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Volumn 20, Issue 2, 2005, Pages 280-287

Insulin cannot activate extracellular-signal-related kinase due to inability to generate reactive oxygen species in SK-N-BE(2) human neuroblastoma cells

Author keywords

Grb2; Insulin; IRS 1; MAPK ERK; Reactive Oxygen Species

Indexed keywords

ACETYLCYSTEINE; HYDROGEN PEROXIDE; INSULIN; INSULIN RECEPTOR; INSULIN RECEPTOR SUBSTRATE 1; MITOGEN ACTIVATED PROTEIN KINASE; PERVANADATE; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; PROTEIN GRB2; RAC1 PROTEIN; RAS PROTEIN; REACTIVE OXYGEN METABOLITE; TYROSINE; WORTMANNIN;

EID: 33645224486     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (8)

References (46)
  • 1
    • 0027416751 scopus 로고
    • Association of IRS-1 with the insulin receptor and the phosphatidylinositol 3′-kinase. Formation of binary and ternary signaling complexes in intact cells
    • Backer, J. M., Myers, M. G. Jr., Sun, X. J., Chin, D. J., Shoelson, S. E., et al. (1993) Association of IRS-1 with the insulin receptor and the phosphatidylinositol 3′-kinase. Formation of binary and ternary signaling complexes in intact cells. J. Biol. Chem. 268, 8204-8212.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8204-8212
    • Backer, J.M.1    Myers Jr., M.G.2    Sun, X.J.3    Chin, D.J.4    Shoelson, S.E.5
  • 2
    • 15144343374 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation
    • Bae, Y. S., Kang, S. W., Seo, M. S., Baines, I. C., Tekle, E., et al. (1997) Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation. J. Biol. Chem. 272, 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
  • 4
    • 0027292553 scopus 로고
    • Binding of the Ras activator son of sevenless to insulin receptor substrate-1 signaling complexes
    • Baltensperger, K., Kozma, L. M., Cherniack, A. D., Klarlund, J. K., Chawla, A., et al. (1993) Binding of the Ras activator son of sevenless to insulin receptor substrate-1 signaling complexes. Science 260, 1950-1952.
    • (1993) Science , vol.260 , pp. 1950-1952
    • Baltensperger, K.1    Kozma, L.M.2    Cherniack, A.D.3    Klarlund, J.K.4    Chawla, A.5
  • 5
    • 0038789165 scopus 로고    scopus 로고
    • Two novel proteins activate superoxide generation by the NADPH oxidase NOX1
    • Banfi, B., Clark, R. A., Steger, K., and Krause, K. (2003) Two novel proteins activate superoxide generation by the NADPH oxidase NOX1. J. Biol. Chem. 278, 3510-3513.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3510-3513
    • Banfi, B.1    Clark, R.A.2    Steger, K.3    Krause, K.4
  • 6
    • 0033105874 scopus 로고    scopus 로고
    • NADPH oxidase: An update
    • Barbior, B. M. (1999) NADPH oxidase: an update. Blood 93, 1464-1476.
    • (1999) Blood , vol.93 , pp. 1464-1476
    • Barbior, B.M.1
  • 7
    • 0029860951 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 720 in the platelet-derived growth factor alpha receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation
    • Bazenet, C. E., Gelderloos, J. A., and Kazlauskas, A. (1996) Phosphorylation of tyrosine 720 in the platelet-derived growth factor alpha receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation. Mol. Cell. Biol. 16, 6926-6936.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6926-6936
    • Bazenet, C.E.1    Gelderloos, J.A.2    Kazlauskas, A.3
  • 8
    • 0018121341 scopus 로고
    • Multiple neurotransmitter synthesis by human neuroblastoma cell lines and clones
    • Biedler, J. L., Rofflrt-Tarlov, S., Schachner, M., and Freedman, M. S. (1978) Multiple neurotransmitter synthesis by human neuroblastoma cell lines and clones. Cancer Res. 38, 3751-3757.
    • (1978) Cancer Res. , vol.38 , pp. 3751-3757
    • Biedler, J.L.1    Rofflrt-Tarlov, S.2    Schachner, M.3    Freedman, M.S.4
  • 9
    • 0037108109 scopus 로고    scopus 로고
    • Current molecular models for NADPH oxidase regulation by Rac GTPase
    • Bokoch, G. M. and Diebold, B. A. (2002) Current molecular models for NADPH oxidase regulation by Rac GTPase. Blood 100, 2692-2696.
    • (2002) Blood , vol.100 , pp. 2692-2696
    • Bokoch, G.M.1    Diebold, B.A.2
  • 10
    • 0027153103 scopus 로고
    • Epidermal growth factor regulates p21 ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor
    • Buday, L. and Downward, J. (1993) Epidermal growth factor regulates p21 ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor. Cell 73, 611-620.
    • (1993) Cell , vol.73 , pp. 611-620
    • Buday, L.1    Downward, J.2
  • 11
    • 0028918334 scopus 로고
    • Superoxide and hydrogen peroxide in relation to mammalian cell proliferation
    • Burdon, R. H. (1995) Superoxide and hydrogen peroxide in relation to mammalian cell proliferation. Free Radic. Biol. Med. 18, 775-794.
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 775-794
    • Burdon, R.H.1
  • 12
    • 0033598677 scopus 로고    scopus 로고
    • Protein-sulfenic acids: Diverse roles for an unlikely player in enzyme catalysis and redox regulation
    • Claiborne, A., Yeh, J. I., Mallett, T. C., Luba, J., Crane, E. J. 3rd, et al. (1999) Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry 38, 15407-15416.
    • (1999) Biochemistry , vol.38 , pp. 15407-15416
    • Claiborne, A.1    Yeh, J.I.2    Mallett, T.C.3    Luba, J.4    Crane III, E.J.5
  • 14
    • 0030890944 scopus 로고    scopus 로고
    • Rapid suppression of free radical formation by nerve growth factor involves the mitogen-activated protein kinase pathway
    • Dugan, L. L., Creedon, D. J., Johnson, E. M., and Holtzman, D. M. (1997) Rapid suppression of free radical formation by nerve growth factor involves the mitogen-activated protein kinase pathway. Proc. Natl. Acad. Sci. USA 94, 4086-4091.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4086-4091
    • Dugan, L.L.1    Creedon, D.J.2    Johnson, E.M.3    Holtzman, D.M.4
  • 16
    • 0032053707 scopus 로고    scopus 로고
    • Oxygen radicals and signaling
    • Finkel, T. (1998) Oxygen radicals and signaling. Curr. Opin. Cell Biol. 10, 248-253.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 248-253
    • Finkel, T.1
  • 17
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin, C. H. (1995) Dimerization of cell surface receptors in signal transduction. Cell 80, 213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 18
    • 0344462719 scopus 로고    scopus 로고
    • Redox regulation of signal transduction in mammalian cells
    • Herrlich, P. and Bohmer, F. D. (2000) Redox regulation of signal transduction in mammalian cells. Biochem. Pharmacol. 59, 35-41.
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 35-41
    • Herrlich, P.1    Bohmer, F.D.2
  • 19
    • 0034614490 scopus 로고    scopus 로고
    • Signaling-2000 and beyond
    • Hunter, T. (2000) Signaling-2000 and beyond. Cell 100, 113-127.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 20
    • 11144264993 scopus 로고
    • Effect of nerve growth factor, insulin, and extracellular matrix proteins on the neurite outgrowth of SK-N-BE(2) human neuroblastoma cells
    • Hwang, J. J., Lim, J. H., Kwon, J. H., Lee, K. Y., and Hur, K. C. (1995) Effect of nerve growth factor, insulin, and extracellular matrix proteins on the neurite outgrowth of SK-N-BE(2) human neuroblastoma cells. Mol. Cells 5, 501-507.
    • (1995) Mol. Cells , vol.5 , pp. 501-507
    • Hwang, J.J.1    Lim, J.H.2    Kwon, J.H.3    Lee, K.Y.4    Hur, K.C.5
  • 21
    • 16044365828 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of I kappa B-alpha activates NF-kappa B without proteolytic degradation of I kappa B-alpha
    • Imbert, V., Rupec, R. A., Livolsi, A., Pahl, H. L., Traenckner, E. B., et al. (1996) Tyrosine phosphorylation of I kappa B-alpha activates NF-kappa B without proteolytic degradation of I kappa B-alpha. Cell 86, 787-798.
    • (1996) Cell , vol.86 , pp. 787-798
    • Imbert, V.1    Rupec, R.A.2    Livolsi, A.3    Pahl, H.L.4    Traenckner, E.B.5
  • 22
    • 0028031527 scopus 로고
    • The mitogen-activated protein kinase cascade is activated by B-Raf in response to nerve growth factor through interaction with p21ras
    • Jaiswal, R. K., Moodie, S. A., Wolfman, A., and Landreth, G. E. (1994) The mitogen-activated protein kinase cascade is activated by B-Raf in response to nerve growth factor through interaction with p21ras. Mol. Cell. Biol. 14, 6944-6953.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6944-6953
    • Jaiswal, R.K.1    Moodie, S.A.2    Wolfman, A.3    Landreth, G.E.4
  • 23
    • 0028851241 scopus 로고
    • 2+ signaling followed by phospholipase-A2 activation and potentiated by an adenosine derivative
    • 2+ signaling followed by phospholipase-A2 activation and potentiated by an adenosine derivative. Endocrinology 136, 116-123.
    • (1995) Endocrinology , vol.136 , pp. 116-123
    • Kimura, T.1    Okajima, F.2    Sho, K.3    Kobayashi, I.4    Kondo, Y.5
  • 25
    • 0030894971 scopus 로고    scopus 로고
    • 2 generation in human adipocyte plasma membranes is mediated by Galphai2
    • 2 generation in human adipocyte plasma membranes is mediated by Galphai2. J. Biol. Chem. 272, 10135-10143.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10135-10143
    • Krieger-Brauer, H.I.1    Medda, P.K.2    Kather, H.3
  • 26
    • 0027158159 scopus 로고
    • The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp
    • Kuhne, M. R., Pawson, T., Lienhard, G. E., and Feng, G. S. (1993) The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp. J. Biol. Chem. 268, 11479-11481.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11479-11481
    • Kuhne, M.R.1    Pawson, T.2    Lienhard, G.E.3    Feng, G.S.4
  • 27
    • 0025172811 scopus 로고
    • Association between the PDGF receptor and members of the src family of tyrosine kinases
    • Kypta, R. M., Goldberg, Y., Ulug, E. T., and Courtneidge, S. A. (1990) Association between the PDGF receptor and members of the src family of tyrosine kinases. Cell 62, 481-492.
    • (1990) Cell , vol.62 , pp. 481-492
    • Kypta, R.M.1    Goldberg, Y.2    Ulug, E.T.3    Courtneidge, S.A.4
  • 28
    • 0028272507 scopus 로고
    • Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
    • Leevers, S. J., Paterson, H. F., and Marshall, C. J. (1994) Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane. Nature 369, 411-414.
    • (1994) Nature , vol.369 , pp. 411-414
    • Leevers, S.J.1    Paterson, H.F.2    Marshall, C.J.3
  • 29
    • 0027312272 scopus 로고
    • Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling
    • Li, N., Batzer, A., Daly, R., Yajnik, V., Skolnik, E., et al. (1993) Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling. Nature 363, 85-88.
    • (1993) Nature , vol.363 , pp. 85-88
    • Li, N.1    Batzer, A.2    Daly, R.3    Yajnik, V.4    Skolnik, E.5
  • 30
    • 0029020218 scopus 로고
    • Involvement of reactive oxygen species in cytokine and growth factor induction of c-fos expression in chondrocytes
    • Lo, Y. Y. and Cruz, T. F. (1995) Involvement of reactive oxygen species in cytokine and growth factor induction of c-fos expression in chondrocytes. J. Biol. Chem. 270, 11727-11730.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11727-11730
    • Lo, Y.Y.1    Cruz, T.F.2
  • 31
    • 0027370827 scopus 로고
    • Reconstitution of the Raf-1-MEK-ERK signal transduction pathway in vitro
    • Macdonald, S. G., Crews, C. M., Wu, L., Driller, J., Clark, R., et al. (1993) Reconstitution of the Raf-1-MEK-ERK signal transduction pathway in vitro. Mol. Cell. Biol. 13, 6615-6620.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6615-6620
    • Macdonald, S.G.1    Crews, C.M.2    Wu, L.3    Driller, J.4    Clark, R.5
  • 32
    • 0035877633 scopus 로고    scopus 로고
    • Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade
    • Mahadev, K., Zilbering, A., Zhu, L., and Goldstein, B. J. (2001a) Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade. J. Biol. Chem. 276, 21938-21942.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21938-21942
    • Mahadev, K.1    Zilbering, A.2    Zhu, L.3    Goldstein, B.J.4
  • 33
    • 0035966052 scopus 로고    scopus 로고
    • Hydrogen peroxide generated during cellular insulin stimulation is integral to activation of the distal insulin signaling cascade in 3T3-L1 adipocytes
    • Mahadev, K., Wu, X., Zilbering, A., Zhu, L., Lawrence, J. T., et al. (2001b) Hydrogen peroxide generated during cellular insulin stimulation is integral to activation of the distal insulin signaling cascade in 3T3-L1 adipocytes. J. Biol. Chem. 276, 48662-48669.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48662-48669
    • Mahadev, K.1    Wu, X.2    Zilbering, A.3    Zhu, L.4    Lawrence, J.T.5
  • 34
    • 0025904386 scopus 로고
    • Identification of a superoxide generating NADPH-oxidase system in human fibroblasts
    • Meier, B., Cross, A. R., Hancock, J. T., Kamp, F., and Jones, O. T. G. (1991) Identification of a superoxide generating NADPH-oxidase system in human fibroblasts. Biochem. J. 275, 241-245.
    • (1991) Biochem. J. , vol.275 , pp. 241-245
    • Meier, B.1    Cross, A.R.2    Hancock, J.T.3    Kamp, F.4    Jones, O.T.G.5
  • 35
    • 0028015832 scopus 로고
    • Production of hydrogen peroxide by transforming growth factor-beta 1 and its involvement in induction of egr-1 in mouse osteoblastic cells
    • Ohba, M., Shibanuma, M., Kuroki, T., and Nose, K. (1994) Production of hydrogen peroxide by transforming growth factor-beta 1 and its involvement in induction of egr-1 in mouse osteoblastic cells. J. Cell Biol. 126, 1079-1088.
    • (1994) J. Cell Biol. , vol.126 , pp. 1079-1088
    • Ohba, M.1    Shibanuma, M.2    Kuroki, T.3    Nose, K.4
  • 37
    • 0027294981 scopus 로고
    • The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1
    • Rozakis-Adcock, M., Fernley, R., Wade, J., Pawson, T., and Bowtell, D. (1993) The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1. Nature 363, 83-85.
    • (1993) Nature , vol.363 , pp. 83-85
    • Rozakis-Adcock, M.1    Fernley, R.2    Wade, J.3    Pawson, T.4    Bowtell, D.5
  • 38
    • 0033135256 scopus 로고    scopus 로고
    • Hematopoietic growth factors signal through the formation of reactive oxygen species
    • Sattler, M., Winkler, T., Verma, S., Byrne, C. H., Shrikhande, G., et al. (1999) Hematopoietic growth factors signal through the formation of reactive oxygen species. Blood 93, 2928-2935.
    • (1999) Blood , vol.93 , pp. 2928-2935
    • Sattler, M.1    Winkler, T.2    Verma, S.3    Byrne, C.H.4    Shrikhande, G.5
  • 39
    • 11144279346 scopus 로고    scopus 로고
    • The major target of the endogenously generated reactive oxygen species in response to insulin stimulation is phosphatase and tensin homolog and not phosphoinositide-3 kinase (PI-3 kinase) in the PI-3 kinase/Akt pathway
    • Seo, J. H., Ahn, Y., Lee, S., Yeo, C. Y., and Hur, K. C. (2005) The major target of the endogenously generated reactive oxygen species in response to insulin stimulation is phosphatase and tensin homolog and not phosphoinositide-3 kinase (PI-3 kinase) in the PI-3 kinase/Akt pathway. Mol. Biol. Cell 16, 348-357.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 348-357
    • Seo, J.H.1    Ahn, Y.2    Lee, S.3    Yeo, C.Y.4    Hur, K.C.5
  • 40
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopeptide sequences
    • Songyang, Z., Shoelson, S. E., Chaudhuri, M., Gish, G., Pawson, T., et al. (1993) SH2 domains recognize specific phosphopeptide sequences. Cell 72, 767-778.
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1    Shoelson, S.E.2    Chaudhuri, M.3    Gish, G.4    Pawson, T.5
  • 42
    • 0029831907 scopus 로고    scopus 로고
    • Regulation of reactive-oxygen-species generation in fibroblasts by Rac1
    • Sundaresan, M., Yu, Z. X., Ferrans, V. J., Sulciner, D. J., Gutkind, J. S., et al. (1996) Regulation of reactive-oxygen-species generation in fibroblasts by Rac1. Biochem. J. 318, 379-382.
    • (1996) Biochem. J. , vol.318 , pp. 379-382
    • Sundaresan, M.1    Yu, Z.X.2    Ferrans, V.J.3    Sulciner, D.J.4    Gutkind, J.S.5
  • 43
    • 0026021362 scopus 로고
    • Production of large amounts of hydrogen peroxide by human tumor cells
    • Szatrowski, T. P. and Nathan, C. F. (1991) Production of large amounts of hydrogen peroxide by human tumor cells. Cancer Res. 51, 794-798.
    • (1991) Cancer Res. , vol.51 , pp. 794-798
    • Szatrowski, T.P.1    Nathan, C.F.2
  • 44
    • 0031918624 scopus 로고    scopus 로고
    • The IRS-signalling system: A network of docking proteins that mediate insulin action
    • White, M. F. (1998) The IRS-signalling system: a network of docking proteins that mediate insulin action. Mol. Cell. Biochem. 182, 3-11.
    • (1998) Mol. Cell. Biochem. , vol.182 , pp. 3-11
    • White, M.F.1
  • 45
    • 0028085078 scopus 로고
    • The insulin signaling system
    • White, M. F. and Kahn, C. R. (1994) The insulin signaling system. J. Biol. Chem. 269, 1-4.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1-4
    • White, M.F.1    Kahn, C.R.2
  • 46
    • 0031893253 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases: Biological function, structural characteristics, and mechanism of catalysis
    • Zhang, Z. Y. (1998) Protein-tyrosine phosphatases: biological function, structural characteristics, and mechanism of catalysis. Crit. Rev. Biochem. Mol. Biol. 33, 1-52.
    • (1998) Crit. Rev. Biochem. Mol. Biol. , vol.33 , pp. 1-52
    • Zhang, Z.Y.1


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