메뉴 건너뛰기




Volumn 17, Issue 1-4, 2003, Pages 287-296

Redox signaling and the MAP kinase pathways

Author keywords

MAP kinase; Redox signaling; Signal transduction; Thiols

Indexed keywords

ANGIOTENSIN; ANTIOXIDANT; G PROTEIN COUPLED RECEPTOR; GLUTATHIONE; GLUTATHIONE TRANSFERASE; HYDROGEN PEROXIDE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LIGAND; LYSOPHOSPHATIDIC ACID; MENADIONE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; PROLINE; PROTEIN P53; PROTEIN SERINE THREONINE KINASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; RHO FACTOR; SEROTONIN; STRESS ACTIVATED PROTEIN KINASE; SUPEROXIDE; SYNAPTOPHYSIN; THREONINE; TRANSCRIPTION FACTOR; TUMOR NECROSIS FACTOR ALPHA; TYROSINE;

EID: 0142043984     PISSN: 09516433     EISSN: None     Source Type: Journal    
DOI: 10.1002/biof.5520170128     Document Type: Conference Paper
Times cited : (503)

References (70)
  • 2
    • 15144343374 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation
    • Y.S. Bae, S.W. Kang, M.S. Seo, I.C. Baines, E. Tekle, P.B. Chock and S.G. Rhee, Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation, J. Biol. Chem. 272 (1997), 217-221.
    • (1997) J. Biol. Chem. , vol.272 , pp. 217-221
    • Bae, Y.S.1    Kang, S.W.2    Seo, M.S.3    Baines, I.C.4    Tekle, E.5    Chock, P.B.6    Rhee, S.G.7
  • 4
    • 0034782946 scopus 로고    scopus 로고
    • Redox signaling in macrophages
    • H.J. Forman and M. Torres, Redox signaling in macrophages, Mol. Aspects Med. 22 (2001), 189-216.
    • (2001) Mol. Aspects Med. , vol.22 , pp. 189-216
    • Forman, H.J.1    Torres, M.2
  • 5
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • W. Droge, Free radicals in the physiological control of cell function, Physiol Rev. 82 (2002), 47-95.
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Droge, W.1
  • 7
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • J.M. Kyriakis and J. Avruch, Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation, Physiol. Rev. 81 (2001), 807-869.
    • (2001) Physiol. Rev. , vol.81 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 9
    • 0034762203 scopus 로고    scopus 로고
    • The Raf/MEK/ERK pathway: New concepts of activation
    • C. Peyssonnaux and A. Eychene, The Raf/MEK/ERK pathway: new concepts of activation, Biol. Cell 93 (2001), 53-62.
    • (2001) Biol. Cell , vol.93 , pp. 53-62
    • Peyssonnaux, C.1    Eychene, A.2
  • 10
    • 0034644522 scopus 로고    scopus 로고
    • Signal transduction by the JNK group of MAP kinases
    • R.J. Davis, Signal transduction by the JNK group of MAP kinases, Cell 103 (2000), 239-252.
    • (2000) Cell , vol.103 , pp. 239-252
    • Davis, R.J.1
  • 11
    • 0035451062 scopus 로고    scopus 로고
    • To be or not to be: A question of B-Raf?
    • W. Kolch, To be or not to be: a question of B-Raf? Trends Neurosci. 24 (2001), 498-500.
    • (2001) Trends Neurosci. , vol.24 , pp. 498-500
    • Kolch, W.1
  • 12
    • 0037080956 scopus 로고    scopus 로고
    • Regulation of Raf-1 activation and signalling by dephosphorylation
    • A.S. Dhillon, S. Meikle, Z. Yazici, M. Eulitz and W. Kolch, Regulation of Raf-1 activation and signalling by dephosphorylation, EMBO J. 21 (2002), 64-71.
    • (2002) EMBO J. , vol.21 , pp. 64-71
    • Dhillon, A.S.1    Meikle, S.2    Yazici, Z.3    Eulitz, M.4    Kolch, W.5
  • 13
    • 0034667593 scopus 로고    scopus 로고
    • Meaningful relationships: The regulation of the Ras/Raf/MEK/ERK pathway by protein interactions
    • W. Kolch, Meaningful relationships: the regulation of the Ras/Raf/MEK/ ERK pathway by protein interactions, Biochem. J. 351 (2000), 289-305.
    • (2000) Biochem. J. , vol.351 , pp. 289-305
    • Kolch, W.1
  • 14
    • 0035398487 scopus 로고    scopus 로고
    • G-protein-coupled receptors and signaling networks: Emerging paradigms
    • M.J. Marinissen and J.S. Gutkind, G-protein-coupled receptors and signaling networks: emerging paradigms, Trends Pharmacol. Sci. 22 (2001), 368-376.
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 368-376
    • Marinissen, M.J.1    Gutkind, J.S.2
  • 15
    • 0035903222 scopus 로고    scopus 로고
    • Impaired synergistic activation of stress-activated protein kinase SAPK/JNK in mouse embryonic stem cells lacking SEK1/MKK4: Different contribution of SEK2/MKK7 isoforms to the synergistic activation
    • T. Wada, K. Nakagawa, T. Watanabe, G. Nishitai, J. Seo, H. Kishimoto, D. Kitagawa, T. Sasaki, J.M. Penninger, H. Nishina and T. Katada, Impaired synergistic activation of stress-activated protein kinase SAPK/JNK in mouse embryonic stem cells lacking SEK1/MKK4: different contribution of SEK2/MKK7 isoforms to the synergistic activation, J. Biol. Chem. 276 (2001), 30892-30897.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30892-30897
    • Wada, T.1    Nakagawa, K.2    Watanabe, T.3    Nishitai, G.4    Seo, J.5    Kishimoto, H.6    Kitagawa, D.7    Sasaki, T.8    Penninger, J.M.9    Nishina, H.10    Katada, T.11
  • 17
    • 0032508538 scopus 로고    scopus 로고
    • MP1: A MEK binding partner that enhances enzymatic activation of the MAP kinase cascade
    • H.J. Schaeffer, A.D. Catling, S.T. Eblen, L.S. Collier, A. Krauss and M.J. Weber, MP1: A MEK binding partner that enhances enzymatic activation of the MAP kinase cascade, Science 281 (1998), 1668-1671.
    • (1998) Science , vol.281 , pp. 1668-1671
    • Schaeffer, H.J.1    Catling, A.D.2    Eblen, S.T.3    Collier, L.S.4    Krauss, A.5    Weber, M.J.6
  • 18
    • 0036499130 scopus 로고    scopus 로고
    • Arresting developments in heptahelical receptor signaling and regulation
    • S.J. Perry and R.J. Lefkowitz, Arresting developments in heptahelical receptor signaling and regulation, Trends Cell Biol. 12 (2002), 130-138.
    • (2002) Trends Cell Biol. , vol.12 , pp. 130-138
    • Perry, S.J.1    Lefkowitz, R.J.2
  • 20
    • 0033499801 scopus 로고    scopus 로고
    • BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G2/M
    • K. Yamamoto, H. Ichijo and S.J. Korsmeyer, BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G2/M, Mol. Cell Biol 19 (1999), 8469-8478.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 8469-8478
    • Yamamoto, K.1    Ichijo, H.2    Korsmeyer, S.J.3
  • 21
    • 0034759115 scopus 로고    scopus 로고
    • Regulation of MAP kinases by docking domains
    • H. Enslen and R.J. Davis, Regulation of MAP kinases by docking domains, Biol. Cell 93 (2001), 5-14.
    • (2001) Biol. Cell , vol.93 , pp. 5-14
    • Enslen, H.1    Davis, R.J.2
  • 22
    • 0029808748 scopus 로고    scopus 로고
    • Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways
    • A.J. Whitmarsh and R.J. Davis, Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways, J Mol. Med 74 (1996), 589-607.
    • (1996) J. Mol. Med. , vol.74 , pp. 589-607
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 23
    • 0032977187 scopus 로고    scopus 로고
    • A network of mitogen-activated protein kinases links G protein-coupled receptors to the c-jun promoter: A role for c-Jun NH2-terminal kinase, p38s, and extracellular signal-regulated kinase 5
    • M.J. Marinissen, M. Chiariello, M. Pallante and J.S. Gutkind, A network of mitogen-activated protein kinases links G protein-coupled receptors to the c-jun promoter: a role for c-Jun NH2-terminal kinase, p38s, and extracellular signal-regulated kinase 5, Mol. Cell Biol. 19 (1999), 4289-4301.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 4289-4301
    • Marinissen, M.J.1    Chiariello, M.2    Pallante, M.3    Gutkind, J.S.4
  • 24
    • 0027238929 scopus 로고
    • Stimulation of human neutrophils with formyl-methionyl-leucyl-phenylalanine induces tyrosine phosphorylation and activation of two distinct mitogen-activated protein kinases
    • M. Torres, F.L. Hall and K.A. O'Neill, Stimulation of human neutrophils with formyl-methionyl-leucyl-phenylalanine induces tyrosine phosphorylation and activation of two distinct mitogen-activated protein kinases, J. Immunol. 150 (1993), 1563-1576.
    • (1993) J. Immunol. , vol.150 , pp. 1563-1576
    • Torres, M.1    Hall, F.L.2    O'Neill, K.A.3
  • 25
    • 0033970533 scopus 로고    scopus 로고
    • Dual specificity phosphatases: A gene family for control of MAP kinase function
    • M. Camps, A. Nichols and S. Arkinstall, Dual specificity phosphatases: a gene family for control of MAP kinase function, FASEB J. 14 (2000), 6-16.
    • (2000) FASEB J. , vol.14 , pp. 6-16
    • Camps, M.1    Nichols, A.2    Arkinstall, S.3
  • 27
    • 0029955623 scopus 로고    scopus 로고
    • Reactive oxygen species mediate cytokine activation of c-Jun NH2-terminal kinases
    • Y.Y.C. Lo, J.M.S. Wong and T.F. Cruz, Reactive oxygen species mediate cytokine activation of c-Jun NH2-terminal kinases, J. Biol. Chem. 271 (1996), 15703-15707.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15703-15707
    • Lo, Y.Y.C.1    Wong, J.M.S.2    Cruz, T.F.3
  • 28
    • 0032527705 scopus 로고    scopus 로고
    • The cellular response to oxidative stress: Influences of mitogen-activated protein kinase signalling pathways on cell survival
    • X.T. Wang, J.L. Martindale, Y.S. Liu and N.J. Holbrook, The cellular response to oxidative stress: influences of mitogen-activated protein kinase signalling pathways on cell survival, Biochem. J 333 (1998), 291-300.
    • (1998) Biochem. J. , vol.333 , pp. 291-300
    • Wang, X.T.1    Martindale, J.L.2    Liu, Y.S.3    Holbrook, N.J.4
  • 29
    • 0032889677 scopus 로고    scopus 로고
    • Redox regulation of cellular signalling
    • H. Kamata and H. Hirata, Redox regulation of cellular signalling, Cell Signal. 11 (1999), 1-14.
    • (1999) Cell Signal. , vol.11 , pp. 1-14
    • Kamata, H.1    Hirata, H.2
  • 30
    • 0030789179 scopus 로고    scopus 로고
    • The level of intracellular glutathione is a key regulator for the induction of stress-activated signal transduction pathways including Jun N-terminal protein kinases and p38 kinase by alkylating agents
    • D. Wilhelm, K. Bender, A. Knebel and P. Angel, The level of intracellular glutathione is a key regulator for the induction of stress-activated signal transduction pathways including Jun N-terminal protein kinases and p38 kinase by alkylating agents, Mol. Cell Biol. 17 (1997), 4792-4800.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 4792-4800
    • Wilhelm, D.1    Bender, K.2    Knebel, A.3    Angel, P.4
  • 31
    • 0029896250 scopus 로고    scopus 로고
    • Big mitogen-activated protein kinase 1 (BMK1) is a redox-sensitive kinase
    • J. Abe, M. Kusuhara, R.J. Ulevitch, B.C. Berk and J.-D. Lee, Big mitogen-activated protein kinase 1 (BMK1) is a redox-sensitive kinase, J. Biol. Chem. 271 (1996), 16586-16590.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16586-16590
    • Abe, J.1    Kusuhara, M.2    Ulevitch, R.J.3    Berk, B.C.4    Lee, J.-D.5
  • 32
    • 0037088584 scopus 로고    scopus 로고
    • Hydrogen Peroxide Stimulates c-Src-mediated Big Mitogen-activated Protein Kinase 1 (BMK1) and the MEF2C Signaling Pathway in PC12 Cells. Potential role in cell survival following oxidative insults
    • Y. Suzaki, M. Yoshizumi, S. Kagami, A.H. Koyama, Y. Taketani, H. Houchi, K. Tsuchiya, E. Takeda and T. Tamaki, Hydrogen Peroxide Stimulates c-Src-mediated Big Mitogen-activated Protein Kinase 1 (BMK1) and the MEF2C Signaling Pathway in PC12 Cells. potential role in cell survival following oxidative insults, J. Biol. Chem. 277 (2002), 9614-9621.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9614-9621
    • Suzaki, Y.1    Yoshizumi, M.2    Kagami, S.3    Koyama, A.H.4    Taketani, Y.5    Houchi, H.6    Tsuchiya, K.7    Takeda, E.8    Tamaki, T.9
  • 33
    • 0035145860 scopus 로고    scopus 로고
    • N-acetylcysteine attenuates TNF-alpha-induced p38 MAP kinase activation and p38 MAP kinase-mediated IL-8 production by human pulmonary vascular endothelial cells
    • S. Hashimoto, Y. Gon, K. Matsumoto, I. Takeshita and T. Horie, N-acetylcysteine attenuates TNF-alpha-induced p38 MAP kinase activation and p38 MAP kinase-mediated IL-8 production by human pulmonary vascular endothelial cells, Br. J. Pharmacol. 132 (2001), 270-276.
    • (2001) Br. J. Pharmacol. , vol.132 , pp. 270-276
    • Hashimoto, S.1    Gon, Y.2    Matsumoto, K.3    Takeshita, I.4    Horie, T.5
  • 34
    • 0034654394 scopus 로고    scopus 로고
    • Involvement of lipoxygenase in lysophosphatidic acid-stimulated hydrogen peroxide release in human HaCaT keratinocytes
    • M. Sekharam, J.M. Cunnick and J. Wu, Involvement of lipoxygenase in lysophosphatidic acid-stimulated hydrogen peroxide release in human HaCaT keratinocytes, Biochem. J. 346 (2000), 751-758.
    • (2000) Biochem. J. , vol.346 , pp. 751-758
    • Sekharam, M.1    Cunnick, J.M.2    Wu, J.3
  • 35
    • 0034975973 scopus 로고    scopus 로고
    • Antioxidants inhibit JNK and p38 MAPK activation but not ERK 1/2 activation by angiotensin II in rat aortic smooth muscle cells
    • M. Kyaw, M. Yoshizumi, K. Tsuchiya, K. Kirima and T. Tamaki, Antioxidants inhibit JNK and p38 MAPK activation but not ERK 1/2 activation by angiotensin II in rat aortic smooth muscle cells, Hypertens. Res. 24 (2001), 251-261.
    • (2001) Hypertens. Res. , vol.24 , pp. 251-261
    • Kyaw, M.1    Yoshizumi, M.2    Tsuchiya, K.3    Kirima, K.4    Tamaki, T.5
  • 38
    • 0032541085 scopus 로고    scopus 로고
    • A Rac 1 effector site controlling mitogenesis through superoxide production
    • T. Joneson and D. Bar-Sagi, A Rac 1 effector site controlling mitogenesis through superoxide production, J. Biol. Chem. 273 (1998), 17991-17994.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17991-17994
    • Joneson, T.1    Bar-Sagi, D.2
  • 40
    • 0034001070 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin
    • H. Liu, H. Nishitoh, H. Ichijo and J.M. Kyriakis, Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin, Mol. Cell Biol. 20 (2000), 2198-2208.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 2198-2208
    • Liu, H.1    Nishitoh, H.2    Ichijo, H.3    Kyriakis, J.M.4
  • 43
    • 0027049804 scopus 로고
    • The mammalian ultraviolet response is triggered by activation of Src tyrosine kinases
    • Y. Devary, R.A. Gottlieb, T. Smeal and M. Karin, The mammalian ultraviolet response is triggered by activation of Src tyrosine kinases, Cell 71 (1992), 1081-1091.
    • (1992) Cell , vol.71 , pp. 1081-1091
    • Devary, Y.1    Gottlieb, R.A.2    Smeal, T.3    Karin, M.4
  • 44
    • 0030761765 scopus 로고    scopus 로고
    • c-Src is required for oxidative stress-mediated activation of big mitogen-activated protein kinase 1 (BMK1)
    • J. Abe, M. Takahashi, M. Ishida, J.D. Lee and B.C. Berk, c-Src is required for oxidative stress-mediated activation of big mitogen-activated protein kinase 1 (BMK1), J. Biol. Chem. 272 (1997), 20389-20394.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20389-20394
    • Abe, J.1    Takahashi, M.2    Ishida, M.3    Lee, J.D.4    Berk, B.C.5
  • 45
    • 0034697148 scopus 로고    scopus 로고
    • Src and Cas mediate JNK activation but not ERK1/2 and p38 kinases by reactive oxygen species
    • M. Yoshizumi, J. Abe, J. Haendeler, Q. Huang and B.C. Berk, Src and Cas mediate JNK activation but not ERK1/2 and p38 kinases by reactive oxygen species, J Biol. Chem. 275 (2000), 11706-11712.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11706-11712
    • Yoshizumi, M.1    Abe, J.2    Haendeler, J.3    Huang, Q.4    Berk, B.C.5
  • 46
    • 0033597766 scopus 로고    scopus 로고
    • Fyn and JAK2 mediate Ras activation by reactive oxygen species
    • J. Abe and B.C. Berk, Fyn and JAK2 mediate Ras activation by reactive oxygen species, J Biol. Chem. 274 (1999), 21003-21010.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21003-21010
    • Abe, J.1    Berk, B.C.2
  • 47
    • 0028982274 scopus 로고
    • p21ras as a common signaling target of reactive free radicals and cellular redox stress
    • H.M. Lander, J.S. Ogiste, K.K. Teng and A. Novofrodsky, p21ras as a common signaling target of reactive free radicals and cellular redox stress, J. Biol. Chem. 270 (1995), 21195-21198.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21195-21198
    • Lander, H.M.1    Ogiste, J.S.2    Teng, K.K.3    Novofrodsky, A.4
  • 48
    • 0031036917 scopus 로고    scopus 로고
    • An essential role for free radicals and derived species in signal transduction
    • H.M. Lander, An essential role for free radicals and derived species in signal transduction, FASEB J. 11 (1997), 118-124.
    • (1997) FASEB J. , vol.11 , pp. 118-124
    • Lander, H.M.1
  • 49
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation
    • J.M. Denu and K.G. Tanner, Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation, Biochemistry 37 (1998), 5633-5642.
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 50
    • 0034255470 scopus 로고    scopus 로고
    • Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH
    • J.R. Kim, H.W. Yoon, K.S. Kwon, S.R. Lee and S.G. Rhee, Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH, Anal Biochem. 283 (2000), 214-221.
    • (2000) Anal. Biochem. , vol.283 , pp. 214-221
    • Kim, J.R.1    Yoon, H.W.2    Kwon, K.S.3    Lee, S.R.4    Rhee, S.G.5
  • 51
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • S.R. Lee, K.S. Kwon, S.R. Kim and S.G. Rhee, Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor, J Biol. Chem. 273 (1998), 15366-15372.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15366-15372
    • Lee, S.R.1    Kwon, K.S.2    Kim, S.R.3    Rhee, S.G.4
  • 52
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases vivo
    • T.C. Meng, T. Fukada and N.K. Tonks, Reversible oxidation and inactivation of protein tyrosine phosphatases vivo, Mol. Cell 9 (2002), 387-399.
    • (2002) Mol. Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 53
    • 0035100127 scopus 로고    scopus 로고
    • Inactivation of JNK activity by mitogen-activated protein kinase phosphatase-2 in EAhy926 endothelial cells is dependent upon agonist-specific JNK translocation to the nucleus
    • C.J. Robinson, C.M. Sloss and R. Plevin, Inactivation of JNK activity by mitogen-activated protein kinase phosphatase-2 in EAhy926 endothelial cells is dependent upon agonist-specific JNK translocation to the nucleus, Cell Signal. 13 (2001), 29-41.
    • (2001) Cell Signal. , vol.13 , pp. 29-41
    • Robinson, C.J.1    Sloss, C.M.2    Plevin, R.3
  • 55
    • 0035018532 scopus 로고    scopus 로고
    • Regulation of angiotensin II-stimulated osteopontin expression in cardiac microvascular endothelial cells: Role of p42/p44 mitogen-activated protein kinase and reactive oxygen species
    • Z. Xie, D.R. Pimental, S. Lohan, A. Vasertriger, C. Pligavko, W.S. Colucci and K. Singh, Regulation of angiotensin II-stimulated osteopontin expression in cardiac microvascular endothelial cells: role of p42/p44 mitogen-activated protein kinase and reactive oxygen species, J. Cell. Physiol. 188 (2001), 132-138.
    • (2001) J. Cell. Physiol. , vol.188 , pp. 132-138
    • Xie, Z.1    Pimental, D.R.2    Lohan, S.3    Vasertriger, A.4    Pligavko, C.5    Colucci, W.S.6    Singh, K.7
  • 56
    • 0033574707 scopus 로고    scopus 로고
    • Modulation of Ras/Raf/extracellular signal-regulated kinase pathway by reactive oxygen species is involved in cyclic strain-induced early growth response-1 gene expression in endothelial cells
    • B.S. Wung, J.J. Cheng, Y.J. Chao, H.J. Hsieh and D.L. Wang, Modulation of Ras/Raf/extracellular signal-regulated kinase pathway by reactive oxygen species is involved in cyclic strain-induced early growth response-1 gene expression in endothelial cells, Circ. Res. 84 (1999), 804-812.
    • (1999) Circ. Res. , vol.84 , pp. 804-812
    • Wung, B.S.1    Cheng, J.J.2    Chao, Y.J.3    Hsieh, H.J.4    Wang, D.L.5
  • 58
    • 0033105874 scopus 로고    scopus 로고
    • NADPH oxidase: An update
    • B.M. Babior, NADPH oxidase: An update, Blood 93 (1999), 1464-1476.
    • (1999) Blood , vol.93 , pp. 1464-1476
    • Babior, B.M.1
  • 61
    • 0033563866 scopus 로고    scopus 로고
    • Activation of several MAP kinases upon stimulation of rat alveolar macrophages: Role of the NADPH oxidase
    • M. Torres and H.J. Forman, Activation of several MAP kinases upon stimulation of rat alveolar macrophages: Role of the NADPH oxidase, Arch. Biochem. Biophys. 366 (1999), 231-239.
    • (1999) Arch. Biochem. Biophys. , vol.366 , pp. 231-239
    • Torres, M.1    Forman, H.J.2
  • 62
    • 0035451856 scopus 로고    scopus 로고
    • ADP stimulates the respiratory burst without activation of ERK and AKT in rat alveolar macrophages
    • E. Gozal, H.J. Forman and M. Torres, ADP stimulates the respiratory burst without activation of ERK and AKT in rat alveolar macrophages, Free Radic. Biol. Med. 31 (2001), 679-687.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 679-687
    • Gozal, E.1    Forman, H.J.2    Torres, M.3
  • 63
    • 0036959483 scopus 로고    scopus 로고
    • Vanadate inhibition of protein tyrosine phosphatases mimics hydrogen peroxide in the activation of the ERK pathway in alveolar macrophages
    • M. Torres and H.J. Forman, Vanadate inhibition of protein tyrosine phosphatases mimics hydrogen peroxide in the activation of the ERK pathway in alveolar macrophages, Ann. NY Acad. Sci. 973 (2002), 345-348.
    • (2002) Ann. NY Acad. Sci. , vol.973 , pp. 345-348
    • Torres, M.1    Forman, H.J.2
  • 64
    • 0027364980 scopus 로고
    • Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase
    • J.R. Fabian, I.O. Daar and D.K. Morrison, Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase, Mol. Cell Biol 13 (1993), 7170-7179.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 7170-7179
    • Fabian, J.R.1    Daar, I.O.2    Morrison, D.K.3
  • 65
    • 0030029343 scopus 로고    scopus 로고
    • Ras-induced activation of Raf-1 is dependent on tyrosine phosphorylation
    • T. Jelinek, P. Dent, T.W. Sturgill and M.J. Weber, Ras-induced activation of Raf-1 is dependent on tyrosine phosphorylation, Mol. Cell Biol. 16 (1996), 1027-1034.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 1027-1034
    • Jelinek, T.1    Dent, P.2    Sturgill, T.W.3    Weber, M.J.4
  • 66
    • 0036165578 scopus 로고    scopus 로고
    • The polarization of T(h)1/T(h)2 balance is dependent on the intracellular thiol redox status of macrophages due to the distinctive cytokine production
    • Y. Murata, T. Shimamura and J. Hamuro, The polarization of T(h)1/T(h)2 balance is dependent on the intracellular thiol redox status of macrophages due to the distinctive cytokine production, Int. Immunol. 14 (2002), 201-212.
    • (2002) Int. Immunol. , vol.14 , pp. 201-212
    • Murata, Y.1    Shimamura, T.2    Hamuro, J.3
  • 67
    • 0036486712 scopus 로고    scopus 로고
    • Glutathione redox regulates lipopolysaccharide-induced IL-12 production through p38 mitogen-activated protein kinase activation in human monocytes: Role of glutathione redox in IFN-gamma priming of IL-12 production
    • M. Utsugi, K. Dobashi, Y. Koga, Y. Shimizu, T. Ishizuka, K. Iizuka, J. Hamuro, T. Nakazawa and M. Mori, Glutathione redox regulates lipopolysaccharide-induced IL-12 production through p38 mitogen-activated protein kinase activation in human monocytes: role of glutathione redox in IFN-gamma priming of IL-12 production, J. Leukoc. Biol. 71 (2002), 339-347.
    • (2002) J. Leukoc. Biol. , vol.71 , pp. 339-347
    • Utsugi, M.1    Dobashi, K.2    Koga, Y.3    Shimizu, Y.4    Ishizuka, T.5    Iizuka, K.6    Hamuro, J.7    Nakazawa, T.8    Mori, M.9
  • 68
    • 0032589882 scopus 로고    scopus 로고
    • Dependence of NF-kappaB activation and free radical generation on silica-induced TNF-alpha production in macrophages
    • Y. Rojanasakul, J. Ye, F. Chen, L. Wang, N. Cheng, V. Castranova, V. Vallyathan and X. Shi, Dependence of NF-kappaB activation and free radical generation on silica-induced TNF-alpha production in macrophages, Mol. Cell Biochem. 200 (1999), 119-125.
    • (1999) Mol. Cell Biochem. , vol.200 , pp. 119-125
    • Rojanasakul, Y.1    Ye, J.2    Chen, F.3    Wang, L.4    Cheng, N.5    Castranova, V.6    Vallyathan, V.7    Shi, X.8
  • 69
    • 0034190367 scopus 로고    scopus 로고
    • Recent advances towards understanding redox mechanisms in the activation of nuclear factor kappaB
    • Y.M. Janssen-Heininger, M.E. Poynter and P.A. Baeuerle, Recent advances towards understanding redox mechanisms in the activation of nuclear factor kappaB, Free Radic. Biol Med. 28 (2000), 1317-1327.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1317-1327
    • Janssen-Heininger, Y.M.1    Poynter, M.E.2    Baeuerle, P.A.3
  • 70
    • 0034677712 scopus 로고    scopus 로고
    • Role of Kupffer cells and oxidants in signaling peroxisome proliferator-induced hepatocyte proliferation
    • M.L. Rose, I. Rusyn, H.K. Bojes, J. Belyea, R.C. Cattley and R.G. Thurman, Role of Kupffer cells and oxidants in signaling peroxisome proliferator-induced hepatocyte proliferation, Mutat. Res. 448 (2000), 179-192.
    • (2000) Mutat. Res. , vol.448 , pp. 179-192
    • Rose, M.L.1    Rusyn, I.2    Bojes, H.K.3    Belyea, J.4    Cattley, R.C.5    Thurman, R.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.