메뉴 건너뛰기




Volumn 38, Issue 8, 2005, Pages 989-1001

Nox 2 stimulates muscle differentiation via NF-κB/iNOS pathway

Author keywords

Free radicals; iNOS; Muscle differentiation; NF B; Nitric oxide; Nox 2; p38 MAPK; PI 3 kinase; Reactive oxygen species (ROS)

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; SYNAPTOPHYSIN;

EID: 20144365876     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2004.11.011     Document Type: Article
Times cited : (74)

References (53)
  • 1
    • 0030219748 scopus 로고    scopus 로고
    • Defining the regulatory networks for muscle development
    • J.D. Molkentin, and E.N. Olson Defining the regulatory networks for muscle development Curr. Opin. Genet. 6 1996 445 453
    • (1996) Curr. Opin. Genet. , vol.6 , pp. 445-453
    • Molkentin, J.D.1    Olson, E.N.2
  • 2
    • 0032705145 scopus 로고    scopus 로고
    • MEF2: A transcriptional target for signaling pathways controlling skeletal muscle growth and differentiation
    • F.S. Naya, and E.N. Olson MEF2: a transcriptional target for signaling pathways controlling skeletal muscle growth and differentiation Curr. Opin. Cell. Biol. 11 1999 683 688
    • (1999) Curr. Opin. Cell. Biol. , vol.11 , pp. 683-688
    • Naya, F.S.1    Olson, E.N.2
  • 3
    • 0031756168 scopus 로고    scopus 로고
    • Insulin receptor substrate-1 and phosphatidylinositol 3-kinase regulate extracellular signal-regulated kinase-dependent and -independent signaling pathways during myogenic differentiation
    • D.D. Sarbassov, and C.A. Peterson Insulin receptor substrate-1 and phosphatidylinositol 3-kinase regulate extracellular signal-regulated kinase-dependent and -independent signaling pathways during myogenic differentiation Mol. Endocrinol. 12 1998 1870 1878
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1870-1878
    • Sarbassov, D.D.1    Peterson, C.A.2
  • 4
    • 0035914338 scopus 로고    scopus 로고
    • Insulin-like growth factor-mediated muscle differentiation:collaboration between phosphatidylinositol 3-kinase-Akt-signaling pathways and myogenin
    • J. Tureckova, E.M. Wilson, J.L. Cappalonga, and P. Rotwein Insulin-like growth factor-mediated muscle differentiation:collaboration between phosphatidylinositol 3-kinase-Akt-signaling pathways and myogenin J. Biol. Chem. 276 2001 39264 39270
    • (2001) J. Biol. Chem. , vol.276 , pp. 39264-39270
    • Tureckova, J.1    Wilson, E.M.2    Cappalonga, J.L.3    Rotwein, P.4
  • 5
    • 0033548233 scopus 로고    scopus 로고
    • Stress-activated protein kinase-2/p38 and a rapamycin-sensitive pathway are required for C2C12 myogenesis
    • A. Cuenda, and P. Cohen Stress-activated protein kinase-2/p38 and a rapamycin-sensitive pathway are required for C2C12 myogenesis J. Biol. Chem. 274 1999 4341 4346
    • (1999) J. Biol. Chem. , vol.274 , pp. 4341-4346
    • Cuenda, A.1    Cohen, P.2
  • 6
    • 0348110375 scopus 로고    scopus 로고
    • IGF-II transcription in skeletal myogenesis is controlled by mTOR and nutrients
    • E. Erbay, I.H. Park, P.D. Nuzzi, C.J. Schoenherr, and J. Chen IGF-II transcription in skeletal myogenesis is controlled by mTOR and nutrients J. Cell Biol. 163 2003 931 936
    • (2003) J. Cell Biol. , vol.163 , pp. 931-936
    • Erbay, E.1    Park, I.H.2    Nuzzi, P.D.3    Schoenherr, C.J.4    Chen, J.5
  • 7
    • 0030934472 scopus 로고    scopus 로고
    • The mitogenic and myogenic actions of insulin-like growth factors utilize distinct signaling pathways
    • S.A. Coolican, D.S. Samuel, D.Z. Ewton, F.J. McWade, and J.R. Florini The mitogenic and myogenic actions of insulin-like growth factors utilize distinct signaling pathways J. Biol. Chem. 272 1997 6653 6662
    • (1997) J. Biol. Chem. , vol.272 , pp. 6653-6662
    • Coolican, S.A.1    Samuel, D.S.2    Ewton, D.Z.3    McWade, F.J.4    Florini, J.R.5
  • 9
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • K.B. Beckman, and B.N. Ames The free radical theory of aging matures Physiol. Rev. 78 1998 547 581
    • (1998) Physiol. Rev. , vol.78 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 10
    • 0034653369 scopus 로고    scopus 로고
    • Reactive oxygen species and proinflammatory cytokine signaling in endothelial cells: Effect of selenium supplementation
    • R. Tolando, A. Jovanovic, R. Brigelius-Flohe, F. Ursini, and M. Maiorino Reactive oxygen species and proinflammatory cytokine signaling in endothelial cells: effect of selenium supplementation Free Radic. Biol. Med. 28 2000 979 986
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 979-986
    • Tolando, R.1    Jovanovic, A.2    Brigelius-Flohe, R.3    Ursini, F.4    Maiorino, M.5
  • 12
    • 0028973482 scopus 로고
    • Requirement for generation of H2O2 for platelet-derived growth factor signal transduction
    • M. Sundaresan, Z.X. Yu, V.J. Ferrans, K. Irani, and T. Finkel Requirement for generation of H2O2 for platelet-derived growth factor signal transduction Science 270 1995 296 299
    • (1995) Science , vol.270 , pp. 296-299
    • Sundaresan, M.1    Yu, Z.X.2    Ferrans, V.J.3    Irani, K.4    Finkel, T.5
  • 13
    • 0035877633 scopus 로고    scopus 로고
    • Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade
    • K. Mahadev, A. Zilbering, L. Zhu, and B.J. Goldstein Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade J. Biol. Chem. 276 2001 21938 21942
    • (2001) J. Biol. Chem. , vol.276 , pp. 21938-21942
    • Mahadev, K.1    Zilbering, A.2    Zhu, L.3    Goldstein, B.J.4
  • 14
    • 0034625372 scopus 로고    scopus 로고
    • Molecular mechanisms of tumor necrosis factor alpha gene expression in monocytic cells via hyperglycemia-induced oxidant stress-dependent and -independent pathways
    • M. Guha, W. Bai, J.L. Nadler, and R. Natarajan Molecular mechanisms of tumor necrosis factor alpha gene expression in monocytic cells via hyperglycemia-induced oxidant stress-dependent and -independent pathways J. Biol. Chem. 275 2000 17728 17739
    • (2000) J. Biol. Chem. , vol.275 , pp. 17728-17739
    • Guha, M.1    Bai, W.2    Nadler, J.L.3    Natarajan, R.4
  • 16
    • 0037108204 scopus 로고    scopus 로고
    • Inhibition of PTPs by H(2)O(2) regulates the activation of distinct MAPK pathways
    • K. Lee, and W.J. Esselman Inhibition of PTPs by H(2)O(2) regulates the activation of distinct MAPK pathways Free Radic. Biol. Med. 33 2002 1121 1132
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1121-1132
    • Lee, K.1    Esselman, W.J.2
  • 17
    • 0028335782 scopus 로고
    • A role for reactive oxygen species in zymosan and beta-glucan induced protein tyrosine phosphorylation and phospholipase A2 activation in murine macrophages
    • R. Goldman, E. Ferber, R. Meller, and U. Zor A role for reactive oxygen species in zymosan and beta-glucan induced protein tyrosine phosphorylation and phospholipase A2 activation in murine macrophages Biochim. Biophys. Acta 1222 1994 265 276
    • (1994) Biochim. Biophys. Acta , vol.1222 , pp. 265-276
    • Goldman, R.1    Ferber, E.2    Meller, R.3    Zor, U.4
  • 19
    • 0033572857 scopus 로고    scopus 로고
    • Direct interaction between p47phox and protein kinase C: Evidence for targeting of protein kinase C by p47phox in neutrophils
    • E.P. Reeves, L.V. Dekker, L.V. Forbes, F.B. Wientjes, A. Grogan, D.J. Pappin, and A.W. Segal Direct interaction between p47phox and protein kinase C: evidence for targeting of protein kinase C by p47phox in neutrophils Biochem. J. 344 1999 859 866
    • (1999) Biochem. J. , vol.344 , pp. 859-866
    • Reeves, E.P.1    Dekker, L.V.2    Forbes, L.V.3    Wientjes, F.B.4    Grogan, A.5    Pappin, D.J.6    Segal, A.W.7
  • 20
    • 0030588188 scopus 로고    scopus 로고
    • Activation of p38 in stimulated human neutrophils: Phosphorylation of the oxidase component p47phox by p38 and ERK but not by JNK
    • J. El Benna, J. Han, J.W. Park, E. Schmid, R.J. Ulevitch, and B.M. Babior Activation of p38 in stimulated human neutrophils: phosphorylation of the oxidase component p47phox by p38 and ERK but not by JNK Arch. Biochem. Biophys. 334 1996 395 400
    • (1996) Arch. Biochem. Biophys. , vol.334 , pp. 395-400
    • El Benna, J.1    Han, J.2    Park, J.W.3    Schmid, E.4    Ulevitch, R.J.5    Babior, B.M.6
  • 21
    • 0001288948 scopus 로고    scopus 로고
    • Platelet-derived growth factor-induced H(2)O(2) production requires the activation of phosphatidylinositol 3-kinase
    • Y.S. Bae, J.Y. Sung, O.S. Kim, Y.J. Kim, K.C. Hur, A. Kazlauskas, and S.G. Rhee Platelet-derived growth factor-induced H(2)O(2) production requires the activation of phosphatidylinositol 3-kinase J. Biol. Chem. 275 2000 10527 10531
    • (2000) J. Biol. Chem. , vol.275 , pp. 10527-10531
    • Bae, Y.S.1    Sung, J.Y.2    Kim, O.S.3    Kim, Y.J.4    Hur, K.C.5    Kazlauskas, A.6    Rhee, S.G.7
  • 24
    • 0036076064 scopus 로고    scopus 로고
    • Relationship between p38 mitogen-activated protein kinase and small GTPase Rac for the activation of NADPH oxidase in bovine neutrophils
    • T. Yamamori, O. Inanami, H. Sumimoto, T. Akasaki, H. Nagahata, and M. Kuwabara Relationship between p38 mitogen-activated protein kinase and small GTPase Rac for the activation of NADPH oxidase in bovine neutrophils Biochem. Biophys. Res. Commun. 293 2002 1571 1578
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 1571-1578
    • Yamamori, T.1    Inanami, O.2    Sumimoto, H.3    Akasaki, T.4    Nagahata, H.5    Kuwabara, M.6
  • 25
    • 0036778387 scopus 로고    scopus 로고
    • Cyclosporine blocks muscle differention by inducing oxidative stress and by inhibiting the peptidylprolyl-cis-trans-isomerase activity of cyclophilin A: CyclophilinA protects myoblasts from cyclosporine-induced cytotoxicity
    • F. Hong, J. Lee, J.W. Song, S.J. Lee, H. Ahn, J.J. Cho, J. Ha, and S.S. Kim Cyclosporine blocks muscle differention by inducing oxidative stress and by inhibiting the peptidylprolyl-cis-trans-isomerase activity of cyclophilin A: cyclophilinA protects myoblasts from cyclosporine-induced cytotoxicity FASEB J. 16 2002 1633 1635
    • (2002) FASEB J. , vol.16 , pp. 1633-1635
    • Hong, F.1    Lee, J.2    Song, J.W.3    Lee, S.J.4    Ahn, H.5    Cho, J.J.6    Ha, J.7    Kim, S.S.8
  • 27
    • 1942518724 scopus 로고    scopus 로고
    • Akt2, a novel functional link between p38 mitogen-activated protein kinase and phosphatidylinositol 3-kinase pathways in myogenesis
    • I. Gonzalez, G. Tripathi, E.J. Carte, L.J. Cobb, D.A. Salih, F.A. Lovett, C. Holding, and J.M. Pell Akt2, a novel functional link between p38 mitogen-activated protein kinase and phosphatidylinositol 3-kinase pathways in myogenesis Mol. Cell. Biol. 24 2004 3607 3622
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 3607-3622
    • Gonzalez, I.1    Tripathi, G.2    Carte, E.J.3    Cobb, L.J.4    Salih, D.A.5    Lovett, F.A.6    Holding, C.7    Pell, J.M.8
  • 28
    • 0030988745 scopus 로고    scopus 로고
    • NF-kappaB-dependent expression of nitric oxide synthase is required for membrane fusion of chick embryonic myoblasts
    • K.H. Lee, D.G. Kim, N.Y. Shin, W.K. Song, H. Kwon, C.H. Chung, and M.S. Kang NF-kappaB-dependent expression of nitric oxide synthase is required for membrane fusion of chick embryonic myoblasts Biochem. J. 324 1997 237 242
    • (1997) Biochem. J. , vol.324 , pp. 237-242
    • Lee, K.H.1    Kim, D.G.2    Shin, N.Y.3    Song, W.K.4    Kwon, H.5    Chung, C.H.6    Kang, M.S.7
  • 29
    • 0033580826 scopus 로고    scopus 로고
    • Insulin-like growth factor-II, phosphatidylinositol 3-kinase, nuclear factor-kappaB and inducible nitric-oxide synthase define a common myogenic signaling pathway
    • P. Kaliman, J. Canicio, X. Testar, M. Palacin, and A. Zorzano Insulin-like growth factor-II, phosphatidylinositol 3-kinase, nuclear factor-kappaB and inducible nitric-oxide synthase define a common myogenic signaling pathway J. Biol. Chem. 274 1999 17437 17444
    • (1999) J. Biol. Chem. , vol.274 , pp. 17437-17444
    • Kaliman, P.1    Canicio, J.2    Testar, X.3    Palacin, M.4    Zorzano, A.5
  • 30
    • 0028978032 scopus 로고
    • Phosphorylation of human I kappa B-alpha on serines 32 and 36 controls I kappa B-alpha proteolysis and NF-kappa B activation in response to diverse stimuli
    • E.B. Traenckner, H.L. Pahl, T. Henkel, K.N. Schmidt, S. Wilk, and P.A. Baeuerle Phosphorylation of human I kappa B-alpha on serines 32 and 36 controls I kappa B-alpha proteolysis and NF-kappa B activation in response to diverse stimuli EMBO J. 14 1995 2876 2883
    • (1995) EMBO J. , vol.14 , pp. 2876-2883
    • Traenckner, E.B.1    Pahl, H.L.2    Henkel, T.3    Schmidt, K.N.4    Wilk, S.5    Baeuerle, P.A.6
  • 31
    • 0025365223 scopus 로고
    • Stimulation by hydrogen peroxide of DNA synthesis, competence family gene expression and phosphorylation of a specific protein in quiescent Balb/3T3 cells
    • M. Shibanuma, T. Kuroki, and K. Nose Stimulation by hydrogen peroxide of DNA synthesis, competence family gene expression and phosphorylation of a specific protein in quiescent Balb/3T3 cells Oncogene 5 1990 1025 1032
    • (1990) Oncogene , vol.5 , pp. 1025-1032
    • Shibanuma, M.1    Kuroki, T.2    Nose, K.3
  • 32
    • 0347318117 scopus 로고    scopus 로고
    • Source of early reactive oxygen species in the apoptosis induced by transforming growth factor-beta in fetal rat hepatocytes
    • B. Herrera, M.M. Murillo, A. Alvarez-Barrientos, J. Beltran, M. Fernandez, and I. Fabregat Source of early reactive oxygen species in the apoptosis induced by transforming growth factor-beta in fetal rat hepatocytes Free Radic. Biol. Med. 36 2004 16 26
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 16-26
    • Herrera, B.1    Murillo, M.M.2    Alvarez-Barrientos, A.3    Beltran, J.4    Fernandez, M.5    Fabregat, I.6
  • 33
    • 0035897653 scopus 로고    scopus 로고
    • Homologs of gp91phox: Cloning and tissue expression of Nox3, Nox4, and Nox5
    • G. Cheng, Z. Cao, X. Xu, E.G. van Meir, and J.D. Lambeth Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5 Gene 269 2001 131 140
    • (2001) Gene , vol.269 , pp. 131-140
    • Cheng, G.1    Cao, Z.2    Xu, X.3    Van Meir, E.G.4    Lambeth, J.D.5
  • 35
    • 0034617467 scopus 로고    scopus 로고
    • Role of reactive oxygen species and phosphatidylinositol 3-kinase in cardiomyocyte differentiation of embryonic stem cells
    • H. Sauer, G. Rahimi, J. Hescheler, and M. Wartenberg Role of reactive oxygen species and phosphatidylinositol 3-kinase in cardiomyocyte differentiation of embryonic stem cells FEBS Lett. 476 2000 218 223
    • (2000) FEBS Lett. , vol.476 , pp. 218-223
    • Sauer, H.1    Rahimi, G.2    Hescheler, J.3    Wartenberg, M.4
  • 37
    • 0034607872 scopus 로고    scopus 로고
    • Nerve growth factor-induced neuronal differentiation requires generation of Rac1-regulated reactive oxygen species
    • K. Suzukawa, K. Miura, J. Mitsushita, J. Resau, K. Hirose, R. Crystal, and T. Kamata Nerve growth factor-induced neuronal differentiation requires generation of Rac1-regulated reactive oxygen species J. Biol. Chem. 275 2000 13175 13178
    • (2000) J. Biol. Chem. , vol.275 , pp. 13175-13178
    • Suzukawa, K.1    Miura, K.2    Mitsushita, J.3    Resau, J.4    Hirose, K.5    Crystal, R.6    Kamata, T.7
  • 38
    • 0035020963 scopus 로고    scopus 로고
    • Inflammatory cytokines inhibit myogenic differentiation through activation of nuclear factor-kappaB
    • R.C. Langen, A.M. Schols, M.C. Kelders, E.F. Wouters, and Y.M. Janssen-Heininger Inflammatory cytokines inhibit myogenic differentiation through activation of nuclear factor-kappaB FASEB J. 15 2001 1169 1180
    • (2001) FASEB J. , vol.15 , pp. 1169-1180
    • Langen, R.C.1    Schols, A.M.2    Kelders, M.C.3    Wouters, E.F.4    Janssen-Heininger, Y.M.5
  • 39
    • 0029921173 scopus 로고    scopus 로고
    • Muscle wasting and dedifferentiation induced by oxidative stress in a murine model of cachexia is prevented by inhibitors of nitric oxide synthesis and antioxidants
    • M. Buck, and M. Chojkier Muscle wasting and dedifferentiation induced by oxidative stress in a murine model of cachexia is prevented by inhibitors of nitric oxide synthesis and antioxidants EMBO J. 15 1996 1753 1765
    • (1996) EMBO J. , vol.15 , pp. 1753-1765
    • Buck, M.1    Chojkier, M.2
  • 40
    • 0031802331 scopus 로고    scopus 로고
    • Skeletal muscle myocytes undergo protein loss and reactive oxygen-mediated NF-kappaB activation in response to tumor necrosis factor alpha
    • Y.P. Li, R.J. Schwartz, I.D. Waddell, B.R. Holloway, and M.B. Reid Skeletal muscle myocytes undergo protein loss and reactive oxygen-mediated NF-kappaB activation in response to tumor necrosis factor alpha FASEB J. 12 1998 871 880
    • (1998) FASEB J. , vol.12 , pp. 871-880
    • Li, Y.P.1    Schwartz, R.J.2    Waddell, I.D.3    Holloway, B.R.4    Reid, M.B.5
  • 41
    • 0036260697 scopus 로고    scopus 로고
    • Cellular response to oxidative stress: Signaling for suicide and survival
    • J.L. Martindale, and N.J. Holbrook Cellular response to oxidative stress: signaling for suicide and survival J. Cell. Physiol. 192 2002 1 15
    • (2002) J. Cell. Physiol. , vol.192 , pp. 1-15
    • Martindale, J.L.1    Holbrook, N.J.2
  • 43
    • 1642423481 scopus 로고    scopus 로고
    • P38 MAPK-induced NF-{kappa}B activity is required for skeletal muscle differentiation: Role of IL-6
    • B. Baeza-Raja, and P. Munoz-Canoves p38 MAPK-induced NF-{kappa}B activity is required for skeletal muscle differentiation: role of IL-6 Mol. Biol. Cell. 15 2004 2013 2026
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 2013-2026
    • Baeza-Raja, B.1    Munoz-Canoves, P.2
  • 44
    • 0035914388 scopus 로고    scopus 로고
    • Akt1/PKBalpha is required for normal growth but dispensable for maintenance of glucose homeostasis in mice
    • H. Cho, J.L. Thorvaldsen, Q. Chu, F. Feng, and M.J. Birnbaum Akt1/PKBalpha is required for normal growth but dispensable for maintenance of glucose homeostasis in mice J. Biol. Chem. 276 2001 38349 38352
    • (2001) J. Biol. Chem. , vol.276 , pp. 38349-38352
    • Cho, H.1    Thorvaldsen, J.L.2    Chu, Q.3    Feng, F.4    Birnbaum, M.J.5
  • 48
    • 0028984840 scopus 로고
    • The p47phox mouse knock-out model of chronic granulomatous disease
    • S.H. Jackson, J.I. Gallin, and S.M. Holland The p47phox mouse knock-out model of chronic granulomatous disease J. Exp. Med. 182 1995 751 758
    • (1995) J. Exp. Med. , vol.182 , pp. 751-758
    • Jackson, S.H.1    Gallin, J.I.2    Holland, S.M.3
  • 49
    • 0028804551 scopus 로고
    • Targeted disruption of the p50 subunit of NF-kappa B leads to multifocal defects in immune responses
    • W.C. Sha, H.C. Liou, E.I. Tuomanen, and D. Baltimore Targeted disruption of the p50 subunit of NF-kappa B leads to multifocal defects in immune responses Cell 80 1995 321 330
    • (1995) Cell , vol.80 , pp. 321-330
    • Sha, W.C.1    Liou, H.C.2    Tuomanen, E.I.3    Baltimore, D.4
  • 51
    • 0029059060 scopus 로고
    • Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-kappa B
    • A.A. Beg, W.C. Sha, R.T. Bronson, S. Ghosh, and D. Baltimore Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-kappa B Nature 376 1995 167 170
    • (1995) Nature , vol.376 , pp. 167-170
    • Beg, A.A.1    Sha, W.C.2    Bronson, R.T.3    Ghosh, S.4    Baltimore, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.