메뉴 건너뛰기




Volumn 1843, Issue 2, 2014, Pages 265-274

T cell activation induces CuZn superoxide dismutase (SOD)-1 intracellular re-localization, production and secretion

Author keywords

Human T lymphocyte; Intracellular localization; Microvesicle secretion; SOD 1; T cell activation; TCR triggering

Indexed keywords

ACETYLCYSTEINE; CD3 ANTIBODY; COPPER ZINC SUPEROXIDE DISMUTASE; EXTRACELLULAR SUPEROXIDE DISMUTASE; GAMMA INTERFERON; HYDROGEN PEROXIDE; MESSENGER RNA; T LYMPHOCYTE RECEPTOR;

EID: 84890285608     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2013.10.020     Document Type: Article
Times cited : (34)

References (76)
  • 2
    • 62849094483 scopus 로고    scopus 로고
    • Navigating the network: signaling cross-talk in hematopoietic cells
    • Fraser I.D., Germain R.N. Navigating the network: signaling cross-talk in hematopoietic cells. Nat. Immunol. 2009, 10:327-331.
    • (2009) Nat. Immunol. , vol.10 , pp. 327-331
    • Fraser, I.D.1    Germain, R.N.2
  • 3
    • 0023903097 scopus 로고
    • Oxidative phenomena are implicated in human T-cell stimulation
    • Sekkat C., Dornand J., Gerber M. Oxidative phenomena are implicated in human T-cell stimulation. Immunology 1988, 63:431-437.
    • (1988) Immunology , vol.63 , pp. 431-437
    • Sekkat, C.1    Dornand, J.2    Gerber, M.3
  • 4
    • 0030587124 scopus 로고    scopus 로고
    • The role of reactive oxygen intermediates in TCR-induced death of T cell blasts and hybridomas
    • Williams M.S., Henkart P.A. The role of reactive oxygen intermediates in TCR-induced death of T cell blasts and hybridomas. J. Immunol. 1996, 157:2395-2402.
    • (1996) J. Immunol. , vol.157 , pp. 2395-2402
    • Williams, M.S.1    Henkart, P.A.2
  • 5
    • 0344286517 scopus 로고    scopus 로고
    • The role of reactive oxygen species in triggering proliferation and IL-2 secretion in T cells
    • Tatla S., Woodhead V., Foreman J.C., Chai B.M. The role of reactive oxygen species in triggering proliferation and IL-2 secretion in T cells. Free Radic. Biol. Med. 1999, 26:14-24.
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 14-24
    • Tatla, S.1    Woodhead, V.2    Foreman, J.C.3    Chai, B.M.4
  • 7
    • 0029164695 scopus 로고
    • IL-2 gene expression and NF-kappa B activation through CD28 requires reactive oxygen production by 5-lipoxygenase
    • Los M., Schenk H., Hexel K., Baeuerle P.A., Droge W., Schulze-Osthoff K. IL-2 gene expression and NF-kappa B activation through CD28 requires reactive oxygen production by 5-lipoxygenase. EMBO J. 1995, 14:3731-3740.
    • (1995) EMBO J. , vol.14 , pp. 3731-3740
    • Los, M.1    Schenk, H.2    Hexel, K.3    Baeuerle, P.A.4    Droge, W.5    Schulze-Osthoff, K.6
  • 8
    • 4444221709 scopus 로고    scopus 로고
    • T cells express a phagocyte-type NADPH oxidase that is activated after T cell receptor stimulation
    • Jackson S.H., Devadas S., Kwon J., Pinto L.A., Williams M.S. T cells express a phagocyte-type NADPH oxidase that is activated after T cell receptor stimulation. Nat. Immunol. 2004, 5:818-827.
    • (2004) Nat. Immunol. , vol.5 , pp. 818-827
    • Jackson, S.H.1    Devadas, S.2    Kwon, J.3    Pinto, L.A.4    Williams, M.S.5
  • 10
    • 0037033433 scopus 로고    scopus 로고
    • Discrete generation of superoxide and hydrogen peroxide by T cell receptor stimulation: selective regulation of mitogen-activated protein kinase activation and fas ligand expression
    • Devadas S., Zaritskaya L., Rhee S.G., Oberley L., Williams M.S. Discrete generation of superoxide and hydrogen peroxide by T cell receptor stimulation: selective regulation of mitogen-activated protein kinase activation and fas ligand expression. J. Exp. Med. 2002, 195:59-70.
    • (2002) J. Exp. Med. , vol.195 , pp. 59-70
    • Devadas, S.1    Zaritskaya, L.2    Rhee, S.G.3    Oberley, L.4    Williams, M.S.5
  • 11
    • 0142075336 scopus 로고    scopus 로고
    • T cell receptor-stimulated generation of hydrogen peroxide inhibits MEK-ERK activation and lck serine phosphorylation
    • Kwon J., Devadas S., Williams M.S. T cell receptor-stimulated generation of hydrogen peroxide inhibits MEK-ERK activation and lck serine phosphorylation. Free Radic. Biol. Med. 2003, 35:406-417.
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 406-417
    • Kwon, J.1    Devadas, S.2    Williams, M.S.3
  • 12
    • 4844227764 scopus 로고    scopus 로고
    • Antimicrobial reactive oxygen and nitrogen species: concepts and controversies
    • Fang F.C. Antimicrobial reactive oxygen and nitrogen species: concepts and controversies. Nat. Rev. Microbiol. 2004, 2:820-832.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 820-832
    • Fang, F.C.1
  • 13
    • 0033818354 scopus 로고    scopus 로고
    • Ras-dependent and -independent regulation of reactive oxygen species by mitogenic growth factors and TGFh1
    • Thannickal V.J., Day R.M., Klinz S.G., Bastien M.C., Larios J.M., Fanburg B.L. Ras-dependent and -independent regulation of reactive oxygen species by mitogenic growth factors and TGFh1. FASEB J. 2000, 14:1741-1748.
    • (2000) FASEB J. , vol.14 , pp. 1741-1748
    • Thannickal, V.J.1    Day, R.M.2    Klinz, S.G.3    Bastien, M.C.4    Larios, J.M.5    Fanburg, B.L.6
  • 14
    • 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., Goldstein B.J. Insulin stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade. J. Biol. Chem. 2001, 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
  • 15
    • 0032510977 scopus 로고    scopus 로고
    • Griendling KK, P38 mitogen-activated protein kinase is a critical component of the redox-sensitive signaling pathways activated by angiotensin II. Role in vascular smooth muscle cell hypertrophy
    • Ushio-Fukai M., Alexander R.W., Akers M. Griendling KK, P38 mitogen-activated protein kinase is a critical component of the redox-sensitive signaling pathways activated by angiotensin II. Role in vascular smooth muscle cell hypertrophy. J. Biol. Chem. 1998, 273:15022-15029.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15022-15029
    • Ushio-Fukai, M.1    Alexander, R.W.2    Akers, M.3
  • 16
    • 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., Rhe S.G. Epidermal growth factor (EGF)-induced generation of hydrogen peroxide: role in EGF receptor-mediated tyrosine phosphorylation. J. Biol. Chem. 1997, 272:217-222.
    • (1997) J. Biol. Chem. , vol.272 , pp. 217-222
    • Bae, Y.S.1    Kang, S.W.2    Seo, M.S.3    Baines, I.C.4    Tekle, E.5    Chock, P.B.6    Rhe, S.G.7
  • 17
    • 0029902928 scopus 로고    scopus 로고
    • Control of cell proliferation by reactive oxygen species
    • Burdon R.H. Control of cell proliferation by reactive oxygen species. Biochem. Soc. Trans. 1996, 24:1028-1032.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 1028-1032
    • Burdon, R.H.1
  • 18
    • 0034633602 scopus 로고    scopus 로고
    • Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation
    • Rhee S.G., Bae Y.S., Lee S.-R., Kwon J. Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation. Sci. STKE 2000, 10:1-6.
    • (2000) Sci. STKE , vol.10 , pp. 1-6
    • Rhee, S.G.1    Bae, Y.S.2    Lee, S.-R.3    Kwon, J.4
  • 19
    • 0036911138 scopus 로고    scopus 로고
    • Hydrogen peroxide as second messenger in lymphocyte activation
    • Reth M. Hydrogen peroxide as second messenger in lymphocyte activation. Nat. Immunol. 2002, 3:1129-1134.
    • (2002) Nat. Immunol. , vol.3 , pp. 1129-1134
    • Reth, M.1
  • 20
    • 33745631769 scopus 로고    scopus 로고
    • 2, a necessary evil for cell signaling
    • 2, a necessary evil for cell signaling. Science 2006, 312:1882-1883.
    • (2006) Science , vol.312 , pp. 1882-1883
    • Rhee, S.G.1
  • 21
    • 84857919018 scopus 로고    scopus 로고
    • Superoxide dismutases: ancient enzymes and new insights
    • Miller A.F. Superoxide dismutases: ancient enzymes and new insights. FEBS Lett. 2012, 586:585-595.
    • (2012) FEBS Lett. , vol.586 , pp. 585-595
    • Miller, A.F.1
  • 22
    • 0006157248 scopus 로고
    • Human copper containing superoxide dismutase of high molecular weight
    • Marklund S.L. Human copper containing superoxide dismutase of high molecular weight. Proc. Natl. Acad. Sci. U. S. A. 1982, 79:7634-7638.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 7634-7638
    • Marklund, S.L.1
  • 23
    • 0023607878 scopus 로고
    • Expression of human extracellular superoxide dismutase in Chinese hamster ovary cells and characterisation of the product
    • Tibell L., Hjalmarsson K., Edlund T., Skogman G., Engstrom A., Marklund S.L. Expression of human extracellular superoxide dismutase in Chinese hamster ovary cells and characterisation of the product. Proc. Natl. Acad. Sci. U. S. A. 1987, 84:634-638.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 634-638
    • Tibell, L.1    Hjalmarsson, K.2    Edlund, T.3    Skogman, G.4    Engstrom, A.5    Marklund, S.L.6
  • 24
    • 0026634285 scopus 로고
    • Regulation of antioxidant enzymes
    • Harris E.D. Regulation of antioxidant enzymes. FASEB J. 1992, 6:2675-2683.
    • (1992) FASEB J. , vol.6 , pp. 2675-2683
    • Harris, E.D.1
  • 25
    • 33749047437 scopus 로고    scopus 로고
    • Localizing NADPH oxidase-derived ROS
    • Ushio-Fukai M. Localizing NADPH oxidase-derived ROS. Sci. STKE 2006, 349:re8.
    • (2006) Sci. STKE , vol.349
    • Ushio-Fukai, M.1
  • 27
    • 70450267433 scopus 로고    scopus 로고
    • Lipid rafts and caveolin-1 coordinate Interleukin-1 beta (IL-1 beta)-dependent activation of NFkB by controlling endocytosis of Nox2 and IL-1 beta receptor 1 from the plasma membrane
    • Oakley F.D., Smith R.L., Engelhargt J.F. Lipid rafts and caveolin-1 coordinate Interleukin-1 beta (IL-1 beta)-dependent activation of NFkB by controlling endocytosis of Nox2 and IL-1 beta receptor 1 from the plasma membrane. J. Biol. Chem. 2009, 284:33255-33264.
    • (2009) J. Biol. Chem. , vol.284 , pp. 33255-33264
    • Oakley, F.D.1    Smith, R.L.2    Engelhargt, J.F.3
  • 29
    • 0029884093 scopus 로고    scopus 로고
    • Evidence for secretion of cytosolic CuZn superoxide dismutase by HEPG2 cells and human fibroblast
    • Mondola P., Annella T., Santillo M., Santangelo F. Evidence for secretion of cytosolic CuZn superoxide dismutase by HEPG2 cells and human fibroblast. Int. J. Biochem. Cell Biol. 1996, 28:677-681.
    • (1996) Int. J. Biochem. Cell Biol. , vol.28 , pp. 677-681
    • Mondola, P.1    Annella, T.2    Santillo, M.3    Santangelo, F.4
  • 30
    • 0032521619 scopus 로고    scopus 로고
    • Secretion and increase of intracellular CuZn superoxide dismutase content in human neuroblastoma SK-N-BE cells
    • Mondola P., Annella T., Seru R., Santangelo F., Iossa S., Gioielli A., Santillo M. Secretion and increase of intracellular CuZn superoxide dismutase content in human neuroblastoma SK-N-BE cells. Brain Res. Bull. 1998, 45:517-520.
    • (1998) Brain Res. Bull. , vol.45 , pp. 517-520
    • Mondola, P.1    Annella, T.2    Seru, R.3    Santangelo, F.4    Iossa, S.5    Gioielli, A.6    Santillo, M.7
  • 31
    • 0031879467 scopus 로고    scopus 로고
    • Rat testicular extracellular superoxide dismutase: its purification, cellular distribution, and regulation
    • Mruk D., Cheng C.H., Cheng Y.H., Mo M.Y., Grima J., Silvestrini B., Lee W.M., Cheng C.Y. Rat testicular extracellular superoxide dismutase: its purification, cellular distribution, and regulation. Biol. Reprod. 1998, 59:298-308.
    • (1998) Biol. Reprod. , vol.59 , pp. 298-308
    • Mruk, D.1    Cheng, C.H.2    Cheng, Y.H.3    Mo, M.Y.4    Grima, J.5    Silvestrini, B.6    Lee, W.M.7    Cheng, C.Y.8
  • 33
    • 12144249923 scopus 로고    scopus 로고
    • Impaired extracellular secretion of mutant superoxide dismutase 1 associates with neurotoxicity in familial amyotrophic lateral sclerosis
    • Turner B.J., Atkin J.D., Farg M.A., Zang D.W., Rembach A., Lopes E.C., Patch J.D., Hill A.F., Cheema S.S. Impaired extracellular secretion of mutant superoxide dismutase 1 associates with neurotoxicity in familial amyotrophic lateral sclerosis. J. Neurosci. 2005, 25:108-117.
    • (2005) J. Neurosci. , vol.25 , pp. 108-117
    • Turner, B.J.1    Atkin, J.D.2    Farg, M.A.3    Zang, D.W.4    Rembach, A.5    Lopes, E.C.6    Patch, J.D.7    Hill, A.F.8    Cheema, S.S.9
  • 35
    • 29444443348 scopus 로고    scopus 로고
    • Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis
    • Urushitani M., Sik A., Sakurai T., Nukina N., Takahashi R., Julien J.-P. Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis. Nat. Neurosci. 2006, 9:108-118.
    • (2006) Nat. Neurosci. , vol.9 , pp. 108-118
    • Urushitani, M.1    Sik, A.2    Sakurai, T.3    Nukina, N.4    Takahashi, R.5    Julien, J.-P.6
  • 36
    • 46749107070 scopus 로고    scopus 로고
    • The endoplasmic reticulum-Golgi pathway is a target for translocation and aggregation of mutant superoxide dismutase linked to ALS
    • Urushitani M., Ezzi S.A., Matsuo A., Tooyama I., Julien J.-P. The endoplasmic reticulum-Golgi pathway is a target for translocation and aggregation of mutant superoxide dismutase linked to ALS. FASEB J. 2008, 22:2476-2487.
    • (2008) FASEB J. , vol.22 , pp. 2476-2487
    • Urushitani, M.1    Ezzi, S.A.2    Matsuo, A.3    Tooyama, I.4    Julien, J.-P.5
  • 37
    • 0037474171 scopus 로고    scopus 로고
    • The Cu,Zn superoxide dismutase in neuroblastoma SK-N-BE cells is exported by a microvesicles dependent pathway
    • Mondola P., Ruggiero G., Seru' R., et al. The Cu,Zn superoxide dismutase in neuroblastoma SK-N-BE cells is exported by a microvesicles dependent pathway. Brain Res. Mol. Brain Res. 2003, 110:45-51.
    • (2003) Brain Res. Mol. Brain Res. , vol.110 , pp. 45-51
    • Mondola, P.1    Ruggiero, G.2    Seru', R.3
  • 38
    • 34447307381 scopus 로고    scopus 로고
    • Evidence of calcium- and SNARE-dependent release of CuZn superoxide dismutase from rat pituitary GH3 cells and synaptosomes in response to depolarization
    • Santillo M., Secondo A., Serù R., Damiano S., Garbi C., Taverna E., Rosa P., Giovedì S., Benfenati F., Mondola P. Evidence of calcium- and SNARE-dependent release of CuZn superoxide dismutase from rat pituitary GH3 cells and synaptosomes in response to depolarization. J. Neurochem. 2007, 102:679-685.
    • (2007) J. Neurochem. , vol.102 , pp. 679-685
    • Santillo, M.1    Secondo, A.2    Serù, R.3    Damiano, S.4    Garbi, C.5    Taverna, E.6    Rosa, P.7    Giovedì, S.8    Benfenati, F.9    Mondola, P.10
  • 40
    • 52049125210 scopus 로고    scopus 로고
    • The Cu-Zn superoxide dismutase (SOD1) inhibits ERK phosphorylation by muscarinic receptor modulation in rat pituitary GH3 cells
    • Secondo A., De Mizio M., Zirpoli L., Santillo M., Mondola P. The Cu-Zn superoxide dismutase (SOD1) inhibits ERK phosphorylation by muscarinic receptor modulation in rat pituitary GH3 cells. Biochem. Biophys. Res. Commun. 2008, 376:143-147.
    • (2008) Biochem. Biophys. Res. Commun. , vol.376 , pp. 143-147
    • Secondo, A.1    De Mizio, M.2    Zirpoli, L.3    Santillo, M.4    Mondola, P.5
  • 45
    • 77956404647 scopus 로고    scopus 로고
    • Exosomes: extracellular organelles important in intercellular communication
    • Mathivanan S., Ji H., Simpson R.J. Exosomes: extracellular organelles important in intercellular communication. J. Proteomics 2010, 73:1907-1920.
    • (2010) J. Proteomics , vol.73 , pp. 1907-1920
    • Mathivanan, S.1    Ji, H.2    Simpson, R.J.3
  • 46
    • 68849129712 scopus 로고    scopus 로고
    • Membrane vesicles as conveyors of immune responses
    • Thery C., Ostrowski M., Segura E. Membrane vesicles as conveyors of immune responses. Nat. Rev. Immunol. 2009, 9:581-593.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 581-593
    • Thery, C.1    Ostrowski, M.2    Segura, E.3
  • 47
    • 0036533633 scopus 로고    scopus 로고
    • TCR activation of human T cells induces the production of exosomes bearing the TCR/CD3/ζ complex
    • Blanchard N., Lankar D., Faure F., Regnault A., Dumont C., Raposo G., Hivroz C. TCR activation of human T cells induces the production of exosomes bearing the TCR/CD3/ζ complex. J. Immunol. 2002, 168:3235-3241.
    • (2002) J. Immunol. , vol.168 , pp. 3235-3241
    • Blanchard, N.1    Lankar, D.2    Faure, F.3    Regnault, A.4    Dumont, C.5    Raposo, G.6    Hivroz, C.7
  • 48
    • 0036373780 scopus 로고    scopus 로고
    • CuZn-superoxide dismutase in human thymus: immunocytochemical localisation and secretion in thymus-derived epithelial and fibroblast cell lines
    • Cimini V., Ruggiero G., Buonomo T., Serù R., Sciorio S., Zanzi C., Santangelo F., Mondola P. CuZn-superoxide dismutase in human thymus: immunocytochemical localisation and secretion in thymus-derived epithelial and fibroblast cell lines. Histochem. Cell Biol. 2002, 118:163-169.
    • (2002) Histochem. Cell Biol. , vol.118 , pp. 163-169
    • Cimini, V.1    Ruggiero, G.2    Buonomo, T.3    Serù, R.4    Sciorio, S.5    Zanzi, C.6    Santangelo, F.7    Mondola, P.8
  • 49
    • 0343090850 scopus 로고    scopus 로고
    • Multiple cytokines regulate the expression of extracellular superoxide dismutase in human vascular smooth muscle cells
    • Strålin P., Marklund S.L. Multiple cytokines regulate the expression of extracellular superoxide dismutase in human vascular smooth muscle cells. Atherosclerosis 2000, 151:433-441.
    • (2000) Atherosclerosis , vol.151 , pp. 433-441
    • Strålin, P.1    Marklund, S.L.2
  • 51
    • 78650569645 scopus 로고    scopus 로고
    • Cigarette smoke condensate causes a decrease of the gene expression of Cu-Zn superoxide dismutase, Mn superoxide dismutase, glutathione peroxidase, catalase, and free radical-induced cell injury in SH-SY5Y human neuroblastoma cells
    • Russo M., Cocco S., Secondo A., Adornetto A., Bassi A., Nunziata A., Polichetti G., De Felice B., Damiano S., Serù R., Mondola P., Di Renzo G. Cigarette smoke condensate causes a decrease of the gene expression of Cu-Zn superoxide dismutase, Mn superoxide dismutase, glutathione peroxidase, catalase, and free radical-induced cell injury in SH-SY5Y human neuroblastoma cells. Neurotox. Res. 2011, 19:49-54.
    • (2011) Neurotox. Res. , vol.19 , pp. 49-54
    • Russo, M.1    Cocco, S.2    Secondo, A.3    Adornetto, A.4    Bassi, A.5    Nunziata, A.6    Polichetti, G.7    De Felice, B.8    Damiano, S.9    Serù, R.10    Mondola, P.11    Di Renzo, G.12
  • 52
    • 43249109372 scopus 로고    scopus 로고
    • Isolation and characterization of exosomes from cell culture supernatants and biological fluids
    • Thery C., Amigorena S., Raposo G., Clayton A. Isolation and characterization of exosomes from cell culture supernatants and biological fluids. Curr. Protoc. Cell Biol. 2006, 3:22-30.
    • (2006) Curr. Protoc. Cell Biol. , vol.3 , pp. 22-30
    • Thery, C.1    Amigorena, S.2    Raposo, G.3    Clayton, A.4
  • 53
    • 79953063739 scopus 로고    scopus 로고
    • N-acetyl-L-cysteine increases acute graft-versus-host disease and promotes T-cell-mediated immunity in vitro
    • Karlsson H., Nava S., Remberger M., Hassan Z., Hassan M., Ringde O. N-acetyl-L-cysteine increases acute graft-versus-host disease and promotes T-cell-mediated immunity in vitro. Eur. J. Immunol. 2011, 41:1143-1153.
    • (2011) Eur. J. Immunol. , vol.41 , pp. 1143-1153
    • Karlsson, H.1    Nava, S.2    Remberger, M.3    Hassan, Z.4    Hassan, M.5    Ringde, O.6
  • 55
    • 0018408486 scopus 로고
    • Amines inhibit the clustering of a2-macroglobulin and EGF on the fibroblast cell surface
    • Maxfield F.R., Willingham M.C., Davies P.J., Pastan I. Amines inhibit the clustering of a2-macroglobulin and EGF on the fibroblast cell surface. Nature 1979, 277:661-663.
    • (1979) Nature , vol.277 , pp. 661-663
    • Maxfield, F.R.1    Willingham, M.C.2    Davies, P.J.3    Pastan, I.4
  • 56
    • 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., Finkel T. Requirement for generation of H2O2 for platelet-derived growth factor signal transduction. Science 1995, 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
  • 57
    • 33746541640 scopus 로고    scopus 로고
    • The diverse antioxidant systems of Helicobacter pylori
    • Wang G., Alamuri P., Maier R.J. The diverse antioxidant systems of Helicobacter pylori. Mol. Microbiol. 2006, 61:847-860.
    • (2006) Mol. Microbiol. , vol.61 , pp. 847-860
    • Wang, G.1    Alamuri, P.2    Maier, R.J.3
  • 58
    • 0030979523 scopus 로고    scopus 로고
    • Reactive oxygen species and nitric oxide in viral diseases
    • Peterhans E. Reactive oxygen species and nitric oxide in viral diseases. Biol. Trace Elem. Res. 1997, 56:107-116.
    • (1997) Biol. Trace Elem. Res. , vol.56 , pp. 107-116
    • Peterhans, E.1
  • 60
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley A.J., Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 1992, 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 61
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A. Rho GTPases and the actin cytoskeleton. Science 1998, 279:509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 62
    • 79251582896 scopus 로고    scopus 로고
    • Redox control of GTPases: from molecular mechanisms to functional significance in health and disease
    • Heo J. Redox control of GTPases: from molecular mechanisms to functional significance in health and disease. Antioxid. Redox Signal. 2011, 15:689-724.
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 689-724
    • Heo, J.1
  • 63
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth J.D. NOX enzymes and the biology of reactive oxygen. Nat. Rev. Immunol. 2004, 4:181-189.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 64
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology
    • Bedard K., Krause K.H. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol. Rev. 2007, 87:245-313.
    • (2007) Physiol. Rev. , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 66
    • 60649089324 scopus 로고    scopus 로고
    • Differential role of reactive oxygen species in the activation of mitogen-activated kinases and Akt by key receptors on B-lymphocytes: CD40, the B cell antigen receptor and CXCR4
    • Lee R.L., Westendorf J., Gold M.R. Differential role of reactive oxygen species in the activation of mitogen-activated kinases and Akt by key receptors on B-lymphocytes: CD40, the B cell antigen receptor and CXCR4. J. Cell Commun. Signal 2007, 1:33-43.
    • (2007) J. Cell Commun. Signal , vol.1 , pp. 33-43
    • Lee, R.L.1    Westendorf, J.2    Gold, M.R.3
  • 67
    • 67650457743 scopus 로고    scopus 로고
    • Cytokine-dependent regulation of NADPH oxidase activity and the consequences for activated T cell homeostasis
    • Purushothaman D., Sarin A. Cytokine-dependent regulation of NADPH oxidase activity and the consequences for activated T cell homeostasis. J. Exp. Med. 2009, 206:1515-1523.
    • (2009) J. Exp. Med. , vol.206 , pp. 1515-1523
    • Purushothaman, D.1    Sarin, A.2
  • 68
    • 73249139454 scopus 로고    scopus 로고
    • BCR-induced superoxide negatively regulates B-cell proliferation and T-cell-independent type 2 Ab responses
    • Richards S.M., Clark E.A. BCR-induced superoxide negatively regulates B-cell proliferation and T-cell-independent type 2 Ab responses. Eur. J. Immunol. 2009, 39:3395-3403.
    • (2009) Eur. J. Immunol. , vol.39 , pp. 3395-3403
    • Richards, S.M.1    Clark, E.A.2
  • 69
    • 84655167902 scopus 로고    scopus 로고
    • Modulation of CD40-activated B lymphocytes by N-acetylcysteine involves decreased phosphorylation of STYAT-3
    • Nadeau P.J., Roy A., Gervais-St-Amour C., Marcotte M.-E., Dussault N., Neron S. Modulation of CD40-activated B lymphocytes by N-acetylcysteine involves decreased phosphorylation of STYAT-3. Mol. Immunol. 2012, 49:582-592.
    • (2012) Mol. Immunol. , vol.49 , pp. 582-592
    • Nadeau, P.J.1    Roy, A.2    Gervais-St-Amour, C.3    Marcotte, M.-E.4    Dussault, N.5    Neron, S.6
  • 70
    • 0027417482 scopus 로고
    • Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events
    • Secrist J.P., Burns L.A., Karnitz L., Koretzky G.A., Abraham R.T. Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events. J. Biol. Chem. 1993, 268:5886-5893.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5886-5893
    • Secrist, J.P.1    Burns, L.A.2    Karnitz, L.3    Koretzky, G.A.4    Abraham, R.T.5
  • 71
    • 0029916504 scopus 로고    scopus 로고
    • T cell antigen receptor ubiquitination is a consequence of receptor-mediated tyrosine kinase activation
    • Cenciarelli C., Wilhelm K.G., Guo A., Weissman A.M. T cell antigen receptor ubiquitination is a consequence of receptor-mediated tyrosine kinase activation. J. Biol. Chem. 1996, 271:8709-8713.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8709-8713
    • Cenciarelli, C.1    Wilhelm, K.G.2    Guo, A.3    Weissman, A.M.4
  • 73
    • 84859321043 scopus 로고    scopus 로고
    • Manganese superoxide dismutase: a regulator of T cell activation-induced oxidative signaling and cell death
    • Kamiński M.M., Röth D., Sass S., Sauer S.W., Krammer P.H., Gülow K. Manganese superoxide dismutase: a regulator of T cell activation-induced oxidative signaling and cell death. Biochim. Biophys. Acta 2012, 1823:1041-1052.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 1041-1052
    • Kamiński, M.M.1    Röth, D.2    Sass, S.3    Sauer, S.W.4    Krammer, P.H.5    Gülow, K.6
  • 74
    • 84875147636 scopus 로고    scopus 로고
    • Redox regulation of T-cell function: from molecular mechanisms to significance in human health and disease
    • Kesarwani P., Murali A.K., Al-Khami A.A., Mehrotra S. Redox regulation of T-cell function: from molecular mechanisms to significance in human health and disease. Antioxid. Redox Signal. 2013, 18:1497-1534.
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 1497-1534
    • Kesarwani, P.1    Murali, A.K.2    Al-Khami, A.A.3    Mehrotra, S.4
  • 75
    • 0032843737 scopus 로고    scopus 로고
    • Structure-based functional motif identifies a potential disulfide oxidoreductase active site in the serine/threonine protein phosphatase-1 subfamily
    • Fetrow J.S., Siew N., Skolnick J. Structure-based functional motif identifies a potential disulfide oxidoreductase active site in the serine/threonine protein phosphatase-1 subfamily. FASEB J. 1999, 13:1866-1874.
    • (1999) FASEB J. , vol.13 , pp. 1866-1874
    • Fetrow, J.S.1    Siew, N.2    Skolnick, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.