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Volumn 587, Issue 10, 2013, Pages 1579-1586

Sodium tungstate modulates ATM function upon DNA damage

Author keywords

Antitumoral; DNA damage; Double strand break; Phosphatase inhibition

Indexed keywords

ATM PROTEIN; ETOPOSIDE; MRE11 PROTEIN; NIBRIN; PHLEOMYCIN; PP2A PROTEIN; RAD50 PROTEIN; TUNGSTATE SODIUM; TUNGSTEN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84877751798     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.04.003     Document Type: Article
Times cited : (10)

References (49)
  • 1
    • 77950505810 scopus 로고    scopus 로고
    • Anticancer drug development: The grand challenges
    • Hait, W. N. (2010) Anticancer drug development: the grand challenges. Nat. Rev. Drug Discov. 9, 253-254.
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 253-254
    • Hait, W.N.1
  • 2
    • 34548324267 scopus 로고    scopus 로고
    • The impact of FDA and EMEA guidelines on drug development in relation to phase 0 trials
    • S. Marchetti, and J.H. Schellens The impact of FDA and EMEA guidelines on drug development in relation to phase 0 trials Br. J. Cancer 97 2007 577 581
    • (2007) Br. J. Cancer , vol.97 , pp. 577-581
    • Marchetti, S.1    Schellens, J.H.2
  • 3
    • 36949026694 scopus 로고    scopus 로고
    • Activation and regulation of ATM kinase activity in response to DNA double-strand breaks
    • J.H. Lee, and T.T. Paull Activation and regulation of ATM kinase activity in response to DNA double-strand breaks Oncogene 26 2007 7741 7748
    • (2007) Oncogene , vol.26 , pp. 7741-7748
    • Lee, J.H.1    Paull, T.T.2
  • 4
    • 84866177058 scopus 로고    scopus 로고
    • Current neoadjuvant treatment options for HER2-positive breast cancer
    • Abdel-Razeq, H. and Marei, L. (2011) Current neoadjuvant treatment options for HER2-positive breast cancer. Biologics 5, 87-94.
    • (2011) Biologics , vol.5 , pp. 87-94
    • Abdel-Razeq, H.1    Marei, L.2
  • 5
    • 79955859969 scopus 로고    scopus 로고
    • Adjuvants for enhancing the immunogenicity of whole tumor cell vaccines
    • Chiang, C.L., Kandalaft, L.E. and Coukos, G. (2011) Adjuvants for enhancing the immunogenicity of whole tumor cell vaccines. Int. Rev. Immunol. 30, 150-182.
    • (2011) Int. Rev. Immunol. , vol.30 , pp. 150-182
    • Chiang, C.L.1    Kandalaft, L.E.2    Coukos, G.3
  • 8
    • 0036693750 scopus 로고    scopus 로고
    • Vanadium and tungsten derivatives as antidiabetic agents: A review of their toxic effects
    • J.L. Domingo Vanadium and tungsten derivatives as antidiabetic agents: a review of their toxic effects Biol. Trace Elem. Res. 88 2002 97 112
    • (2002) Biol. Trace Elem. Res. , vol.88 , pp. 97-112
    • Domingo, J.L.1
  • 9
    • 0035061253 scopus 로고    scopus 로고
    • Tungstate is an effective antidiabetic agent in streptozotocin-induced diabetic rats: A long-term study
    • A. Barbera, R.R. Gomis, N. Prats, J.E. Rodriguez-Gil, and M. Domingo Tungstate is an effective antidiabetic agent in streptozotocin-induced diabetic rats: a long-term study Diabetologia 44 2001 507 513
    • (2001) Diabetologia , vol.44 , pp. 507-513
    • Barbera, A.1    Gomis, R.R.2    Prats, N.3    Rodriguez-Gil, J.E.4    Domingo, M.5
  • 10
    • 0031019298 scopus 로고    scopus 로고
    • Effects of tungstate in neonatally streptozotocin-induced diabetic rats: Mechanism leading to normalization of glycaemia
    • A. Barbera, J. Fernandez-Alvarez, A. Truc, R. Gomis, and J.J. Guinovart Effects of tungstate in neonatally streptozotocin-induced diabetic rats: mechanism leading to normalization of glycaemia Diabetologia 40 1997 143 149
    • (1997) Diabetologia , vol.40 , pp. 143-149
    • Barbera, A.1    Fernandez-Alvarez, J.2    Truc, A.3    Gomis, R.4    Guinovart, J.J.5
  • 11
    • 0028128179 scopus 로고
    • Insulin-like actions of tungstate in diabetic rats. Normalization of hepatic glucose metabolism
    • A. Barbera, J.E. Rodriguez-Gil, and J.J. Guinovart Insulin-like actions of tungstate in diabetic rats. Normalization of hepatic glucose metabolism J. Biol. Chem. 269 1994 20047 20053
    • (1994) J. Biol. Chem. , vol.269 , pp. 20047-20053
    • Barbera, A.1    Rodriguez-Gil, J.E.2    Guinovart, J.J.3
  • 12
    • 0035149832 scopus 로고    scopus 로고
    • Effects of tungstate, a new potential oral antidiabetic agent, in Zucker diabetic fatty rats
    • M.C. Munoz, A. Barbera, J. Dominguez, J. Fernandez-Alvarez, and R. Gomis Effects of tungstate, a new potential oral antidiabetic agent, in Zucker diabetic fatty rats Diabetes 50 2001 131 138
    • (2001) Diabetes , vol.50 , pp. 131-138
    • Munoz, M.C.1    Barbera, A.2    Dominguez, J.3    Fernandez-Alvarez, J.4    Gomis, R.5
  • 13
    • 24944511514 scopus 로고    scopus 로고
    • Tungstate decreases weight gain and adiposity in obese rats through increased thermogenesis and lipid oxidation
    • M. Claret, H. Corominola, I. Canals, J. Saura, and S. Barcelo-Batllori Tungstate decreases weight gain and adiposity in obese rats through increased thermogenesis and lipid oxidation Endocrinology 146 2005 4362 4369
    • (2005) Endocrinology , vol.146 , pp. 4362-4369
    • Claret, M.1    Corominola, H.2    Canals, I.3    Saura, J.4    Barcelo-Batllori, S.5
  • 14
    • 0029583122 scopus 로고
    • Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate
    • M.P. Egloff, P.T. Cohen, P. Reinemer, and D. Barford Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate J. Mol. Biol. 254 1995 942 959
    • (1995) J. Mol. Biol. , vol.254 , pp. 942-959
    • Egloff, M.P.1    Cohen, P.T.2    Reinemer, P.3    Barford, D.4
  • 15
    • 0029780526 scopus 로고    scopus 로고
    • The X-ray crystal structures of Yersinia tyrosine phosphatase with bound tungstate and nitrate. Mechanistic implications
    • E.B. Fauman, C. Yuvaniyama, H.L. Schubert, J.A. Stuckey, and M.A. Saper The X-ray crystal structures of Yersinia tyrosine phosphatase with bound tungstate and nitrate. Mechanistic implications J. Biol. Chem. 271 1996 18780 18788
    • (1996) J. Biol. Chem. , vol.271 , pp. 18780-18788
    • Fauman, E.B.1    Yuvaniyama, C.2    Schubert, H.L.3    Stuckey, J.A.4    Saper, M.A.5
  • 16
  • 17
    • 0028122711 scopus 로고
    • Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Å and the complex with tungstate
    • J.A. Stuckey, H.L. Schubert, E.B. Fauman, Z.Y. Zhang, and J.E. Dixon Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Å and the complex with tungstate Nature 370 1994 571 575
    • (1994) Nature , vol.370 , pp. 571-575
    • Stuckey, J.A.1    Schubert, H.L.2    Fauman, E.B.3    Zhang, Z.Y.4    Dixon, J.E.5
  • 18
    • 84856221597 scopus 로고    scopus 로고
    • Anti-diabetic and anti-obesity agent sodium tungstate enhances GCN pathway activation through Glc7p inhibition
    • Rodriguez-Hernandez, C.J., Guinovart, J.J. and Murguia, J.R. (2012) Anti-diabetic and anti-obesity agent sodium tungstate enhances GCN pathway activation through Glc7p inhibition. FEBS Lett. 586, 270-276.
    • (2012) FEBS Lett. , vol.586 , pp. 270-276
    • Rodriguez-Hernandez, C.J.1    Guinovart, J.J.2    Murguia, J.R.3
  • 19
    • 77957269135 scopus 로고    scopus 로고
    • Proof-of-concept trial on the efficacy of sodium tungstate in human obesity
    • Hanzu, F., Gomis, R., Coves, M.J., Viaplana, J., Palomo, M., et al. (2010) Proof-of-concept trial on the efficacy of sodium tungstate in human obesity. Diabetes Obes. Metab. 12, 1013-1018.
    • (2010) Diabetes Obes. Metab. , vol.12 , pp. 1013-1018
    • Hanzu, F.1    Gomis, R.2    Coves, M.J.3    Viaplana, J.4    Palomo, M.5
  • 20
    • 84877749299 scopus 로고    scopus 로고
    • Guide to Yeast Genetics and Molecular Cell Biology
    • C. Guthrie, G.R. Fink, Methods in Enzymology Academic Press New York
    • W. Prinz Guide to Yeast Genetics and Molecular Cell Biology C. Guthrie, G.R. Fink, Guide to Yeast Genetics and Molecular Cell Biology, Part B Methods in Enzymology vol. 350 2003 Academic Press New York
    • (2003) Guide to Yeast Genetics and Molecular Cell Biology, Part B , vol.350
    • Prinz, W.1
  • 21
    • 0346156075 scopus 로고    scopus 로고
    • Checkpoint failure and chromosomal instability without lymphomagenesis in Mre11(ATLD1/ATLD1) mice
    • J.W. Theunissen, M.I. Kaplan, P.A. Hunt, B.R. Williams, and D.O. Ferguson Checkpoint failure and chromosomal instability without lymphomagenesis in Mre11(ATLD1/ATLD1) mice Mol. Cell. 12 2003 1511 1523
    • (2003) Mol. Cell. , vol.12 , pp. 1511-1523
    • Theunissen, J.W.1    Kaplan, M.I.2    Hunt, P.A.3    Williams, B.R.4    Ferguson, D.O.5
  • 22
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • T. Mosmann Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays J. Immunol. Methods 65 1983 55 63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 24
    • 0021154718 scopus 로고
    • Isolation and characterization of rabbit skeletal muscle protein phosphatases C-I and C-II
    • S.R. Silberman, M. Speth, R. Nemani, M.K. Ganapathi, and V. Dombradi Isolation and characterization of rabbit skeletal muscle protein phosphatases C-I and C-II J. Biol. Chem. 259 1984 2913 2922
    • (1984) J. Biol. Chem. , vol.259 , pp. 2913-2922
    • Silberman, S.R.1    Speth, M.2    Nemani, R.3    Ganapathi, M.K.4    Dombradi, V.5
  • 25
    • 0036261707 scopus 로고    scopus 로고
    • Sensing and repairing DNA double-strand breaks
    • S.P. Jackson Sensing and repairing DNA double-strand breaks Carcinogenesis 23 2002 687 696
    • (2002) Carcinogenesis , vol.23 , pp. 687-696
    • Jackson, S.P.1
  • 26
    • 70449642870 scopus 로고    scopus 로고
    • Type II topoisomerases-inhibitors, repair mechanisms and mutations
    • P. Heisig Type II topoisomerases-inhibitors, repair mechanisms and mutations Mutagenesis 24 2009 465 469
    • (2009) Mutagenesis , vol.24 , pp. 465-469
    • Heisig, P.1
  • 27
    • 7644232348 scopus 로고    scopus 로고
    • Requirement of the Mre11 complex and exonuclease 1 for activation of the Mec1 signaling pathway
    • D. Nakada, Y. Hirano, and K. Sugimoto Requirement of the Mre11 complex and exonuclease 1 for activation of the Mec1 signaling pathway Mol. Cell. Biol. 24 2004 10016 10025
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10016-10025
    • Nakada, D.1    Hirano, Y.2    Sugimoto, K.3
  • 28
    • 34247483506 scopus 로고    scopus 로고
    • ATM activation and DNA damage response
    • M.F. Lavin, and S. Kozlov ATM activation and DNA damage response Cell Cycle 6 2007 931 942
    • (2007) Cell Cycle , vol.6 , pp. 931-942
    • Lavin, M.F.1    Kozlov, S.2
  • 29
    • 2942687831 scopus 로고    scopus 로고
    • Phosphorylation of SMC1 is a critical downstream event in the ATM-NBS1-BRCA1 pathway
    • R. Kitagawa, C.J. Bakkenist, P.J. McKinnon, and M.B. Kastan Phosphorylation of SMC1 is a critical downstream event in the ATM-NBS1-BRCA1 pathway Genes Dev. 18 2004 1423 1438
    • (2004) Genes Dev. , vol.18 , pp. 1423-1438
    • Kitagawa, R.1    Bakkenist, C.J.2    McKinnon, P.J.3    Kastan, M.B.4
  • 30
    • 50849141104 scopus 로고    scopus 로고
    • Early events in the mammalian response to DNA double-strand breaks
    • L.C. Riches, A.M. Lynch, and N.J. Gooderham Early events in the mammalian response to DNA double-strand breaks Mutagenesis 23 2008 331 339
    • (2008) Mutagenesis , vol.23 , pp. 331-339
    • Riches, L.C.1    Lynch, A.M.2    Gooderham, N.J.3
  • 31
    • 1042301303 scopus 로고    scopus 로고
    • Requirement of protein phosphatase 5 in DNA-damage-induced ATM activation
    • A. Ali, J. Zhang, S. Bao, I. Liu, and D. Otterness Requirement of protein phosphatase 5 in DNA-damage-induced ATM activation Genes Dev. 18 2004 249 254
    • (2004) Genes Dev. , vol.18 , pp. 249-254
    • Ali, A.1    Zhang, J.2    Bao, S.3    Liu, I.4    Otterness, D.5
  • 32
    • 10044225999 scopus 로고    scopus 로고
    • Autophosphorylation of ataxia-telangiectasia mutated is regulated by protein phosphatase 2A
    • A.A. Goodarzi, J.C. Jonnalagadda, P. Douglas, D. Young, and R. Ye Autophosphorylation of ataxia-telangiectasia mutated is regulated by protein phosphatase 2A EMBO J. 23 2004 4451 4461
    • (2004) EMBO J. , vol.23 , pp. 4451-4461
    • Goodarzi, A.A.1    Jonnalagadda, J.C.2    Douglas, P.3    Young, D.4    Ye, R.5
  • 33
    • 0024592297 scopus 로고
    • Effects of the tumour promoter okadaic acid on intracellular protein phosphorylation and metabolism
    • T.A. Haystead, A.T. Sim, D. Carling, R.C. Honnor, and Y. Tsukitani Effects of the tumour promoter okadaic acid on intracellular protein phosphorylation and metabolism Nature 337 1989 78 81
    • (1989) Nature , vol.337 , pp. 78-81
    • Haystead, T.A.1    Sim, A.T.2    Carling, D.3    Honnor, R.C.4    Tsukitani, Y.5
  • 34
    • 0142011461 scopus 로고    scopus 로고
    • The cellular response to DNA double-strand breaks: Defining the sensors and mediators
    • J.H. Petrini, and T.H. Stracker The cellular response to DNA double-strand breaks: defining the sensors and mediators Trends Cell Biol. 13 2003 458 462
    • (2003) Trends Cell Biol. , vol.13 , pp. 458-462
    • Petrini, J.H.1    Stracker, T.H.2
  • 35
    • 0034854142 scopus 로고    scopus 로고
    • Checkpoint activation in response to double-strand breaks requires the Mre11/Rad50/Xrs2 complex
    • M. Grenon, C. Gilbert, and N.F. Lowndes Checkpoint activation in response to double-strand breaks requires the Mre11/Rad50/Xrs2 complex Nat. Cell Biol. 3 2001 844 847
    • (2001) Nat. Cell Biol. , vol.3 , pp. 844-847
    • Grenon, M.1    Gilbert, C.2    Lowndes, N.F.3
  • 36
    • 0034612307 scopus 로고    scopus 로고
    • A mechanistic basis for Mre11-directed DNA joining at microhomologies
    • T.T. Paull, and M. Gellert A mechanistic basis for Mre11-directed DNA joining at microhomologies Proc. Natl. Acad. Sci. USA 97 2000 6409 6414
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6409-6414
    • Paull, T.T.1    Gellert, M.2
  • 37
    • 34548492016 scopus 로고    scopus 로고
    • MRE11-RAD50-NBS1 and ATM function as co-mediators of TRF1 in telomere length control
    • Y. Wu, S. Xiao, and X.D. Zhu MRE11-RAD50-NBS1 and ATM function as co-mediators of TRF1 in telomere length control Nat. Struct. Mol. Biol. 14 2007 832 840
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 832-840
    • Wu, Y.1    Xiao, S.2    Zhu, X.D.3
  • 38
    • 0034749425 scopus 로고    scopus 로고
    • DNA damage-dependent nuclear dynamics of the Mre11 complex
    • O.K. Mirzoeva, and J.H. Petrini DNA damage-dependent nuclear dynamics of the Mre11 complex Mol. Cell. Biol. 21 2001 281 288
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 281-288
    • Mirzoeva, O.K.1    Petrini, J.H.2
  • 39
  • 40
    • 0142186242 scopus 로고    scopus 로고
    • The MRN complex: Coordinating and mediating the response to broken chromosomes
    • M. van den Bosch, R.T. Bree, and N.F. Lowndes The MRN complex: coordinating and mediating the response to broken chromosomes EMBO Rep. 4 2003 844 849
    • (2003) EMBO Rep. , vol.4 , pp. 844-849
    • Van Den Bosch, M.1    Bree, R.T.2    Lowndes, N.F.3
  • 41
    • 56649086648 scopus 로고    scopus 로고
    • Aberrations of the MRE11-RAD50-NBS1 DNA damage sensor complex in human breast cancer: MRE11 as a candidate familial cancer-predisposing gene
    • J. Bartkova, J. Tommiska, L. Oplustilova, K. Aaltonen, and A. Tamminen Aberrations of the MRE11-RAD50-NBS1 DNA damage sensor complex in human breast cancer: MRE11 as a candidate familial cancer-predisposing gene Mol. Oncol. 2 2008 296 316
    • (2008) Mol. Oncol. , vol.2 , pp. 296-316
    • Bartkova, J.1    Tommiska, J.2    Oplustilova, L.3    Aaltonen, K.4    Tamminen, A.5
  • 42
    • 0141923141 scopus 로고    scopus 로고
    • Altered expression of DNA double-strand break detection and repair proteins in breast carcinomas
    • S. Angele, I. Treilleux, A. Bremond, P. Taniere, and J. Hall Altered expression of DNA double-strand break detection and repair proteins in breast carcinomas Histopathology 43 2003 347 353
    • (2003) Histopathology , vol.43 , pp. 347-353
    • Angele, S.1    Treilleux, I.2    Bremond, A.3    Taniere, P.4    Hall, J.5
  • 44
    • 79953000069 scopus 로고    scopus 로고
    • Protein phosphatase 2A as a potential target for anticancer therapy
    • Kalev, P. and Sablina, A.A. (2011) Protein phosphatase 2A as a potential target for anticancer therapy. Anti-cancer Agents Med. Chem. 11, 38-46.
    • (2011) Anti-cancer Agents Med. Chem. , vol.11 , pp. 38-46
    • Kalev, P.1    Sablina, A.A.2
  • 45
    • 0032931844 scopus 로고    scopus 로고
    • The nuclease activity of Mre11 is required for meiosis but not for mating type switching, end joining, or telomere maintenance
    • S. Moreau, J.R. Ferguson, and L.S. Symington The nuclease activity of Mre11 is required for meiosis but not for mating type switching, end joining, or telomere maintenance Mol. Cell. Biol. 19 1999 556 566
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 556-566
    • Moreau, S.1    Ferguson, J.R.2    Symington, L.S.3
  • 48
    • 0032079366 scopus 로고    scopus 로고
    • RAD9 and RAD24 define two additive, interacting branches of the DNA damage checkpoint pathway in budding yeast normally required for Rad53 modification and activation
    • M.A. de la Torre-Ruiz, C.M. Green, and N.F. Lowndes RAD9 and RAD24 define two additive, interacting branches of the DNA damage checkpoint pathway in budding yeast normally required for Rad53 modification and activation EMBO J. 17 1998 2687 2698
    • (1998) EMBO J. , vol.17 , pp. 2687-2698
    • De La Torre-Ruiz, M.A.1    Green, C.M.2    Lowndes, N.F.3
  • 49
    • 0035449349 scopus 로고    scopus 로고
    • The yeast Xrs2 complex functions in S phase checkpoint regulation
    • D. D'Amours, and S.P. Jackson The yeast Xrs2 complex functions in S phase checkpoint regulation Genes Dev. 15 2001 2238 2249
    • (2001) Genes Dev. , vol.15 , pp. 2238-2249
    • D'Amours, D.1    Jackson, S.P.2


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