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Volumn 16, Issue 1, 2005, Pages 73-83

Insulin inhibits platelet-derived growth factor-induced cell proliferation

Author keywords

[No Author keywords available]

Indexed keywords

GROWTH FACTOR; HYDROGEN PEROXIDE; INSULIN; MITOGENIC AGENT; PLATELET DERIVED GROWTH FACTOR; PLATELET DERIVED GROWTH FACTOR RECEPTOR; PROTEIN TYROSINE PHOSPHATASE; REACTIVE OXYGEN METABOLITE;

EID: 19944407085     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E04-01-0011     Document Type: Article
Times cited : (17)

References (40)
  • 1
    • 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., Chock, P. B., and Rhee, S. G. (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    Chock, P.B.6    Rhee, S.G.7
  • 2
    • 0001288948 scopus 로고    scopus 로고
    • Platelet-derived growth factor-induced H(2)O(2) production requires the activation of phosphatidylinositol 3-kinase
    • Bae, Y. S., Sung, J. Y., Kim, O. S., Kim, Y. J., Hur, K. C., Kazlauskas, A., and Rhee, S. G. (2000). Platelet-derived growth factor-induced H(2)O(2) production requires the activation of phosphatidylinositol 3-kinase. J. Biol. Chem. 275, 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
  • 3
    • 0028856550 scopus 로고
    • An in-gel assay for protein tyrosine phosphatase activity: Detection of widespread distribution in cells and tissue
    • Burridge, K. and Nelson, A. (1995). An in-gel assay for protein tyrosine phosphatase activity: detection of widespread distribution in cells and tissue. Anal. Biochem. 232, 56-64.
    • (1995) Anal. Biochem. , vol.232 , pp. 56-64
    • Burridge, K.1    Nelson, A.2
  • 4
    • 0031806620 scopus 로고    scopus 로고
    • Inhibition of clathrin-mediated endocytosis selectively attenuates specific insulin receptor signal transduction pathways
    • Ceresa, B. P., Kao, A. W., Santeler, S. R., and Pessin, J. E. (1998). Inhibition of clathrin-mediated endocytosis selectively attenuates specific insulin receptor signal transduction pathways. Mol. Cell Biol. 18, 3862-3870.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 3862-3870
    • Ceresa, B.P.1    Kao, A.W.2    Santeler, S.R.3    Pessin, J.E.4
  • 6
    • 0029090238 scopus 로고
    • Platelet-derived growth factor receptor as a specific in vivo target for low M(r) phosphotyrosine protein phosphatase
    • Chiarugi, P., Cirri, P., Raugei, G., Camici, G., Dolfi, F., Berti, A., and Ramponi, G. (1995). platelet-derived growth factor receptor as a specific in vivo target for low M(r) phosphotyrosine protein phosphatase. FEBS Lett. 372, 49-53.
    • (1995) FEBS Lett. , vol.372 , pp. 49-53
    • Chiarugi, P.1    Cirri, P.2    Raugei, G.3    Camici, G.4    Dolfi, F.5    Berti, A.6    Ramponi, G.7
  • 7
    • 0037092501 scopus 로고    scopus 로고
    • New perspectives in platelet-derived growth factor receptor downregulation: The main role of phosphotyrosine phosphatases
    • Giannoni, E., Camici, G., Raugei, G., and Ramponi, G. (2002). New perspectives in platelet-derived growth factor receptor downregulation: the main role of phosphotyrosine phosphatases. J. Cell Sci. 115, 2219-2232.
    • (2002) J. Cell Sci. , vol.115 , pp. 2219-2232
    • Giannoni, E.1    Camici, G.2    Raugei, G.3    Ramponi, G.4
  • 8
    • 0035823539 scopus 로고    scopus 로고
    • Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation
    • Chiarugi, P., Fiaschi, T., Taddei, M. L., Talini, D., Giannoni, E., Raugei, G., and Ramponi, G. (2001). Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation. J. Biol. Chem. 276, 33478-33487.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33478-33487
    • Chiarugi, P.1    Fiaschi, T.2    Taddei, M.L.3    Talini, D.4    Giannoni, E.5    Raugei, G.6    Ramponi, G.7
  • 9
    • 0025741580 scopus 로고
    • A mutational analysis of phosphatidylinositol-3-kinase activation by human colony-stimulating factor-1 receptor
    • Choudhury, G. G., Wang, L. M., Pierce, J., Harvey, S. A., and Sakaguchi, A. Y. (1991). A mutational analysis of phosphatidylinositol-3-kinase activation by human colony-stimulating factor-1 receptor. J. Biol. Chem. 266, 8068-8072.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8068-8072
    • Choudhury, G.G.1    Wang, L.M.2    Pierce, J.3    Harvey, S.A.4    Sakaguchi, A.Y.5
  • 10
    • 0242385220 scopus 로고
    • cDNA cloning and expression of the human A-type platelet-derived growth factor receptor establishes structural similarity to the B-type platelet-derived growth factor receptor
    • Claesson-Welsh, L., Eriksson, A., Westermark, B., and Heldin, C. H. (1989). cDNA cloning and expression of the human A-type platelet-derived growth factor receptor establishes structural similarity to the B-type platelet-derived growth factor receptor. Proc. Natl. Acad. Sci. USA 86, 4917-4921.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4917-4921
    • Claesson-Welsh, L.1    Eriksson, A.2    Westermark, B.3    Heldin, C.H.4
  • 11
    • 0032875460 scopus 로고    scopus 로고
    • Mechanism of action and in vivo role of platelet-derived growth factor
    • Heldin, C. H., and Westermark, B. (1999). Mechanism of action and in vivo role of platelet-derived growth factor. Physiol. Rev. 79, 1283-1316.
    • (1999) Physiol. Rev. , vol.79 , pp. 1283-1316
    • Heldin, C.H.1    Westermark, B.2
  • 13
    • 0029873387 scopus 로고    scopus 로고
    • Reactive oxygen species and programmed cell death
    • Jacobson, M. D. (1996). Reactive oxygen species and programmed cell death. Trends Biochem. Sci. 21, 83-86.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 83-86
    • Jacobson, M.D.1
  • 14
    • 0033615077 scopus 로고    scopus 로고
    • Receptor signaling: When dimerization is not enough
    • Jiang, G., and Hunter, T. (1999). Receptor signaling: when dimerization is not enough. Curr. Biol. 9, R568-R571.
    • (1999) Curr. Biol. , vol.9
    • Jiang, G.1    Hunter, T.2
  • 15
    • 0032889677 scopus 로고    scopus 로고
    • Redox regulation of cellular signalling
    • Kamata, H., and Hirata, H. (1999). Redox regulation of cellular signalling. Cell Signal. 11, 1-14.
    • (1999) Cell Signal. , vol.11 , pp. 1-14
    • Kamata, H.1    Hirata, H.2
  • 17
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with EGF
    • Lee, S. R., Kwon, K. S., Kim, S. R., and Rhee, S. G. (1998). Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with EGF. J. Biol. Chem. 273, 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
  • 18
    • 0028104202 scopus 로고
    • Regulation of signal transduction and signal diversity by receptor oligomerization
    • Lemmon, M. A., and Schlessinger, J. (1994). Regulation of signal transduction and signal diversity by receptor oligomerization. Trends Biochem. Sci. 19, 459-463.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 459-463
    • Lemmon, M.A.1    Schlessinger, J.2
  • 19
    • 0029589584 scopus 로고
    • Insulin-induced activation of phosphatidylinositol (PI) 3-kinase. Insulin-induced phosphorylation of insulin receptors and insulin receptor substrate-1 displaces phosphorylated platelet-derived growth factor receptors from binding sites on PI 3-kinase
    • Levy-Toledano, R., Blaettler, D. H., LaRochelle, W. J., and Taylor, S. I. (1995). Insulin-induced activation of phosphatidylinositol (PI) 3-kinase. Insulin-induced phosphorylation of insulin receptors and insulin receptor substrate-1 displaces phosphorylated platelet-derived growth factor receptors from binding sites on PI 3-kinase. J. Biol. Chem. 270, 30018-30022.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30018-30022
    • Levy-Toledano, R.1    Blaettler, D.H.2    LaRochelle, W.J.3    Taylor, S.I.4
  • 20
    • 0031896438 scopus 로고    scopus 로고
    • Binding of SH2 containing proteins to the insulin receptor: A new way for modulating insulin signalling
    • Liu, F., and Roth, R. A. (1998). Binding of SH2 containing proteins to the insulin receptor: a new way for modulating insulin signalling. Mol. Cell Biochem. 182, 73-78.
    • (1998) Mol. Cell Biochem. , vol.182 , pp. 73-78
    • Liu, F.1    Roth, R.A.2
  • 21
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • Meng, T. C., Fukada, T., and Tonks, N. K. (2002). Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol. Cell 9, 387-399.
    • (2002) Mol. Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 22
    • 0001515988 scopus 로고    scopus 로고
    • Involvement of tyrosine phosphorylation and PKC in the activation of phospholipase D by H2O2 in Swiss 3T3 fibroblasts
    • Min, D. S., Kim, E. G., and Exton, J. H. (1998). Involvement of tyrosine phosphorylation and PKC in the activation of phospholipase D by H2O2 in Swiss 3T3 fibroblasts. J. Biol. Chem. 273, 29986-29994.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29986-29994
    • Min, D.S.1    Kim, E.G.2    Exton, J.H.3
  • 23
    • 0026664626 scopus 로고
    • Ligand-induced polyubiquitination of the platelet-derived growth factor beta-receptor
    • Mori, S., Heldin, C. H., and Claesson-Welsh, L. (1992). Ligand-induced polyubiquitination of the platelet-derived growth factor beta-receptor. J. Biol. Chem. 267, 6429-6434.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6429-6434
    • Mori, S.1    Heldin, C.H.2    Claesson-Welsh, L.3
  • 24
    • 0027402689 scopus 로고
    • Ligand-induced ubiquitination of the platelet-derived growth factor beta-receptor plays a negative regulatory role in its mitogenic signaling
    • Mori, S., Heldin, C. H., and Claesson-Welsh, L. (1993). Ligand-induced ubiquitination of the platelet-derived growth factor beta-receptor plays a negative regulatory role in its mitogenic signaling. J. Biol. Chem. 268, 577-583.
    • (1993) J. Biol. Chem. , vol.268 , pp. 577-583
    • Mori, S.1    Heldin, C.H.2    Claesson-Welsh, L.3
  • 25
    • 0028788180 scopus 로고
    • Degradation process of ligand-stimulated platelet-derived growth factor beta-receptor involves ubiquitin-proteasome proteolytic pathway
    • Mori, S., Tanaka, K., Omura, S., and Saito, Y. (1995). Degradation process of ligand-stimulated platelet-derived growth factor beta-receptor involves ubiquitin-proteasome proteolytic pathway. J. Biol. Chem. 270, 29447-29452.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29447-29452
    • Mori, S.1    Tanaka, K.2    Omura, S.3    Saito, Y.4
  • 26
    • 0031919049 scopus 로고    scopus 로고
    • Role of binding proteins to IRS-1 in insulin signalling
    • Ogawa, W., Matozaki, T., and Kasuga, M. (1998). Role of binding proteins to IRS-1 in insulin signalling. Mol. Cell Biochem. 182, 13-22.
    • (1998) Mol. Cell Biochem. , vol.182 , pp. 13-22
    • Ogawa, W.1    Matozaki, T.2    Kasuga, M.3
  • 27
    • 0035371620 scopus 로고    scopus 로고
    • Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatases
    • Ostman, A., and Bohmer, F. D. (2001). Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatases. Trends Cell Biol. 11, 258-266.
    • (2001) Trends Cell Biol. , vol.11 , pp. 258-266
    • Ostman, A.1    Bohmer, F.D.2
  • 28
    • 0028466383 scopus 로고
    • Oxygen and the control of gene expression
    • Pahl, H. L., and Baeuerle, P. A. (1994). Oxygen and the control of gene expression. Bioessays 16, 497-502.
    • (1994) Bioessays , vol.16 , pp. 497-502
    • Pahl, H.L.1    Baeuerle, P.A.2
  • 29
    • 0027466903 scopus 로고
    • Insulin-induced phosphorylation of the 46- and 52-kDa Shc proteins
    • Pronk, G. J., McGlade, J., Pelicci, G., Pawson, T., and Bos, J. L. (1993). Insulin-induced phosphorylation of the 46- and 52-kDa Shc proteins. J. Biol. Chem. 268, 5748-5753.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5748-5753
    • Pronk, G.J.1    McGlade, J.2    Pelicci, G.3    Pawson, T.4    Bos, J.L.5
  • 30
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. (2000). Cell signaling by receptor tyrosine kinases. Cell 103, 211-225.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 31
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1
    • Schreck, R., Rieber, P., and Baeuerle, P. A. (1991). Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1. EMBO J 10, 2247-2258.
    • (1991) EMBO J. , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 32
    • 0027288587 scopus 로고
    • The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: Implications for insulin control of ras signalling
    • Skolnik, E. Y., Lee, C. H., Batzer, A., Vicentini, L. M., Zhou, M., Daly, R., Myers, M. J., Jr., Backer, J. M., Ullrich, A., and White, M. F. (1993). The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: implications for insulin control of ras signalling. EMBO J. 12, 1929-1936.
    • (1993) EMBO J. , vol.12 , pp. 1929-1936
    • Skolnik, E.Y.1    Lee, C.H.2    Batzer, A.3    Vicentini, L.M.4    Zhou, M.5    Daly, R.6    Myers Jr., M.J.7    Backer, J.M.8    Ullrich, A.9    White, M.F.10
  • 33
    • 0025971082 scopus 로고
    • Effect of receptor kinase inactivation on the rate of internalization and degradation of platelet-derived growth factor and the platelet-derived growth factor beta-receptor
    • Sorkin, A., Westermark, B., Heldin, C. H., and Claesson-Welsh, L. (1991). Effect of receptor kinase inactivation on the rate of internalization and degradation of platelet-derived growth factor and the platelet-derived growth factor beta-receptor. J. Cell Biol. 112, 469-478.
    • (1991) J. Cell Biol. , vol.112 , pp. 469-478
    • Sorkin, A.1    Westermark, B.2    Heldin, C.H.3    Claesson-Welsh, L.4
  • 34
    • 0032566525 scopus 로고    scopus 로고
    • Platelet-derived growth factor inhibits insulin stimulation of insulin receptor substrate-1-associated phosphatidylinositol 3-kinase in 3T3-L1 adipocytes without affecting glucose transport
    • Staubs, P. A., Nelson, J. G., Reichart, D. R., and Olefsky, J. M. (1998). Platelet-derived growth factor inhibits insulin stimulation of insulin receptor substrate-1-associated phosphatidylinositol 3-kinase in 3T3-L1 adipocytes without affecting glucose transport. J. Biol. Chem. 273, 25139-25147.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25139-25147
    • Staubs, P.A.1    Nelson, J.G.2    Reichart, D.R.3    Olefsky, J.M.4
  • 35
    • 0027437376 scopus 로고
    • Pleiotropic insulin signals are engaged by multisite phosphorylation of IRS-1
    • Sun, X. J., Crimmins, D. L., Myers, M. G., Jr., Miralpeix, M., and White, M. F. (1993). Pleiotropic insulin signals are engaged by multisite phosphorylation of IRS-1. Mol. Cell Biol. 13, 7418-7428.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 7418-7428
    • Sun, X.J.1    Crimmins, D.L.2    Myers Jr., M.G.3    Miralpeix, M.4    White, M.F.5
  • 36
    • 0028973482 scopus 로고
    • Requirement for generation of H2O2 for platelet-derived growth factor signal transduction
    • Sundaresan, M., Yu, Z. X., Ferrans, V. J., Irani, K., and Finkel, T. (1995). Requirement for generation of H2O2 for platelet-derived growth factor signal transduction. Science 270, 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
  • 37
    • 9444267146 scopus 로고    scopus 로고
    • Csk enhances insulin-stimulated dephosphorylation of focal adhesion proteins
    • Tobe, K., et al. (1996). Csk enhances insulin-stimulated dephosphorylation of focal adhesion proteins. Mol. Cell Biol. 16, 4765-4772.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 4765-4772
    • Tobe, K.1
  • 38
    • 0032784061 scopus 로고    scopus 로고
    • Grb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesis
    • Wang, J., Dai, H., Yousaf, N., Moussaif, M., Deng, Y., Boufelliga, A., Swamy, O. R., Leone, M. E., and Riedel, H. (1999). Grb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesis. Mol. Cell Biol. 19, 6217-6228.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 6217-6228
    • Wang, J.1    Dai, H.2    Yousaf, N.3    Moussaif, M.4    Deng, Y.5    Boufelliga, A.6    Swamy, O.R.7    Leone, M.E.8    Riedel, H.9
  • 39
    • 0031616132 scopus 로고    scopus 로고
    • The IRS-signaling system: A network of docking proteins that mediate insulin and cytokine action
    • White, M. F. (1998). The IRS-signaling system: a network of docking proteins that mediate insulin and cytokine action. Recent Prog. Horm. Res. 53, 119-138.
    • (1998) Recent Prog. Horm. Res. , vol.53 , pp. 119-138
    • White, M.F.1
  • 40
    • 0027482041 scopus 로고
    • Reactive oxygen species mediate phorbol ester-regulated tyrosine phosphorylation and phospholipase A2 activation: Potentiation by vanadate
    • Zor, U., Ferber, E., Gergely, P., Szucs, K., Dombradi, V., and Goldman, R. (1993). Reactive oxygen species mediate phorbol ester-regulated tyrosine phosphorylation and phospholipase A2 activation: potentiation by vanadate. Biochem. J. 295, 879-888.
    • (1993) Biochem. J. , vol.295 , pp. 879-888
    • Zor, U.1    Ferber, E.2    Gergely, P.3    Szucs, K.4    Dombradi, V.5    Goldman, R.6


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