메뉴 건너뛰기




Volumn 25, Issue 15, 2005, Pages 6391-6403

Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growth

Author keywords

[No Author keywords available]

Indexed keywords

INTEGRIN; PROTEIN TYROSINE KINASE; REACTIVE OXYGEN METABOLITE;

EID: 22544453858     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.25.15.6391-6403.2005     Document Type: Article
Times cited : (382)

References (39)
  • 1
    • 0344827268 scopus 로고    scopus 로고
    • Oxidants in receptor tyrosine kinase signal transduction pathways
    • Aslan, M., and T. Ozben. 2003. Oxidants in receptor tyrosine kinase signal transduction pathways. Antioxid. Redox Signal. 5:781-788.
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 781-788
    • Aslan, M.1    Ozben, T.2
  • 2
    • 0027986585 scopus 로고
    • Transforming growth factor beta down-regulates Src family protein tyrosine kinase signaling pathways
    • Atfi, A., E. Drobetsky, M. Boissonneault, A. Chapdelaine, and S. Chevalier. 1994. Transforming growth factor beta down-regulates Src family protein tyrosine kinase signaling pathways. J. Biol. Chem. 269:30688-30693.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30688-30693
    • Atfi, A.1    Drobetsky, E.2    Boissonneault, M.3    Chapdelaine, A.4    Chevalier, S.5
  • 3
    • 0035984912 scopus 로고    scopus 로고
    • ROS, stress-activated kinases and stress signaling in cancer
    • Benhar, M., D. Engelberg, and A. Levitzki. 2002. ROS, stress-activated kinases and stress signaling in cancer. EMBO Rep. 3:420-425.
    • (2002) EMBO Rep. , vol.3 , pp. 420-425
    • Benhar, M.1    Engelberg, D.2    Levitzki, A.3
  • 4
    • 0034731372 scopus 로고    scopus 로고
    • Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines
    • Bjorge, J. D., A. Pang, and D. J. Fujita. 2000. Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines. J. Biol. Chem. 275:41439-41446.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41439-41446
    • Bjorge, J.D.1    Pang, A.2    Fujita, D.J.3
  • 5
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of src
    • Brown, M. T., and J. A. Cooper. 1996. Regulation, substrates and functions of src. Biochim. Biophys. Acta 1287:121-149.
    • (1996) Biochim. Biophys. Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 6
    • 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
  • 7
    • 0642276003 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction
    • Chiarugi, P., and P. Cirri. 2003. Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction. Trends Biochem. Sci. 28:509-514.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 509-514
    • Chiarugi, P.1    Cirri, P.2
  • 9
    • 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., T. Fiaschi, M. L. Taddei, D. Talini, E. Giannoni, G. Raugei, and G. Ramponi. 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
  • 10
    • 0037780966 scopus 로고    scopus 로고
    • Reactive oxygen species as essential mediators of cell adhesion: The oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion
    • Chiarugi, P., G. Pani, E. Giannoni, L. Taddei, R. Colavitti, G. Raugei, M. Symons, S. Borrello, T. Galeotti, and G. Ramponi. 2003. Reactive oxygen species as essential mediators of cell adhesion: the oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion. J. Cell Biol. 161: 933-944.
    • (2003) J. Cell Biol. , vol.161 , pp. 933-944
    • Chiarugi, P.1    Pani, G.2    Giannoni, E.3    Taddei, L.4    Colavitti, R.5    Raugei, G.6    Symons, M.7    Borrello, S.8    Galeotti, T.9    Ramponi, G.10
  • 11
    • 0027300619 scopus 로고
    • The when and how of Src regulation
    • Cooper, J. A., and B. Howell. 1993. The when and how of Src regulation. Cell 73:1051-1054.
    • (1993) Cell , vol.73 , pp. 1051-1054
    • Cooper, J.A.1    Howell, B.2
  • 12
    • 0032486476 scopus 로고    scopus 로고
    • Role of tyrosine kinase activity of epidermal growth factor receptor in the lysophosphatidic acid-stimulated mitogen-activated protein kinase pathway
    • Cunnick, J. M., J. F. Dorsey, T. Standley, J. Turkson, A. J. Kraker, D. W. Fry, R. Jove, and J. Wu. 1998. Role of tyrosine kinase activity of epidermal growth factor receptor in the lysophosphatidic acid-stimulated mitogen-activated protein kinase pathway. J. Biol. Chem. 273:14468-14475.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14468-14475
    • Cunnick, J.M.1    Dorsey, J.F.2    Standley, T.3    Turkson, J.4    Kraker, A.J.5    Fry, D.W.6    Jove, R.7    Wu, J.8
  • 13
    • 0036139524 scopus 로고    scopus 로고
    • Reactive oxygen species and signal transduction
    • Finkel, T. 2001. Reactive oxygen species and signal transduction. IUBMB Life 52:3-6.
    • (2001) IUBMB Life , vol.52 , pp. 3-6
    • Finkel, T.1
  • 15
    • 0031464009 scopus 로고    scopus 로고
    • The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src
    • Gonfloni, S., J. C. Williams, K. Hattula, A. Weijland, R. K. Wierenga, and G. Superti-Furga. 1997. The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src. EMBO J. 16:7261-7271.
    • (1997) EMBO J. , vol.16 , pp. 7261-7271
    • Gonfloni, S.1    Williams, J.C.2    Hattula, K.3    Weijland, A.4    Wierenga, R.K.5    Superti-Furga, G.6
  • 16
    • 0035953855 scopus 로고    scopus 로고
    • Different kinds of reactive oxygen and nitrogen species were detected in colon and breast tumors
    • Haklar, G., E. Sayin-Ozveri, M. Yuksel, A. O. Aktan, and A. S. Yalcin. 2001. Different kinds of reactive oxygen and nitrogen species were detected in colon and breast tumors. Cancer Lett. 165:219-224.
    • (2001) Cancer Lett. , vol.165 , pp. 219-224
    • Haklar, G.1    Sayin-Ozveri, E.2    Yuksel, M.3    Aktan, A.O.4    Yalcin, A.S.5
  • 17
    • 0028903083 scopus 로고
    • Augmentation of metalloproteinase (gelatinase) activity secreted from Rous sarcoma virus-infected cells correlates with transforming activity of src
    • Hamaguchi, M., S. Yamagata, A. A. Thant, H. Xiao, H. Iwata, T. Mazaki, and H. Hanafusa. 1995. Augmentation of metalloproteinase (gelatinase) activity secreted from Rous sarcoma virus-infected cells correlates with transforming activity of src. Oncogene 10:1037-1043.
    • (1995) Oncogene , vol.10 , pp. 1037-1043
    • Hamaguchi, M.1    Yamagata, S.2    Thant, A.A.3    Xiao, H.4    Iwata, H.5    Mazaki, T.6    Hanafusa, H.7
  • 19
    • 0027410485 scopus 로고
    • Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the lck, fyn, and c-src tyrosine protein kinases
    • Hurley, T. R., R. Hyman, and B. M. Sefton. 1993. Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the lck, fyn, and c-src tyrosine protein kinases. Mol. Cell. Biol. 13:1651-1656.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1651-1656
    • Hurley, T.R.1    Hyman, R.2    Sefton, B.M.3
  • 21
    • 0032537022 scopus 로고    scopus 로고
    • Expression of the v-Src oncoprotein in fibroblasts disrupts normal regulation of the CDK inhibitor p27 and inhibits quiescence
    • Johnson, D., M. C. Frame, and J. A. Wyke. 1998. Expression of the v-Src oncoprotein in fibroblasts disrupts normal regulation of the CDK inhibitor p27 and inhibits quiescence. Oncogene 16:2017-2028.
    • (1998) Oncogene , vol.16 , pp. 2017-2028
    • Johnson, D.1    Frame, M.C.2    Wyke, J.A.3
  • 23
    • 0033955104 scopus 로고    scopus 로고
    • Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinase inhibitor
    • Mott, J. D., C. L. Thomas, M. T. Rosenbach, K. Takahara, D. S. Greenspan, and M. J. Banda. 2000. Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinase inhibitor. J. Biol. Chem. 275:1384-1390.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1384-1390
    • Mott, J.D.1    Thomas, C.L.2    Rosenbach, M.T.3    Takahara, K.4    Greenspan, D.S.5    Banda, M.J.6
  • 24
    • 0037341905 scopus 로고    scopus 로고
    • Redox-dependent downregulation of Rho by Rac
    • Nimnual, A. S., L. J. Taylor, and D. Bar-Sagi. 2003. Redox-dependent downregulation of Rho by Rac. Nat. Cell Biol. 5:236-241.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 236-241
    • Nimnual, A.S.1    Taylor, L.J.2    Bar-Sagi, D.3
  • 25
    • 3142751485 scopus 로고    scopus 로고
    • Src in human carcinogenesis
    • Russello, S. V., and S. K. Shore. 2003. Src in human carcinogenesis. Front. Biosci. 8:51068-51073.
    • (2003) Front. Biosci. , vol.8 , pp. 51068-51073
    • Russello, S.V.1    Shore, S.K.2
  • 26
    • 0030965296 scopus 로고    scopus 로고
    • Cell to substratum adhesion is involved in v-Src-induced cellular protein tyrosine phosphorylation: Implication for the adhesion-regulated protein tyrosine phosphatase activity
    • Sabe, H., M. Hamaguchi, and H. Hanafusa. 1997. Cell to substratum adhesion is involved in v-Src-induced cellular protein tyrosine phosphorylation: implication for the adhesion-regulated protein tyrosine phosphatase activity. Oncogene 14:1779-1788.
    • (1997) Oncogene , vol.14 , pp. 1779-1788
    • Sabe, H.1    Hamaguchi, M.2    Hanafusa, H.3
  • 27
    • 0036229694 scopus 로고    scopus 로고
    • Networks and crosstalk: Integrin signalling spreads
    • Schwartz, M. A., and M. H. Ginsberg. 2002. Networks and crosstalk: integrin signalling spreads. Nat. Cell Biol. 4:E65-E68.
    • (2002) Nat. Cell Biol. , vol.4
    • Schwartz, M.A.1    Ginsberg, M.H.2
  • 28
    • 0032416113 scopus 로고    scopus 로고
    • Activation of the JAK-STAT pathway by reactive oxygen species
    • Simon, A. R., U. Rai, B. L. Fanburg, and B. H. Cochran. 1998. Activation of the JAK-STAT pathway by reactive oxygen species. Am. J. Physiol. 275: C1640-C1652.
    • (1998) Am. J. Physiol. , vol.275
    • Simon, A.R.1    Rai, U.2    Fanburg, B.L.3    Cochran, B.H.4
  • 29
    • 0033587069 scopus 로고    scopus 로고
    • Receptor protein tyrosine phosphatase alpha activates Src-family kinases and controls integrin-mediated responses in fibroblasts
    • Su, J., M. Muranjan, and J. Sap. 1999. Receptor protein tyrosine phosphatase alpha activates Src-family kinases and controls integrin-mediated responses in fibroblasts. Curr. Biol. 9:505-511.
    • (1999) Curr. Biol. , vol.9 , pp. 505-511
    • Su, J.1    Muranjan, M.2    Sap, J.3
  • 30
    • 0026021362 scopus 로고
    • Production of large amounts of hydrogen peroxide by human tumor cells
    • Szatrowski, T. P., and C. F. Nathan. 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
  • 31
    • 0033628016 scopus 로고    scopus 로고
    • Kinases of the Src family: Structure and functions
    • Tatosyan, A. G., and O. A. Mizenina. 2000. Kinases of the Src family: structure and functions. Biochemistry (Moscow) 65:49-58.
    • (2000) Biochemistry (Moscow) , vol.65 , pp. 49-58
    • Tatosyan, A.G.1    Mizenina, O.A.2
  • 32
    • 0033529675 scopus 로고    scopus 로고
    • Reactive oxygen species mediate the activation of Akt/protein kinase B by angiotensin II in vascular smooth muscle cells
    • Ushio-Fukai, M., R. W. Alexander, M. Akers, Q. Yin, Y. Fujio, K. Walsh, and K. K. Griendling. 1999. Reactive oxygen species mediate the activation of Akt/protein kinase B by angiotensin II in vascular smooth muscle cells. J. Biol. Chem. 274:22699-22704.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22699-22704
    • Ushio-Fukai, M.1    Alexander, R.W.2    Akers, M.3    Yin, Q.4    Fujio, Y.5    Walsh, K.6    Griendling, K.K.7
  • 34
    • 0037157824 scopus 로고    scopus 로고
    • Integrins engage mitochondrial function for signal transduction by a mechanism dependent on Rho GTPases
    • Werner, E., and Z. Werb. 2002. Integrins engage mitochondrial function for signal transduction by a mechanism dependent on Rho GTPases. J. Cell Biol. 158:357-368.
    • (2002) J. Cell Biol. , vol.158 , pp. 357-368
    • Werner, E.1    Werb, Z.2
  • 35
    • 0036193746 scopus 로고    scopus 로고
    • Oxidants painting the cysteine chapel: Redox regulation of PTPs
    • Xu, D., I. I. Rovira, and T. Finkel. 2002. Oxidants painting the cysteine chapel: redox regulation of PTPs. Dev. Cell 2:251-252.
    • (2002) Dev. Cell , vol.2 , pp. 251-252
    • Xu, D.1    Rovira, I.I.2    Finkel, T.3
  • 36
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., S. C. Harrison, and M. J. Eck. 1997. Three-dimensional structure of the tyrosine kinase c-Src. Nature 385:595-602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 37
    • 0024348296 scopus 로고
    • Suppression by cathepsin L inhibitors of the invasion of amnion membranes by murine cancer cells
    • Yagel, S., A. H. Warner, H. N. Nellans, P. K. Lala, C. Waghorne, and D. T. Denhardt. 1989. Suppression by cathepsin L inhibitors of the invasion of amnion membranes by murine cancer cells. Cancer Res. 49:3553-3557.
    • (1989) Cancer Res. , vol.49 , pp. 3553-3557
    • Yagel, S.1    Warner, A.H.2    Nellans, H.N.3    Lala, P.K.4    Waghorne, C.5    Denhardt, D.T.6
  • 39
    • 0034161405 scopus 로고    scopus 로고
    • A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
    • Zheng, X. M., R. J. Resnick, and D. Shalloway. 2000. A phosphotyrosine displacement mechanism for activation of Src by PTPalpha. EMBO J. 19: 964-978.
    • (2000) EMBO J. , vol.19 , pp. 964-978
    • Zheng, X.M.1    Resnick, R.J.2    Shalloway, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.