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Volumn 99, Issue 12, 2007, Pages 677-687

Overexpression of thioredoxin reductase 1 inhibits migration of HEK-293 cells

Author keywords

Cell migration; Diphenyltin; Protein kinase C (PKC); Redox regulation; Thioredoxin reductase (TrxR)

Indexed keywords

DIPHENYLTIN; F ACTIN; OXIDOREDUCTASE; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C ACTIVATOR; PROTEIN KINASE C DELTA; SMALL INTERFERING RNA; THIOREDOXIN REDUCTASE; THIOREDOXIN REDUCTASE 1; THIOREDOXIN REDUCTASE 11; THIOREDOXIN REDUCTASE 15; UNCLASSIFIED DRUG;

EID: 36749003719     PISSN: 02484900     EISSN: None     Source Type: Journal    
DOI: 10.1042/BC20070024     Document Type: Article
Times cited : (31)

References (45)
  • 1
    • 29344437045 scopus 로고    scopus 로고
    • Interplay between the actin cytoskeleton, focal adhesions and microtubules
    • Ridley, A, Peckham, M. and Clark, P, eds, pp, John Willey and Sons, London
    • Ballestrem, C., Magid, N., Zonis, J., Shtutman and Bershadsky, A. (2004) Interplay between the actin cytoskeleton, focal adhesions and microtubules. Cell Motility (Ridley, A., Peckham, M. and Clark, P., eds), pp. 75-99, John Willey and Sons, London
    • (2004) Cell Motility , pp. 75-99
    • Ballestrem, C.1    Magid, N.2    Zonis, J.3    Shtutman4    Bershadsky, A.5
  • 2
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae, H.Z., Chung, S.J. and Rhee, S.G. (1994) Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 269, 27670-27678
    • (1994) J. Biol. Chem , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 3
    • 18144383207 scopus 로고    scopus 로고
    • PTPs versus PTKs: The redox side of the coin
    • Chiarugi, P. (2005) PTPs versus PTKs: the redox side of the coin. Free Radical Res. 39, 353-364
    • (2005) Free Radical Res , vol.39 , pp. 353-364
    • Chiarugi, P.1
  • 5
    • 0035971197 scopus 로고    scopus 로고
    • CD45 negatively regulates monocytic cell differentiation by inhibiting phorbol 12-myristate 13-acetate-dependent activation and tyrosine phosphorylation of protein kinase C delta
    • Deszo, E.L., Brake, D.K., Cengel, K.A., Kelley, K.W. and Freund, G.G. (2001) CD45 negatively regulates monocytic cell differentiation by inhibiting phorbol 12-myristate 13-acetate-dependent activation and tyrosine phosphorylation of protein kinase C delta. J. Biol. Chem. 276, 10212-10217
    • (2001) J. Biol. Chem , vol.276 , pp. 10212-10217
    • Deszo, E.L.1    Brake, D.K.2    Cengel, K.A.3    Kelley, K.W.4    Freund, G.G.5
  • 7
    • 33751279892 scopus 로고    scopus 로고
    • Thioredoxin and protein kinases; in redox signaling
    • Fujino, G., Noguchi, T., Takeda, K. and Ichijo, H. (2006) Thioredoxin and protein kinases; in redox signaling. Semin. Cancer Biol. 16, 427-435
    • (2006) Semin. Cancer Biol , vol.16 , pp. 427-435
    • Fujino, G.1    Noguchi, T.2    Takeda, K.3    Ichijo, H.4
  • 8
    • 0034190297 scopus 로고    scopus 로고
    • Protein kinase C signaling and oxidative stress
    • Gopalakrishna, R. and Jaken, S. (2000) Protein kinase C signaling and oxidative stress. Free Radical Biol. Med. 28, 1349-1361
    • (2000) Free Radical Biol. Med , vol.28 , pp. 1349-1361
    • Gopalakrishna, R.1    Jaken, S.2
  • 9
    • 0035674060 scopus 로고    scopus 로고
    • Protein kinase C as a molecular target for cancer prevention by selenocompounds
    • Gopalakrishna, R. and Gundimeda, U. (2001) Protein kinase C as a molecular target for cancer prevention by selenocompounds. Nutr. Cancer 40, 55-63
    • (2001) Nutr. Cancer , vol.40 , pp. 55-63
    • Gopalakrishna, R.1    Gundimeda, U.2
  • 11
    • 0036587743 scopus 로고    scopus 로고
    • Fas activation opposes PMA-stimulated changes in the localization of PKCδ: A mechanism for reducing neutrophil adhesion to endothelial cells
    • Hendey, B., Zhu, C.L. and Greenstein, S. (2002) Fas activation opposes PMA-stimulated changes in the localization of PKCδ: a mechanism for reducing neutrophil adhesion to endothelial cells. J. Leukocyte Biol. 71, 863-870
    • (2002) J. Leukocyte Biol , vol.71 , pp. 863-870
    • Hendey, B.1    Zhu, C.L.2    Greenstein, S.3
  • 12
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren, A. (1989) Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264, 13963-13966
    • (1989) J. Biol. Chem , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 13
    • 0034534165 scopus 로고    scopus 로고
    • Antioxidant function of thioredoxin and glutaredoxin systems
    • Holmgren, A. (2000) Antioxidant function of thioredoxin and glutaredoxin systems. Antioxid. Redox Signal. 2, 811-820
    • (2000) Antioxid. Redox Signal , vol.2 , pp. 811-820
    • Holmgren, A.1
  • 14
    • 0029753008 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its α subunit
    • Huang, L.E., Arany, Z., Livingston, D.M. and Bunn, H.F. (1996) Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its α subunit. J. Biol. Chem. 271, 32253-32259
    • (1996) J. Biol. Chem , vol.271 , pp. 32253-32259
    • Huang, L.E.1    Arany, Z.2    Livingston, D.M.3    Bunn, H.F.4
  • 15
    • 0033809063 scopus 로고    scopus 로고
    • Protein kinase C isoforms involved in regulation of cell shape and locomotion of human fibrosarcoma HT1080 cells
    • Keller, H.U., Hunziker, I.P., Sordat, B., Niggli, V. and Sroka, J. (2000) Protein kinase C isoforms involved in regulation of cell shape and locomotion of human fibrosarcoma HT1080 cells. Int. J. Cancer. 88, 195-203
    • (2000) Int. J. Cancer , vol.88 , pp. 195-203
    • Keller, H.U.1    Hunziker, I.P.2    Sordat, B.3    Niggli, V.4    Sroka, J.5
  • 18
    • 0037113925 scopus 로고    scopus 로고
    • Zinc release from protein kinase C as the common event during activation by lipid second messenger or reactive oxygen
    • Korichneva, I., Hoyos, B., Chua, R., Levi, E. and Hammerling, U. 2002) Zinc release from protein kinase C as the common event during activation by lipid second messenger or reactive oxygen. J. Biol. Chem. 277, 44327-44331
    • (2002) J. Biol. Chem , vol.277 , pp. 44327-44331
    • Korichneva, I.1    Hoyos, B.2    Chua, R.3    Levi, E.4    Hammerling, U.5
  • 19
    • 27844539756 scopus 로고    scopus 로고
    • Protein kinase C and the regulation of the actin cytoskeleton
    • Larsson, C. (2006) Protein kinase C and the regulation of the actin cytoskeleton. Cell Signal. 18, 276-284
    • (2006) Cell Signal , vol.18 , pp. 276-284
    • Larsson, C.1
  • 20
    • 78651146370 scopus 로고    scopus 로고
    • Laurent, TC., Moore, E.C. and Reichard, P. (1964) Enzymatic synthesis of deoxyribonucleotides. iv. isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli b. J. Biol. Chem. 239, 3436-3444
    • Laurent, TC., Moore, E.C. and Reichard, P. (1964) Enzymatic synthesis of deoxyribonucleotides. iv. isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli b. J. Biol. Chem. 239, 3436-3444
  • 23
    • 0036797413 scopus 로고    scopus 로고
    • Reporter gene transactivation by human p53 is inhibited in thioredoxin reductase null yeast by a mechanism associated with thioredoxin oxidation and independent of changes in the redox state of glutathione
    • Merwin, J.R., Mustacich, D.J., Muller, E.G., Pearson, G.D. and Merrill, G.F. (2002) Reporter gene transactivation by human p53 is inhibited in thioredoxin reductase null yeast by a mechanism associated with thioredoxin oxidation and independent of changes in the redox state of glutathione. Carcinogenesis 23, 1609-1615
    • (2002) Carcinogenesis , vol.23 , pp. 1609-1615
    • Merwin, J.R.1    Mustacich, D.J.2    Muller, E.G.3    Pearson, G.D.4    Merrill, G.F.5
  • 24
    • 29244438457 scopus 로고    scopus 로고
    • Contact stimulation of prostate cancer cell migration: The role of gap junctional coupling and migration stimulated by heterotypic cell-to-cell contacts in determination of the metastatic phenotype of Dunning rat prostate cancer cells
    • Miekus, K., Czernik, M., Sroka, J., Czyz, J. and Madeja, Z. (2005) Contact stimulation of prostate cancer cell migration: the role of gap junctional coupling and migration stimulated by heterotypic cell-to-cell contacts in determination of the metastatic phenotype of Dunning rat prostate cancer cells. Biol Cell. 97, 893-903
    • (2005) Biol Cell , vol.97 , pp. 893-903
    • Miekus, K.1    Czernik, M.2    Sroka, J.3    Czyz, J.4    Madeja, Z.5
  • 27
    • 0034652113 scopus 로고    scopus 로고
    • Thioredoxin reductase
    • Mustacich, D. and Powis, G. (2000) Thioredoxin reductase. Biochem. J. 346, 1-8
    • (2000) Biochem. J , vol.346 , pp. 1-8
    • Mustacich, D.1    Powis, G.2
  • 29
    • 3042602196 scopus 로고    scopus 로고
    • Mitochondrial thioredoxin system: Effects of TrxR2 overexpression on redox balance, cell growth, and apoptosis
    • Patenaude, A., Ven Murthy, M.R. and Mirault, M.E. (2004) Mitochondrial thioredoxin system: effects of TrxR2 overexpression on redox balance, cell growth, and apoptosis. J. Biol. Chem. 279, 27302-27314
    • (2004) J. Biol. Chem , vol.279 , pp. 27302-27314
    • Patenaude, A.1    Ven Murthy, M.R.2    Mirault, M.E.3
  • 30
    • 0028858196 scopus 로고
    • Activation of protein kinase C by trimethyltin: Relevance to neurotoxicity
    • Pavlakovic, G., Kane, M.D., Eyer, C.L., Kanthasamy, A. and Isom, G.E. (1995) Activation of protein kinase C by trimethyltin: relevance to neurotoxicity. J. Neurochem. 65, 2338-2343
    • (1995) J. Neurochem , vol.65 , pp. 2338-2343
    • Pavlakovic, G.1    Kane, M.D.2    Eyer, C.L.3    Kanthasamy, A.4    Isom, G.E.5
  • 32
    • 15044362438 scopus 로고    scopus 로고
    • Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins
    • Rhee, S.G., Kang, S.W., Jeong, W., Chang, TS., Yang, K.S. and Woo, H.A. (2005) Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins. Curr. Opin. Cell Biol. 17, 183-189
    • (2005) Curr. Opin. Cell Biol , vol.17 , pp. 183-189
    • Rhee, S.G.1    Kang, S.W.2    Jeong, W.3    Chang, T.S.4    Yang, K.S.5    Woo, H.A.6
  • 33
    • 1242338754 scopus 로고    scopus 로고
    • Rundlof, A.K., Janard, M., Miranda-Vizuete, A. and and Arner, E.S. (2004) Evidence for intriguingly complex transcription of human thioredoxin reductase 1. Free Radical Biol. Med. 36, 641-656
    • Rundlof, A.K., Janard, M., Miranda-Vizuete, A. and and Arner, E.S. (2004) Evidence for intriguingly complex transcription of human thioredoxin reductase 1. Free Radical Biol. Med. 36, 641-656
  • 34
    • 2442498430 scopus 로고    scopus 로고
    • Stimulus-specific differences in protein kinase Cδ localization and activation mechanisms in cardiomyocytes
    • Rybin, V.O., Guo, J., Sabri, A., Elouardighi, H., Schaefer, E. and Steinberg, S.F. (2004) Stimulus-specific differences in protein kinase Cδ localization and activation mechanisms in cardiomyocytes. J. Biol. Chem. 279, 19350-19361
    • (2004) J. Biol. Chem , vol.279 , pp. 19350-19361
    • Rybin, V.O.1    Guo, J.2    Sabri, A.3    Elouardighi, H.4    Schaefer, E.5    Steinberg, S.F.6
  • 36
    • 0028344541 scopus 로고
    • Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-kB and AP-1
    • Schenk, H., Klein, M., Erdbrugger, W., Droge, W. and Schulze-Osthoff, K. (1994) Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-kB and AP-1. Proc. Natl. Acad. Sci. U.S.A. 91, 1672-1676
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 1672-1676
    • Schenk, H.1    Klein, M.2    Erdbrugger, W.3    Droge, W.4    Schulze-Osthoff, K.5
  • 37
    • 0037010617 scopus 로고    scopus 로고
    • Folic acid, ascorbic acid and sodium selenite restore the motility of Dictyostelium discoideum inhibited by triethyllead
    • Sroka, J., Madeja, Z., Michalik, M., Przestalski, S. and Korohoda, W. (2002) Folic acid, ascorbic acid and sodium selenite restore the motility of Dictyostelium discoideum inhibited by triethyllead. Toxicology 180, 275-292
    • (2002) Toxicology , vol.180 , pp. 275-292
    • Sroka, J.1    Madeja, Z.2    Michalik, M.3    Przestalski, S.4    Korohoda, W.5
  • 38
    • 12744261583 scopus 로고    scopus 로고
    • Thioredoxin reductase, regulates angiogenesis by increasing endothelial cell-derived vascular endothelial growth factor
    • Streicher, K.L., Sylte, M.J., Johnson, S.E. and Sordillo, L.M. (2004) Thioredoxin reductase, regulates angiogenesis by increasing endothelial cell-derived vascular endothelial growth factor. Nutr. Cancer 50, 221-231
    • (2004) Nutr. Cancer , vol.50 , pp. 221-231
    • Streicher, K.L.1    Sylte, M.J.2    Johnson, S.E.3    Sordillo, L.M.4
  • 39
    • 0034677930 scopus 로고    scopus 로고
    • Interaction between protein kinase Cδ and the c-Abl tyrosine kinase in the cellular response to oxidative stress
    • Sun, X., Wu, F, Datta, R., Kharbanda, S. and Kufe, D. (2000) Interaction between protein kinase Cδ and the c-Abl tyrosine kinase in the cellular response to oxidative stress. J. Biol. Chem. 275, 7470-7473
    • (2000) J. Biol. Chem , vol.275 , pp. 7470-7473
    • Sun, X.1    Wu, F.2    Datta, R.3    Kharbanda, S.4    Kufe, D.5
  • 42
    • 0033569457 scopus 로고    scopus 로고
    • Phage display identifies thioredoxin and superoxide dismutase as novel protein kinase C-interacting proteins: Thioredoxin inhibits protein kinase C-mediated phosphorylation of histone
    • Watson, J.A., Rumsby, M.G. and Wolowacz, R.G. (1999) Phage display identifies thioredoxin and superoxide dismutase as novel protein kinase C-interacting proteins: thioredoxin inhibits protein kinase C-mediated phosphorylation of histone. Biochem. J. 343, 301-305
    • (1999) Biochem. J , vol.343 , pp. 301-305
    • Watson, J.A.1    Rumsby, M.G.2    Wolowacz, R.G.3
  • 43
    • 0032963835 scopus 로고    scopus 로고
    • Role of protein kinase C isoforms in locomotion of Walker 256 carcinosarcoma cells
    • Wicki, A. and Niggli, V. (1999) Role of protein kinase C isoforms in locomotion of Walker 256 carcinosarcoma cells. Int. J. Cancer. 81, 255-261
    • (1999) Int. J. Cancer , vol.81 , pp. 255-261
    • Wicki, A.1    Niggli, V.2


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