial cells
    • Kroll J., Waltenberger J. The vascular endothelial growth factor receptor KDR activates multiple signal transduction pathways in porcine aortic endothelial cells. The Journal of Biological Chemistry 1997, 272:32521-32527.
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 32521-32527
    • Kroll, J.1    Waltenberger, J.2
  • 64
    • 2642709170 scopus 로고    scopus 로고
    • Characterization of vascular endothelial growth factor's effect on the activation of protein kinase C, its isoforms, and endothelial cell growth
    • Xia P., Aiello L.P., Ishii H., Jiang Z.Y., Park D.J., Robinson G.S., et al. Characterization of vascular endothelial growth factor's effect on the activation of protein kinase C, its isoforms, and endothelial cell growth. Journal of Clinical Investigation 1996, 98:2018-2026.
    • (1996) Journal of Clinical Investigation , vol.98 , pp. 2018-2026
    • Xia, P.1    Aiello, L.P.2    Ishii, H.3    Jiang, Z.Y.4    Park, D.J.5    Robinson, G.S.6
  • 66
    • 5544237716 scopus 로고    scopus 로고
    • Reactive oxygen species as mediators of angiogenesis signaling: role of NAD(P)H oxidase
    • Ushio-Fukai M., Alexander R.W. Reactive oxygen species as mediators of angiogenesis signaling: role of NAD(P)H oxidase. Molecular and Cellular Biochemistry 2004, 264:85-97.
    • (2004) Molecular and Cellular Biochemistry , vol.264 , pp. 85-97
    • Ushio-Fukai, M.1    Alexander, R.W.2
  • 69
    • 80051790391 scopus 로고    scopus 로고
    • NADPH oxidase 4 promotes endothelial angiogenesis through endothelial nitric oxide synthase activation
    • Craige S.M., Chen K., Pei Y., Li C., Huang X., Chen C., et al. NADPH oxidase 4 promotes endothelial angiogenesis through endothelial nitric oxide synthase activation. Circulation 2011, 124:731-740.
    • (2011) Circulation , vol.124 , pp. 731-740
    • Craige, S.M.1    Chen, K.2    Pei, Y.3    Li, C.4    Huang, X.5    Chen, C.6
  • 70
    • 0036479214 scopus 로고    scopus 로고
    • Reactive oxygen species as downstream mediators of angiogenic signaling by vascular endothelial growth factor receptor-2/KDR
    • Colavitti R., Pani G., Bedogni B., Anzevino R., Borrello S., Waltenberger J., et al. Reactive oxygen species as downstream mediators of angiogenic signaling by vascular endothelial growth factor receptor-2/KDR. The Journal of Biological Chemistry 2002, 277:3101-3108.
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 3101-3108
    • Colavitti, R.1    Pani, G.2    Bedogni, B.3    Anzevino, R.4    Borrello, S.5    Waltenberger, J.6
  • 71
    • 77953542905 scopus 로고    scopus 로고
    • NADPH oxidase 4 mediates reactive oxygen species induction of CD146 dimerization in VEGF signal transduction
    • Zhuang J., Jiang T., Lu D., Luo Y., Zheng C., Feng J., et al. NADPH oxidase 4 mediates reactive oxygen species induction of CD146 dimerization in VEGF signal transduction. Free Radical Biology & Medicine 2010, 49:227-236.
    • (2010) Free Radical Biology & Medicine , vol.49 , pp. 227-236
    • Zhuang, J.1    Jiang, T.2    Lu, D.3    Luo, Y.4    Zheng, C.5    Feng, J.6
  • 73
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • Meng T.C., Fukada T., Tonks N.K. Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Molecular Cell 2002, 9:387-399.
    • (2002) Molecular Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 75
    • 77956634584 scopus 로고    scopus 로고
    • Targeting the reversibly oxidized protein tyrosine phosphatase superfamily
    • Boivin B., Yang M., Tonks N.K. Targeting the reversibly oxidized protein tyrosine phosphatase superfamily. Science Signaling 2010, 3:pl2.
    • (2010) Science Signaling , vol.3
    • Boivin, B.1    Yang, M.2    Tonks, N.K.3
  • 76
    • 17644371347 scopus 로고    scopus 로고
    • Functions and mechanisms of redox regulation of cysteine-based phosphatases
    • Salmeen A., Barford D. Functions and mechanisms of redox regulation of cysteine-based phosphatases. Antioxidants & Redox Signaling 2005, 7:560-577.
    • (2005) Antioxidants & Redox Signaling , vol.7 , pp. 560-577
    • Salmeen, A.1    Barford, D.2
  • 77
    • 58049200135 scopus 로고    scopus 로고
    • Cysteine S-nitrosylation protects protein-tyrosine phosphatase 1B against oxidation-induced permanent inactivation
    • Chen Y.Y., Chu H.M., Pan K.T., Teng C.H., Wang D.L., Wang A.H., et al. Cysteine S-nitrosylation protects protein-tyrosine phosphatase 1B against oxidation-induced permanent inactivation. The Journal of Biological Chemistry 2008, 283:35265-35272.
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 35265-35272
    • Chen, Y.Y.1    Chu, H.M.2    Pan, K.T.3    Teng, C.H.4    Wang, D.L.5    Wang, A.H.6
  • 78
    • 0033794917 scopus 로고    scopus 로고
    • Roles of the SHP-1 tyrosine phosphatase in the negative regulation of cell signalling
    • Zhang J., Somani A.K., Siminovitch K.A. Roles of the SHP-1 tyrosine phosphatase in the negative regulation of cell signalling. Seminars in Immunology 2000, 12:361-378.
    • (2000) Seminars in Immunology , vol.12 , pp. 361-378
    • Zhang, J.1    Somani, A.K.2    Siminovitch, K.A.3
  • 79
    • 0037434930 scopus 로고    scopus 로고
    • The function of the protein tyrosine phosphatase SHP-1 in cancer
    • Wu C., Sun M., Liu L., Zhou G.W. The function of the protein tyrosine phosphatase SHP-1 in cancer. Gene 2003, 306:1-12.
    • (2003) Gene , vol.306 , pp. 1-12
    • Wu, C.1    Sun, M.2    Liu, L.3    Zhou, G.W.4
  • 80
    • 15744393966 scopus 로고    scopus 로고
    • Comparison of the signaling mechanisms by which VEGF, H2O2, and phosphatase inhibitors activate endothelial cell ERK1/2 MAP-kinase
    • Tao Q., Spring S.C., Terman B.I. Comparison of the signaling mechanisms by which VEGF, H2O2, and phosphatase inhibitors activate endothelial cell ERK1/2 MAP-kinase. Microvascular Research 2005, 69:36-44.
    • (2005) Microvascular Research , vol.69 , pp. 36-44
    • Tao, Q.1    Spring, S.C.2    Terman, B.I.3
  • 81
    • 49849084827 scopus 로고    scopus 로고
    • Redox control of endothelial function and dysfunction: molecular mechanisms and therapeutic opportunities
    • Thomas S.R., Witting P.K., Drummond G.R. Redox control of endothelial function and dysfunction: molecular mechanisms and therapeutic opportunities. Antioxidants & Redox Signaling 2008, 10:1713-1765.
    • (2008) Antioxidants & Redox Signaling , vol.10 , pp. 1713-1765
    • Thomas, S.R.1    Witting, P.K.2    Drummond, G.R.3
  • 82
    • 0029174009 scopus 로고
    • Modifications of cysteine-rich regions in protein kinase C induced by oxidant tumor promoters and enzyme-specific inhibitors
    • Gopalakrishna R., Chen Z.H., Gundimeda U. Modifications of cysteine-rich regions in protein kinase C induced by oxidant tumor promoters and enzyme-specific inhibitors. Methods in Enzymology 1995, 252:132-146.
    • (1995) Methods in Enzymology , vol.252 , pp. 132-146
    • Gopalakrishna, R.1    Chen, Z.H.2    Gundimeda, U.3
  • 84
    • 0031825098 scopus 로고    scopus 로고
    • Role of protein kinase C in basal and hydrogen peroxide-stimulated NF-kappa B activation in the murine macrophage J774A.1 cell line
    • Kaul N., Gopalakrishna R., Gundimeda U., Choi J., Forman H.J. Role of protein kinase C in basal and hydrogen peroxide-stimulated NF-kappa B activation in the murine macrophage J774A.1 cell line. Archives of Biochemistry and Biophysics 1998, 350:79-86.
    • (1998) Archives of Biochemistry and Biophysics , vol.350 , pp. 79-86
    • Kaul, N.1    Gopalakrishna, R.2    Gundimeda, U.3    Choi, J.4    Forman, H.J.5
  • 86
    • 0027231627 scopus 로고
    • Hydroperoxide-induced diacylglycerol formation and protein kinase C activation in vascular endothelial cells
    • Taher M.M., Garcia J.G., Natarajan V. Hydroperoxide-induced diacylglycerol formation and protein kinase C activation in vascular endothelial cells. Archives of Biochemistry and Biophysics 1993, 303:260-266.
    • (1993) Archives of Biochemistry and Biophysics , vol.303 , pp. 260-266
    • Taher, M.M.1    Garcia, J.G.2    Natarajan, V.3
  • 87
    • 0026639327 scopus 로고
    • Activation of protein kinase C pathway contributes to hydrogen peroxide-induced increase in endothelial permeability
    • Siflinger-Birnboim A., Goligorsky M.S., Del Vecchio P.J., Malik A.B. Activation of protein kinase C pathway contributes to hydrogen peroxide-induced increase in endothelial permeability. Laboratory Investigation 1992, 67:24-30.
    • (1992) Laboratory Investigation , vol.67 , pp. 24-30
    • Siflinger-Birnboim, A.1    Goligorsky, M.S.2    Del Vecchio, P.J.3    Malik, A.B.4
  • 88
    • 21444450963 scopus 로고    scopus 로고
    • 2 induces paracellular permeability of porcine brain-derived microvascular endothelial cells by activation of the p44/42 MAP kinase pathway
    • 2 induces paracellular permeability of porcine brain-derived microvascular endothelial cells by activation of the p44/42 MAP kinase pathway. European Journal of Cell Biology 2005, 84:687-697.
    • (2005) European Journal of Cell Biology , vol.84 , pp. 687-697
    • Fischer, S.1    Wiesnet, M.2    Renz, D.3    Schaper, W.4
  • 90
    • 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., Keenan A.K. Evidence for modulation of hydrogen peroxide-induced endothelial barrier dysfunction by nitric oxide in vitro. European Journal of Pharmacology 1996, 307:233-241.
    • (1996) European Journal of Pharmacology , vol.307 , pp. 233-241
    • McQuaid, K.E.1    Smyth, E.M.2    Keenan, A.K.3
  • 92
    • 0033529650 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-induced endothelial cell migration and proliferation depend on a nitric oxide-mediated decrease in protein kinase Cdelta activity
    • Shizukuda Y., Tang S., Yokota R., Ware J.A. Vascular endothelial growth factor-induced endothelial cell migration and proliferation depend on a nitric oxide-mediated decrease in protein kinase Cdelta activity. Circulation Research 1999, 85:247-256.
    • (1999) Circulation Research , vol.85 , pp. 247-256
    • Shizukuda, Y.1    Tang, S.2    Yokota, R.3    Ware, J.A.4
  • 93
    • 0029918676 scopus 로고    scopus 로고
    • The chemistry and tumoricidal activity of nitric oxide/hydrogen peroxide and the implications to cell resistance/susceptibility
    • Farias-Eisner R., Chaudhuri G., Aeberhard E., Fukuto J.M. The chemistry and tumoricidal activity of nitric oxide/hydrogen peroxide and the implications to cell resistance/susceptibility. The Journal of Biological Chemistry 1996, 271:6144-6151.
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 6144-6151
    • Farias-Eisner, R.1    Chaudhuri, G.2    Aeberhard, E.3    Fukuto, J.M.4
  • 97
    • 0029955451 scopus 로고    scopus 로고
    • Activation of protein phosphorylation by oxidants in vascular endothelial cells: identification of tyrosine phosphorylation of caveolin
    • Vepa S., Scribner W.M., Natarajan V. Activation of protein phosphorylation by oxidants in vascular endothelial cells: identification of tyrosine phosphorylation of caveolin. Free Radical Biology & Medicine 1997, 22:25-35.
    • (1997) Free Radical Biology & Medicine , vol.22 , pp. 25-35
    • Vepa, S.1    Scribner, W.M.2    Natarajan, V.3
  • 99
    • 0942287674 scopus 로고    scopus 로고
    • Enhanced survival effect of pyruvate correlates MAPK and NF-kappaB activation in hydrogen peroxide-treated human endothelial cells
    • [discussion 792]
    • Lee Y.J., Kang I.J., Bunger R., Kang Y.H. Enhanced survival effect of pyruvate correlates MAPK and NF-kappaB activation in hydrogen peroxide-treated human endothelial cells. Journal of Applied Physiology 2004, 96:793-801. [discussion 792].
    • (2004) Journal of Applied Physiology , vol.96 , pp. 793-801
    • Lee, Y.J.1    Kang, I.J.2    Bunger, R.3    Kang, Y.H.4
  • 101
    • 33845637858 scopus 로고    scopus 로고
    • 2 prosurvival effects in cultured endothelial cells
    • 2 prosurvival effects in cultured endothelial cells. FASEB Journal 2006, 20:1501-1503.
    • (2006) FASEB Journal , vol.20 , pp. 1501-1503
    • Yang, B.1    Oo, T.N.2    Rizzo, V.3
  • 102
    • 39749100001 scopus 로고    scopus 로고
    • Protein tyrosine phosphorylation and protein tyrosine nitration in redox signaling
    • Monteiro H.P., Arai R.J., Travassos L.R. Protein tyrosine phosphorylation and protein tyrosine nitration in redox signaling. Antioxidants & Redox Signaling 2008, 10:843-889.
    • (2008) Antioxidants & Redox Signaling , vol.10 , pp. 843-889
    • Monteiro, H.P.1    Arai, R.J.2    Travassos, L.R.3
  • 103
    • 0142106964 scopus 로고    scopus 로고
    • Nitric oxide and cGMP activate the Ras-MAP kinase pathway-stimulating protein tyrosine phosphorylation in rabbit aortic endothelial cells
    • Oliveira C.J., Schindler F., Ventura A.M., Morais M.S., Arai R.J., Debbas V., et al. Nitric oxide and cGMP activate the Ras-MAP kinase pathway-stimulating protein tyrosine phosphorylation in rabbit aortic endothelial cells. Free Radical Biology & Medicine 2003, 35:381-396.
    • (2003) Free Radical Biology & Medicine , vol.35 , pp. 381-396
    • Oliveira, C.J.1    Schindler, F.2    Ventura, A.M.3    Morais, M.S.4    Arai, R.J.5    Debbas, V.6
  • 105
    • 0030734010 scopus 로고    scopus 로고
    • P38 MAP kinase activation by vascular endothelial growth factor mediates actin reorganization and cell migration in human endothelial cells
    • Rousseau S., Houle F., Landry J., Huot J. p38 MAP kinase activation by vascular endothelial growth factor mediates actin reorganization and cell migration in human endothelial cells. Oncogene 1997, 15:2169-2177.
    • (1997) Oncogene , vol.15 , pp. 2169-2177
    • Rousseau, S.1    Houle, F.2    Landry, J.3    Huot, J.4
  • 106
    • 0031057892 scopus 로고    scopus 로고
    • Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells
    • Huot J., Houle F., Marceau F., Landry J. Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells. Circulation Research 1997, 80:383-392.
    • (1997) Circulation Research , vol.80 , pp. 383-392
    • Huot, J.1    Houle, F.2    Marceau, F.3    Landry, J.4
  • 109
    • 0029944965 scopus 로고    scopus 로고
    • Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1
    • Jiang B.H., Rue E., Wang G.L., Roe R., Semenza G.L. Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1. The Journal of Biological Chemistry 1996, 271:17771-17778.
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 17771-17778
    • Jiang, B.H.1    Rue, E.2    Wang, G.L.3    Roe, R.4    Semenza, G.L.5
  • 110
    • 0036216692 scopus 로고    scopus 로고
    • HIF-1 and tumor progression: pathophysiology and therapeutics
    • Semenza G.L. HIF-1 and tumor progression: pathophysiology and therapeutics. Trends in Molecular Medicine 2002, 8:S62-S67.
    • (2002) Trends in Molecular Medicine , vol.8
    • Semenza, G.L.1
  • 113
    • 0037472651 scopus 로고    scopus 로고
    • HIF-1 alpha protein as a target for S-nitrosation
    • Sumbayev V.V., Budde A., Zhou J., Brune B. HIF-1 alpha protein as a target for S-nitrosation. FEBS Letters 2003, 535:106-112.
    • (2003) FEBS Letters , vol.535 , pp. 106-112
    • Sumbayev, V.V.1    Budde, A.2    Zhou, J.3    Brune, B.4
  • 114
    • 2542506333 scopus 로고    scopus 로고
    • Redox-sensitive regulation of the HIF pathway under non-hypoxic conditions in pulmonary artery smooth muscle cells
    • BelAiba R.S., Djordjevic T., Bonello S., Flugel D., Hess J., Kietzmann T., et al. Redox-sensitive regulation of the HIF pathway under non-hypoxic conditions in pulmonary artery smooth muscle cells. Biological Chemistry 2004, 385:249-257.
    • (2004) Biological Chemistry , vol.385 , pp. 249-257
    • BelAiba, R.S.1    Djordjevic, T.2    Bonello, S.3    Flugel, D.4    Hess, J.5    Kietzmann, T.6
  • 115
    • 24344438196 scopus 로고    scopus 로고
    • Reactive oxygen species in the control of hypoxia-inducible factor-mediated gene expression
    • Kietzmann T., Gorlach A. Reactive oxygen species in the control of hypoxia-inducible factor-mediated gene expression. Seminars in Cell & Developmental Biology 2005, 16:474-486.
    • (2005) Seminars in Cell & Developmental Biology , vol.16 , pp. 474-486
    • Kietzmann, T.1    Gorlach, A.2
  • 118
    • 36048994258 scopus 로고    scopus 로고
    • Ets-1 is a critical transcriptional regulator of reactive oxygen species and p47(phox) gene expression in response to angiotensin II
    • Ni W., Zhan Y., He H., Maynard E., Balschi J.A., Oettgen P. Ets-1 is a critical transcriptional regulator of reactive oxygen species and p47(phox) gene expression in response to angiotensin II. Circulation Research 2007, 101:985-994.
    • (2007) Circulation Research , vol.101 , pp. 985-994
    • Ni, W.1    Zhan, Y.2    He, H.3    Maynard, E.4    Balschi, J.A.5    Oettgen, P.6
  • 119
    • 85027950157 scopus 로고    scopus 로고
    • Early inflammatory reactions in atherosclerosis are induced by proline-rich tyrosine kinase/reactive oxygen species-mediated release of tumor necrosis factor-alpha and subsequent activation of the p21Cip1/Ets-1/p300 system
    • Katsume A., Okigaki M., Matsui A., Che J., Adachi Y., Kishita E., et al. Early inflammatory reactions in atherosclerosis are induced by proline-rich tyrosine kinase/reactive oxygen species-mediated release of tumor necrosis factor-alpha and subsequent activation of the p21Cip1/Ets-1/p300 system. Arteriosclerosis, Thrombosis, and Vascular Biology 2011, 31:1084-1092.
    • (2011) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.31 , pp. 1084-1092
    • Katsume, A.1    Okigaki, M.2    Matsui, A.3    Che, J.4    Adachi, Y.5    Kishita, E.6
  • 122
    • 18544384985 scopus 로고    scopus 로고
    • Regulation of bone morphogenetic protein-2 expression in endothelial cells: role of nuclear factor-kappaB activation by tumor necrosis factor-alpha, H2O2, and high intravascular pressure
    • Csiszar A., Smith K.E., Koller A., Kaley G., Edwards J.G., Ungvari Z. Regulation of bone morphogenetic protein-2 expression in endothelial cells: role of nuclear factor-kappaB activation by tumor necrosis factor-alpha, H2O2, and high intravascular pressure. Circulation 2005, 111:2364-2372.
    • (2005) Circulation , vol.111 , pp. 2364-2372
    • Csiszar, A.1    Smith, K.E.2    Koller, A.3    Kaley, G.4    Edwards, J.G.5    Ungvari, Z.6
  • 123
    • 0030014964 scopus 로고    scopus 로고
    • Involvement of the transcription factor NF-kappaB in tubular morphogenesis of human microvascular endothelial cells by oxidative stress
    • Shono T., Ono M., Izumi H., Jimi S.I., Matsushima K., Okamoto T., et al. Involvement of the transcription factor NF-kappaB in tubular morphogenesis of human microvascular endothelial cells by oxidative stress. Molecular and Cellular Biology 1996, 16:4231-4239.
    • (1996) Molecular and Cellular Biology , vol.16 , pp. 4231-4239
    • Shono, T.1    Ono, M.2    Izumi, H.3    Jimi, S.I.4    Matsushima, K.5    Okamoto, T.6
  • 124
    • 38849199866 scopus 로고    scopus 로고
    • Mitochondrial dysfunction results from oxidative stress in the skeletal muscle of diet-induced insulin-resistant mice
    • Bonnard C., Durand A., Peyrol S., Chanseaume E., Chauvin M.A., Morio B., et al. Mitochondrial dysfunction results from oxidative stress in the skeletal muscle of diet-induced insulin-resistant mice. Journal of Clinical Investigation 2008, 118:789-800.
    • (2008) Journal of Clinical Investigation , vol.118 , pp. 789-800
    • Bonnard, C.1    Durand, A.2    Peyrol, S.3    Chanseaume, E.4    Chauvin, M.A.5    Morio, B.6
  • 125
    • 21444439103 scopus 로고    scopus 로고
    • NAD(P)H oxidase activation: a potential target mechanism for diabetic vascular complications, progressive beta-cell dysfunction and metabolic syndrome
    • Inoguchi T., Nawata H. NAD(P)H oxidase activation: a potential target mechanism for diabetic vascular complications, progressive beta-cell dysfunction and metabolic syndrome. Current Drug Targets 2005, 6:495-501.
    • (2005) Current Drug Targets , vol.6 , pp. 495-501
    • Inoguchi, T.1    Nawata, H.2
  • 126
    • 0037414393 scopus 로고    scopus 로고
    • NAD(P)H oxidase participates in the signaling events in high glucose-induced proliferation of vascular smooth muscle cells
    • Lee H.S., Son S.M., Kim Y.K., Hong K.W., Kim C.D. NAD(P)H oxidase participates in the signaling events in high glucose-induced proliferation of vascular smooth muscle cells. Life Sciences 2003, 72:2719-2730.
    • (2003) Life Sciences , vol.72 , pp. 2719-2730
    • Lee, H.S.1    Son, S.M.2    Kim, Y.K.3    Hong, K.W.4    Kim, C.D.5
  • 127
    • 79953265632 scopus 로고    scopus 로고
    • High glucose induces dysfunction and apoptosis in endothelial cells: is the effect of high glucose persistence more important than concentration?
    • Zhang Y., Shi H., Sun G., Li S., Xu X., Ye C., et al. High glucose induces dysfunction and apoptosis in endothelial cells: is the effect of high glucose persistence more important than concentration?. Experimental and Clinical Endocrinology & Diabetes 2011, 119:225-233.
    • (2011) Experimental and Clinical Endocrinology & Diabetes , vol.119 , pp. 225-233
    • Zhang, Y.1    Shi, H.2    Sun, G.3    Li, S.4    Xu, X.5    Ye, C.6
  • 128
    • 0028821016 scopus 로고
    • Theodore cooper memorial lecture hypertension and the pathogenesis of atherosclerosis. Oxidative stress and the mediation of arterial inflammatory response: a new perspective
    • Alexander R.W. Theodore cooper memorial lecture hypertension and the pathogenesis of atherosclerosis. Oxidative stress and the mediation of arterial inflammatory response: a new perspective. Hypertension 1995, 25:155-161.
    • (1995) Hypertension , vol.25 , pp. 155-161
    • Alexander, R.W.1
  • 129
    • 0037046214 scopus 로고    scopus 로고
    • Mechanisms of increased vascular superoxide production in human diabetes mellitus: role of NAD(P)H oxidase and endothelial nitric oxide synthase
    • Guzik T.J., Mussa S., Gastaldi D., Sadowski J., Ratnatunga C., Pillai R., et al. Mechanisms of increased vascular superoxide production in human diabetes mellitus: role of NAD(P)H oxidase and endothelial nitric oxide synthase. Circulation 2002, 105:1656-1662.
    • (2002) Circulation , vol.105 , pp. 1656-1662
    • Guzik, T.J.1    Mussa, S.2    Gastaldi, D.3    Sadowski, J.4    Ratnatunga, C.5    Pillai, R.6
  • 131
    • 79952163577 scopus 로고    scopus 로고
    • Inhibition of xanthine oxidase reduces hyperglycemia-induced oxidative stress and improves mitochondrial alterations in skeletal muscle of diabetic mice
    • Bravard A., Bonnard C., Durand A., Chauvin M.A., Favier R., Vidal H., et al. Inhibition of xanthine oxidase reduces hyperglycemia-induced oxidative stress and improves mitochondrial alterations in skeletal muscle of diabetic mice. American Journal of Physiology - Endocrinology And Metabolism 2011, 300:E581-E591.
    • (2011) American Journal of Physiology - Endocrinology And Metabolism , vol.300
    • Bravard, A.1    Bonnard, C.2    Durand, A.3    Chauvin, M.A.4    Favier, R.5    Vidal, H.6
  • 132
    • 0032965317 scopus 로고    scopus 로고
    • Rescue of diabetes-related impairment of angiogenesis by intramuscular gene therapy with adeno-VEGF
    • Rivard A., Silver M., Chen D., Kearney M., Magner M., Annex B., et al. Rescue of diabetes-related impairment of angiogenesis by intramuscular gene therapy with adeno-VEGF. American Journal of Pathology 1999, 154:355-363.
    • (1999) American Journal of Pathology , vol.154 , pp. 355-363
    • Rivard, A.1    Silver, M.2    Chen, D.3    Kearney, M.4    Magner, M.5    Annex, B.6
  • 134
    • 0034636835 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-A-induced chemotaxis of monocytes is attenuated in patients with diabetes mellitus: A potential predictor for the individual capacity to develop collaterals
    • Waltenberger J., Lange J., Kranz A. Vascular endothelial growth factor-A-induced chemotaxis of monocytes is attenuated in patients with diabetes mellitus: A potential predictor for the individual capacity to develop collaterals. Circulation 2000, 102:185-190.
    • (2000) Circulation , vol.102 , pp. 185-190
    • Waltenberger, J.1    Lange, J.2    Kranz, A.3
  • 135
    • 0037180517 scopus 로고    scopus 로고
    • Human endothelial progenitor cells from type II diabetics exhibit impaired proliferation, adhesion, and incorporation into vascular structures
    • Tepper O.M., Galiano R.D., Capla J.M., Kalka C., Gagne P.J., Jacobowitz G.R., et al. Human endothelial progenitor cells from type II diabetics exhibit impaired proliferation, adhesion, and incorporation into vascular structures. Circulation 2002, 106:2781-2786.
    • (2002) Circulation , vol.106 , pp. 2781-2786
    • Tepper, O.M.1    Galiano, R.D.2    Capla, J.M.3    Kalka, C.4    Gagne, P.J.5    Jacobowitz, G.R.6
  • 136
    • 33746641678 scopus 로고    scopus 로고
    • NADPH oxidase-derived overproduction of reactive oxygen species impairs postischemic neovascularization in mice with type 1 diabetes
    • Ebrahimian T.G., Heymes C., You D., Blanc-Brude O., Mees B., Waeckel L., et al. NADPH oxidase-derived overproduction of reactive oxygen species impairs postischemic neovascularization in mice with type 1 diabetes. The American Journal of Pathology 2006, 169:719-728.
    • (2006) The American Journal of Pathology , vol.169 , pp. 719-728
    • Ebrahimian, T.G.1    Heymes, C.2    You, D.3    Blanc-Brude, O.4    Mees, B.5    Waeckel, L.6
  • 137
    • 0345276632 scopus 로고    scopus 로고
    • Essential role of endothelial nitric oxide synthase for mobilization of stem and progenitor cells
    • Aicher A., Heeschen C., Mildner-Rihm C., Urbich C., Ihling C., Technau-Ihling K., et al. Essential role of endothelial nitric oxide synthase for mobilization of stem and progenitor cells. Nature Medicine 2003, 9:1370-1376.
    • (2003) Nature Medicine , vol.9 , pp. 1370-1376
    • Aicher, A.1    Heeschen, C.2    Mildner-Rihm, C.3    Urbich, C.4    Ihling, C.5    Technau-Ihling, K.6
  • 138
    • 0023576328 scopus 로고
    • Alterations in free radical tissue-defense mechanisms in streptozocin-induced diabetes in rat. Effects of insulin treatment
    • Wohaieb S.A., Godin D.V. Alterations in free radical tissue-defense mechanisms in streptozocin-induced diabetes in rat. Effects of insulin treatment. Diabetes 1987, 36:1014-1018.
    • (1987) Diabetes , vol.36 , pp. 1014-1018
    • Wohaieb, S.A.1    Godin, D.V.2
  • 139
    • 78149386479 scopus 로고    scopus 로고
    • N-acetyl cysteine promotes angiogenesis and clearance of free oxygen radicals, thus improving wound healing in an alloxan-induced diabetic mouse model of incisional wound
    • Aktunc E., Ozacmak V.H., Ozacmak H.S., Barut F., Buyukates M., Kandemir O., et al. N-acetyl cysteine promotes angiogenesis and clearance of free oxygen radicals, thus improving wound healing in an alloxan-induced diabetic mouse model of incisional wound. Clinical and Experimental Dermatology 2010, 35:902-909.
    • (2010) Clinical and Experimental Dermatology , vol.35 , pp. 902-909
    • Aktunc, E.1    Ozacmak, V.H.2    Ozacmak, H.S.3    Barut, F.4    Buyukates, M.5    Kandemir, O.6
  • 141
    • 0035434119 scopus 로고    scopus 로고
    • Abnormalities of retinal metabolism in diabetes and experimental galactosemia VII. Effect of long-term administration of antioxidants on the development of retinopathy
    • Kowluru R.A., Tang J., Kern T.S. Abnormalities of retinal metabolism in diabetes and experimental galactosemia VII. Effect of long-term administration of antioxidants on the development of retinopathy. Diabetes 2001, 50:1938-1942.
    • (2001) Diabetes , vol.50 , pp. 1938-1942
    • Kowluru, R.A.1    Tang, J.2    Kern, T.S.3
  • 142
    • 0032520871 scopus 로고    scopus 로고
    • Advanced glycation end products increase retinal vascular endothelial growth factor expression
    • Lu M., Kuroki M., Amano S., Tolentino M., Keough K., Kim I., et al. Advanced glycation end products increase retinal vascular endothelial growth factor expression. Journal of Clinical Investigation 1998, 101:1219-1224.
    • (1998) Journal of Clinical Investigation , vol.101 , pp. 1219-1224
    • Lu, M.1    Kuroki, M.2    Amano, S.3    Tolentino, M.4    Keough, K.5    Kim, I.6
  • 143
    • 78650894319 scopus 로고    scopus 로고
    • Crosstalk of reactive oxygen species and NF-κB signaling
    • Morgan M.J., Liu Z.G. Crosstalk of reactive oxygen species and NF-κB signaling. Cell Research 2011, 21:103-115.
    • (2011) Cell Research , vol.21 , pp. 103-115
    • Morgan, M.J.1    Liu, Z.G.2
  • 144
    • 0032796794 scopus 로고    scopus 로고
    • L-Arginine transport in retinas from streptozotocin diabetic rats: correlation with the level of IL-1 beta and NO synthase activity
    • Carmo A., Cunha-Vaz J.G., Carvalho A.P., Lopes M.C. l-Arginine transport in retinas from streptozotocin diabetic rats: correlation with the level of IL-1 beta and NO synthase activity. Vision Research 1999, 39:3817-3823.
    • (1999) Vision Research , vol.39 , pp. 3817-3823
    • Carmo, A.1    Cunha-Vaz, J.G.2    Carvalho, A.P.3    Lopes, M.C.4
  • 145
    • 4744347272 scopus 로고    scopus 로고
    • Role of interleukin-1beta in the pathogenesis of diabetic retinopathy
    • Kowluru R.A., Odenbach S. Role of interleukin-1beta in the pathogenesis of diabetic retinopathy. British Journal of Ophthalmology 2004, 88:1343-1347.
    • (2004) British Journal of Ophthalmology , vol.88 , pp. 1343-1347
    • Kowluru, R.A.1    Odenbach, S.2
  • 146
    • 0032415840 scopus 로고    scopus 로고
    • Expression of nitric oxide synthases and formation of nitrotyrosine and reactive oxygen species in inflammatory bowel disease
    • Dijkstra G., Moshage H., van Dullemen H.M., de Jager-Krikken A., Tiebosch A.T., Kleibeuker J.H., et al. Expression of nitric oxide synthases and formation of nitrotyrosine and reactive oxygen species in inflammatory bowel disease. Journal of Pathology 1998, 186:416-421.
    • (1998) Journal of Pathology , vol.186 , pp. 416-421
    • Dijkstra, G.1    Moshage, H.2    van Dullemen, H.M.3    de Jager-Krikken, A.4    Tiebosch, A.T.5    Kleibeuker, J.H.6
  • 147
    • 33749537296 scopus 로고    scopus 로고
    • Reactive oxygen species regulate epidermal growth factor-induced vascular endothelial growth factor and hypoxia-inducible factor-1alpha expression through activation of AKT and P70S6K1 in human ovarian cancer cells
    • Liu L.Z., Hu X.W., Xia C., He J., Zhou Q., Shi X., et al. Reactive oxygen species regulate epidermal growth factor-induced vascular endothelial growth factor and hypoxia-inducible factor-1alpha expression through activation of AKT and P70S6K1 in human ovarian cancer cells. Free Radical Biology & Medicine 2006, 41:1521-1533.
    • (2006) Free Radical Biology & Medicine , vol.41 , pp. 1521-1533
    • Liu, L.Z.1    Hu, X.W.2    Xia, C.3    He, J.4    Zhou, Q.5    Shi, X.6
  • 148
    • 0035796023 scopus 로고    scopus 로고
    • The contribution of endogenous sources of DNA damage to the multiple mutations in cancer
    • Jackson A.L., Loeb L.A. The contribution of endogenous sources of DNA damage to the multiple mutations in cancer. Mutation Research 2001, 477:7-21.
    • (2001) Mutation Research , vol.477 , pp. 7-21
    • Jackson, A.L.1    Loeb, L.A.2
  • 149
    • 0028115871 scopus 로고
    • X-irradiation, phorbol esters, and H2O2 stimulate mitogen-activated protein kinase activity in NIH-3T3 cells through the formation of reactive oxygen intermediates
    • Stevenson M.A., Pollock S.S., Coleman C.N., Calderwood S.K. X-irradiation, phorbol esters, and H2O2 stimulate mitogen-activated protein kinase activity in NIH-3T3 cells through the formation of reactive oxygen intermediates. Cancer Research 1994, 54:12-15.
    • (1994) Cancer Research , vol.54 , pp. 12-15
    • Stevenson, M.A.1    Pollock, S.S.2    Coleman, C.N.3    Calderwood, S.K.4
  • 150
    • 8544273759 scopus 로고    scopus 로고
    • Vascular endothelial growth factor transcriptional activation is mediated by hypoxia-inducible factor 1alpha, HDM2, and p70S6K1 in response to phosphatidylinositol 3-kinase/AKT signaling
    • Skinner H.D., Zheng J.Z., Fang J., Agani F., Jiang B.H. Vascular endothelial growth factor transcriptional activation is mediated by hypoxia-inducible factor 1alpha, HDM2, and p70S6K1 in response to phosphatidylinositol 3-kinase/AKT signaling. The Journal of Biological Chemistry 2004, 279:45643-45651.
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 45643-45651
    • Skinner, H.D.1    Zheng, J.Z.2    Fang, J.3    Agani, F.4    Jiang, B.H.5
  • 151
    • 16644395747 scopus 로고    scopus 로고
    • The role of VEGF in the regulation of physiological and pathological angiogenesis
    • Ferrara N. The role of VEGF in the regulation of physiological and pathological angiogenesis. EXS 2005, 209-233.
    • (2005) EXS , pp. 209-233
    • Ferrara, N.1
  • 152
    • 77951241278 scopus 로고    scopus 로고
    • Terpestacin inhibits tumor angiogenesis by targeting UQCRB of mitochondrial complex III and suppressing hypoxia-induced reactive oxygen species production and cellular oxygen sensing
    • Jung H.J., Shim J.S., Lee J., Song Y.M., Park K.C., Choi S.H., et al. Terpestacin inhibits tumor angiogenesis by targeting UQCRB of mitochondrial complex III and suppressing hypoxia-induced reactive oxygen species production and cellular oxygen sensing. The Journal of Biological Chemistry 2010, 285:11584-11595.
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 11584-11595
    • Jung, H.J.1    Shim, J.S.2    Lee, J.3    Song, Y.M.4    Park, K.C.5    Choi, S.H.6
  • 153
    • 84555187316 scopus 로고    scopus 로고
    • Cadmium increases HIF-1 and VEGF expression through ROS, ERK, and AKT signaling pathways and induces malignant transformation of human bronchial epithelial cells
    • Jing Y., Liu L.Z., Jiang Y., Zhu Y., Guo N.L., Barnett J., et al. Cadmium increases HIF-1 and VEGF expression through ROS, ERK, and AKT signaling pathways and induces malignant transformation of human bronchial epithelial cells. Toxicological Sciences 2012, 125:10-19.
    • (2012) Toxicological Sciences , vol.125 , pp. 10-19
    • Jing, Y.1    Liu, L.Z.2    Jiang, Y.3    Zhu, Y.4    Guo, N.L.5    Barnett, J.6
  • 157
    • 14644392861 scopus 로고    scopus 로고
    • Redox control of angiogenic factors and CD31-positive vessel-like structures in mouse embryonic stem cells after direct current electrical field stimulation
    • Sauer H., Bekhite M.M., Hescheler J., Wartenberg M. Redox control of angiogenic factors and CD31-positive vessel-like structures in mouse embryonic stem cells after direct current electrical field stimulation. Experimental Cell Research 2005, 304:380-390.
    • (2005) Experimental Cell Research , vol.304 , pp. 380-390
    • Sauer, H.1    Bekhite, M.M.2    Hescheler, J.3    Wartenberg, M.4
  • 158
    • 33845647995 scopus 로고    scopus 로고
    • Embryonic stem cells utilize reactive oxygen species as transducers of mechanical strain-induced cardiovascular differentiation
    • Schmelter M., Ateghang B., Helmig S., Wartenberg M., Sauer H. Embryonic stem cells utilize reactive oxygen species as transducers of mechanical strain-induced cardiovascular differentiation. FASEB Journal 2006, 20:1182-1184.
    • (2006) FASEB Journal , vol.20 , pp. 1182-1184
    • Schmelter, M.1    Ateghang, B.2    Helmig, S.3    Wartenberg, M.4    Sauer, H.5
  • 160
    • 18444401175 scopus 로고    scopus 로고
    • Role of gp91phox (Nox2)-containing NAD(P)H oxidase in angiogenesis in response to hindlimb ischemia
    • Tojo T., Ushio-Fukai M., Yamaoka-Tojo M., Ikeda S., Patrushev N., Alexander R.W. Role of gp91phox (Nox2)-containing NAD(P)H oxidase in angiogenesis in response to hindlimb ischemia. Circulation 2005, 111:2347-2355.
    • (2005) Circulation , vol.111 , pp. 2347-2355
    • Tojo, T.1    Ushio-Fukai, M.2    Yamaoka-Tojo, M.3    Ikeda, S.4    Patrushev, N.5    Alexander, R.W.6
  • 164
    • 0344875019 scopus 로고    scopus 로고
    • Thioredoxin: a key regulator of cardiovascular homeostasis
    • Yamawaki H., Haendeler J., Berk B.C. Thioredoxin: a key regulator of cardiovascular homeostasis. Circulation Research 2003, 93:1029-1033.
    • (2003) Circulation Research , vol.93 , pp. 1029-1033
    • Yamawaki, H.1    Haendeler, J.2    Berk, B.C.3
  • 165
    • 0036735392 scopus 로고    scopus 로고
    • The redox protein thioredoxin-1 (Trx-1) increases hypoxia-inducible factor 1alpha protein expression: Trx-1 overexpression results in increased vascular endothelial growth factor production and enhanced tumor angiogenesis
    • Welsh S.J., Bellamy W.T., Briehl M.M., Powis G. The redox protein thioredoxin-1 (Trx-1) increases hypoxia-inducible factor 1alpha protein expression: Trx-1 overexpression results in increased vascular endothelial growth factor production and enhanced tumor angiogenesis. Cancer Research 2002, 62:5089-5095.
    • (2002) Cancer Research , vol.62 , pp. 5089-5095
    • Welsh, S.J.1    Bellamy, W.T.2    Briehl, M.M.3    Powis, G.4
  • 166
    • 84866618479 scopus 로고    scopus 로고
    • Expression of thioredoxin-1 and hypoxia inducible factor-1alpha in cerebral arteriovenous malformations: possible role of redox regulatory factor in neoangiogenic property
    • Takagi Y., Kikuta K., Moriwaki T., Aoki T., Nozaki K., Hashimoto N., et al. Expression of thioredoxin-1 and hypoxia inducible factor-1alpha in cerebral arteriovenous malformations: possible role of redox regulatory factor in neoangiogenic property. Surgical Neurology International 2011, 2:61.
    • (2011) Surgical Neurology International , vol.2 , pp. 61
    • Takagi, Y.1    Kikuta, K.2    Moriwaki, T.3    Aoki, T.4    Nozaki, K.5    Hashimoto, N.6
  • 167
    • 77950496435 scopus 로고    scopus 로고
    • Thioredoxin-1 gene therapy enhances angiogenic signaling and reduces ventricular remodeling in infarcted myocardium of diabetic rats
    • Samuel S.M., Thirunavukkarasu M., Penumathsa S.V., Koneru S., Zhan L., Maulik G., et al. Thioredoxin-1 gene therapy enhances angiogenic signaling and reduces ventricular remodeling in infarcted myocardium of diabetic rats. Circulation 2010, 121:1244-1255.
    • (2010) Circulation , vol.121 , pp. 1244-1255
    • Samuel, S.M.1    Thirunavukkarasu, M.2    Penumathsa, S.V.3    Koneru, S.4    Zhan, L.5    Maulik, G.6
  • 168
    • 78650806850 scopus 로고    scopus 로고
    • Thioredoxin 1 enhances neovascularization and reduces ventricular remodeling during chronic myocardial infarction: a study using thioredoxin 1 transgenic mice
    • Adluri R.S., Thirunavukkarasu M., Zhan L., Akita Y., Samuel S.M., Otani H., et al. Thioredoxin 1 enhances neovascularization and reduces ventricular remodeling during chronic myocardial infarction: a study using thioredoxin 1 transgenic mice. Journal of Molecular and Cellular Cardiology 2011, 50:239-247.
    • (2011) Journal of Molecular and Cellular Cardiology , vol.50 , pp. 239-247
    • Adluri, R.S.1    Thirunavukkarasu, M.2    Zhan, L.3    Akita, Y.4    Samuel, S.M.5    Otani, H.6
  • 169
    • 63449128721 scopus 로고    scopus 로고
    • Endothelial-specific expression of mitochondrial thioredoxin promotes ischemia-mediated arteriogenesis and angiogenesis
    • Dai S., He Y., Zhang H., Yu L., Wan T., Xu Z., et al. Endothelial-specific expression of mitochondrial thioredoxin promotes ischemia-mediated arteriogenesis and angiogenesis. Arteriosclerosis, Thrombosis, and Vascular Biology 2009, 29:495-502.
    • (2009) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.29 , pp. 495-502
    • Dai, S.1    He, Y.2    Zhang, H.3    Yu, L.4    Wan, T.5    Xu, Z.6
  • 171
    • 84856741245 scopus 로고    scopus 로고
    • Posttranslational modification of cysteine in redox signaling and oxidative stress: focus on S-glutathionylation
    • Mieyal J.J., Chock P.B. Posttranslational modification of cysteine in redox signaling and oxidative stress: focus on S-glutathionylation. Antioxidants & Redox Signaling 2012, 16:471-475.
    • (2012) Antioxidants & Redox Signaling , vol.16 , pp. 471-475
    • Mieyal, J.J.1    Chock, P.B.2
  • 172
    • 84866601999 scopus 로고    scopus 로고
    • Glutathione synthesis and its role in redox signaling
    • [Epub ahead of print]
    • Zhang H., Forman H.J. Glutathione synthesis and its role in redox signaling. Seminars in Cell & Developmental Biology 2012, [Epub ahead of print]. 10.1016/j.semcdb.2012.03.017.
    • (2012) Seminars in Cell & Developmental Biology
    • Zhang, H.1    Forman, H.J.2
  • 173
    • 0027730870 scopus 로고
    • Modulation of human microvascular endothelial cell bioenergetic status and glutathione levels during proliferative and differentiated growth
    • Mallery S.R., Lantry L.E., Laufman H.B., Stephens R.E., Brierley G.P. Modulation of human microvascular endothelial cell bioenergetic status and glutathione levels during proliferative and differentiated growth. Journal of Cellular Biochemistry 1993, 53:360-372.
    • (1993) Journal of Cellular Biochemistry , vol.53 , pp. 360-372
    • Mallery, S.R.1    Lantry, L.E.2    Laufman, H.B.3    Stephens, R.E.4    Brierley, G.P.5
  • 174
    • 0035890541 scopus 로고    scopus 로고
    • Inhibition of angiogenesis-driven Kaposi's sarcoma tumor growth in nude mice by oral N-acetylcysteine
    • Albini A., Morini M., D'Agostini F., Ferrari N., Campelli F., Arena G., et al. Inhibition of angiogenesis-driven Kaposi's sarcoma tumor growth in nude mice by oral N-acetylcysteine. Cancer Research 2001, 61:8171-8178.
    • (2001) Cancer Research , vol.61 , pp. 8171-8178
    • Albini, A.1    Morini, M.2    D'Agostini, F.3    Ferrari, N.4    Campelli, F.5    Arena, G.6
  • 175
    • 0029737527 scopus 로고    scopus 로고
    • Glutathione inhibits experimental oral carcinogenesis, p53 expression, and angiogenesis
    • Schwartz J.L., Shklar G. Glutathione inhibits experimental oral carcinogenesis, p53 expression, and angiogenesis. Nutrition and Cancer 1996, 26:229-236.
    • (1996) Nutrition and Cancer , vol.26 , pp. 229-236
    • Schwartz, J.L.1    Shklar, G.2
  • 180
    • 77955516336 scopus 로고    scopus 로고
    • ICAM-1 cytoplasmic tail regulates endothelial glutathione synthesis through a NOX4/PI3-kinase-dependent pathway
    • Pattillo C.B., Pardue S., Shen X., Fang K., Langston W., Jourd'heuil D., et al. ICAM-1 cytoplasmic tail regulates endothelial glutathione synthesis through a NOX4/PI3-kinase-dependent pathway. Free Radical Biology & Medicine 2010, 49:1119-1128.
    • (2010) Free Radical Biology & Medicine , vol.49 , pp. 1119-1128
    • Pattillo, C.B.1    Pardue, S.2    Shen, X.3    Fang, K.4    Langston, W.5    Jourd'heuil, D.6
  • 182
    • 33644866801 scopus 로고    scopus 로고
    • Impaired angiogenesis in glutathione peroxidase-1-deficient mice is associated with endothelial progenitor cell dysfunction
    • Galasso G., Schiekofer S., Sato K., Shibata R., Handy D.E., Ouchi N., et al. Impaired angiogenesis in glutathione peroxidase-1-deficient mice is associated with endothelial progenitor cell dysfunction. Circulation Research 2006, 98:254-261.
    • (2006) Circulation Research , vol.98 , pp. 254-261
    • Galasso, G.1    Schiekofer, S.2    Sato, K.3    Shibata, R.4    Handy, D.E.5    Ouchi, N.6
  • 183
    • 79951643450 scopus 로고    scopus 로고
    • Multiple functions of peroxiredoxins: peroxidases, sensors and regulators of the intracellular messenger H(2)O(2), and protein chaperones
    • Rhee S.G., Woo H.A. Multiple functions of peroxiredoxins: peroxidases, sensors and regulators of the intracellular messenger H(2)O(2), and protein chaperones. Antioxidants & Redox Signaling 2011, 15:781-794.
    • (2011) Antioxidants & Redox Signaling , vol.15 , pp. 781-794
    • Rhee, S.G.1    Woo, H.A.2
  • 185
    • 80052970775 scopus 로고    scopus 로고
    • Peroxiredoxin 2 deficiency exacerbates atherosclerosis in apolipoprotein E-deficient mice
    • Park J.G., Yoo J.Y., Jeong S.J., Choi J.H., Lee M.R., Lee M.N., et al. Peroxiredoxin 2 deficiency exacerbates atherosclerosis in apolipoprotein E-deficient mice. Circulation Research 2011, 109:739-749.
    • (2011) Circulation Research , vol.109 , pp. 739-749
    • Park, J.G.1    Yoo, J.Y.2    Jeong, S.J.3    Choi, J.H.4    Lee, M.R.5    Lee, M.N.6
  • 186
    • 38349117219 scopus 로고    scopus 로고
    • Laminar shear stress up-regulates peroxiredoxins (PRX) in endothelial cells: PRX 1 as a mechanosensitive antioxidant
    • Mowbray A.L., Kang D.H., Rhee S.G., Kang S.W., Jo H. Laminar shear stress up-regulates peroxiredoxins (PRX) in endothelial cells: PRX 1 as a mechanosensitive antioxidant. The Journal of Biological Chemistry 2008, 283:1622-1627.
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 1622-1627
    • Mowbray, A.L.1    Kang, D.H.2    Rhee, S.G.3    Kang, S.W.4    Jo, H.5
  • 187
    • 79952231198 scopus 로고    scopus 로고
    • Peroxiredoxin 1 controls prostate cancer growth through Toll-like receptor 4-dependent regulation of tumor vasculature
    • Riddell J.R., Bshara W., Moser M.T., Spernyak J.A., Foster B.A., Gollnick S.O. Peroxiredoxin 1 controls prostate cancer growth through Toll-like receptor 4-dependent regulation of tumor vasculature. Cancer Research 2011, 71:1637-1646.
    • (2011) Cancer Research , vol.71 , pp. 1637-1646
    • Riddell, J.R.1    Bshara, W.2    Moser, M.T.3    Spernyak, J.A.4    Foster, B.A.5    Gollnick, S.O.6
  • 188
    • 0041355362 scopus 로고    scopus 로고
    • Expression of peroxiredoxin II in vascular tumors of the skin: a novel vascular marker of endothelial cells
    • Lee S.C., Na Y.P., Lee J.B. Expression of peroxiredoxin II in vascular tumors of the skin: a novel vascular marker of endothelial cells. Journal of the American Academy of Dermatology 2003, 49:487-491.
    • (2003) Journal of the American Academy of Dermatology , vol.49 , pp. 487-491
    • Lee, S.C.1    Na, Y.P.2    Lee, J.B.3
  • 189
    • 81355150904 scopus 로고    scopus 로고
    • Peroxiredoxin II is an essential antioxidant enzyme that prevents the oxidative inactivation of VEGF receptor-2 in vascular endothelial cells
    • Kang D.H., Lee D.J., Lee K.W., Park Y.S., Lee J.Y., Lee S.H., et al. Peroxiredoxin II is an essential antioxidant enzyme that prevents the oxidative inactivation of VEGF receptor-2 in vascular endothelial cells. Molecular Cell 2011, 44:545-558.
    • (2011) Molecular Cell , vol.44 , pp. 545-558
    • Kang, D.H.1    Lee, D.J.2    Lee, K.W.3    Park, Y.S.4    Lee, J.Y.5    Lee, S.H.6


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