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Volumn 7, Issue 11, 2008, Pages 1580-1586

Identification and characterization of a novel Mdm2 splice variant acutely induced by the chemotherapeutic agents adriamycin and actinomycin D

Author keywords

Adriamycin; Alternative mRNA splicing; DNA damage; mdm2

Indexed keywords

CYCLOHEXIMIDE; DACTINOMYCIN; DOXORUBICIN; ETOPOSIDE; MESSENGER RNA; PROTEIN MDM2; PROTEIN P53;

EID: 45849130152     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.7.11.5985     Document Type: Article
Times cited : (9)

References (58)
  • 2
    • 4043181214 scopus 로고    scopus 로고
    • Cancer genes and the pathways they control
    • Vogelstein B, Kinzler KW. Cancer genes and the pathways they control. Nature medicine 2004; 10:789-99.
    • (2004) Nature medicine , vol.10 , pp. 789-799
    • Vogelstein, B.1    Kinzler, K.W.2
  • 5
    • 14644437751 scopus 로고    scopus 로고
    • MDM2 is a central node in the p53 pathway: 12 years and counting
    • Bond GL, Hu W, Levine AJ. MDM2 is a central node in the p53 pathway: 12 years and counting. Current cancer drug targets 2005; 5:3-8.
    • (2005) Current cancer drug targets , vol.5 , pp. 3-8
    • Bond, G.L.1    Hu, W.2    Levine, A.J.3
  • 6
    • 0033655386 scopus 로고    scopus 로고
    • Taubert H, Koehler T, Meye A, Bartel F, Lautenschlager C, Borchert S, Bache M, Schmidt H, Wurl P. mdm2 mRNA level is a prognostic factor in soft tissue sarcoma. Molecular medicine (Cambridge, Mass) 2000; 6:50-9.
    • Taubert H, Koehler T, Meye A, Bartel F, Lautenschlager C, Borchert S, Bache M, Schmidt H, Wurl P. mdm2 mRNA level is a prognostic factor in soft tissue sarcoma. Molecular medicine (Cambridge, Mass) 2000; 6:50-9.
  • 7
    • 0026649648 scopus 로고
    • The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation
    • Momand J, Zambetti GP, Olson DC, George D, Levine AJ. The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell 1992; 69:1237-45.
    • (1992) Cell , vol.69 , pp. 1237-1245
    • Momand, J.1    Zambetti, G.P.2    Olson, D.C.3    George, D.4    Levine, A.J.5
  • 8
    • 0032475878 scopus 로고    scopus 로고
    • Signaling to p53: Breaking the MDM2-p53 circuit
    • Prives C. Signaling to p53: breaking the MDM2-p53 circuit. Cell 1998; 95:5-8.
    • (1998) Cell , vol.95 , pp. 5-8
    • Prives, C.1
  • 11
    • 34147187341 scopus 로고    scopus 로고
    • Coutts AS, La Thangue NB. Mdm2 widens its repertoire. Cell Cycle 2007; 6:827-9.
    • Coutts AS, La Thangue NB. Mdm2 widens its repertoire. Cell Cycle 2007; 6:827-9.
  • 12
    • 0001510491 scopus 로고    scopus 로고
    • The RB and p53 pathways in cancer
    • Sherr CJ, McCormick F. The RB and p53 pathways in cancer. Cancer Cell 2002; 2:103.
    • (2002) Cancer Cell , vol.2 , pp. 103
    • Sherr, C.J.1    McCormick, F.2
  • 13
    • 34248185454 scopus 로고    scopus 로고
    • Efeyan A, Serrano M. p53: guardian of the genome and policeman of the oncogenes. Cell Cycle 2007; 6:1006-10.
    • Efeyan A, Serrano M. p53: guardian of the genome and policeman of the oncogenes. Cell Cycle 2007; 6:1006-10.
  • 14
    • 0041696480 scopus 로고    scopus 로고
    • p53 - guardian of a genome's guardian?
    • Rubbi CP, Milner J. p53 - guardian of a genome's guardian? Cell Cycle 2003; 2:20-1.
    • (2003) Cell Cycle , vol.2 , pp. 20-21
    • Rubbi, C.P.1    Milner, J.2
  • 15
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda R, Tanaka H, Yasuda H. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS letters 1997; 420:25-7.
    • (1997) FEBS letters , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 16
    • 40549099702 scopus 로고    scopus 로고
    • Unlocking the Mdm2-p53 loop: Ubiquitin is the key
    • Clegg HV, Itahana K, Zhang Y. Unlocking the Mdm2-p53 loop: Ubiquitin is the key. Cell Cycle 2007; 7.
    • (2007) Cell Cycle , pp. 7
    • Clegg, H.V.1    Itahana, K.2    Zhang, Y.3
  • 17
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y, Maya R, Kazaz A, Oren M. Mdm2 promotes the rapid degradation of p53. Nature 1997; 387:296-9.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 18
  • 20
    • 0027501841 scopus 로고
    • Wild type p53 can mediate sequence-specific transactivation of an internal promoter within the mdm2 gene
    • Juven T, Barak Y, Zauberman A, George DL, Oren M. Wild type p53 can mediate sequence-specific transactivation of an internal promoter within the mdm2 gene. Oncogene 1993; 8:3411-6.
    • (1993) Oncogene , vol.8 , pp. 3411-3416
    • Juven, T.1    Barak, Y.2    Zauberman, A.3    George, D.L.4    Oren, M.5
  • 21
    • 0027459198 scopus 로고
    • mdm2 expression is induced by wild type p53 activity
    • Barak Y, Juven T, Haffner R, Oren M. mdm2 expression is induced by wild type p53 activity. The EMBO journal 1993; 12:461-8.
    • (1993) The EMBO journal , vol.12 , pp. 461-468
    • Barak, Y.1    Juven, T.2    Haffner, R.3    Oren, M.4
  • 22
    • 0027244853 scopus 로고
    • The p53-mdm-2 autoregulatory feedback loop
    • Wu X, Bayle JH, Olson D, Levine AJ. The p53-mdm-2 autoregulatory feedback loop. Genes Dev 1993; 7:1126-32.
    • (1993) Genes Dev , vol.7 , pp. 1126-1132
    • Wu, X.1    Bayle, J.H.2    Olson, D.3    Levine, A.J.4
  • 23
    • 0029131447 scopus 로고
    • A functional p53-responsive intronic promoter is contained within the human mdm2 gene
    • Zauberman A, Flusberg D, Haupt Y, Barak Y, Oren M. A functional p53-responsive intronic promoter is contained within the human mdm2 gene. Nucleic Acids Res 1995; 23:2584-92.
    • (1995) Nucleic Acids Res , vol.23 , pp. 2584-2592
    • Zauberman, A.1    Flusberg, D.2    Haupt, Y.3    Barak, Y.4    Oren, M.5
  • 24
    • 0027248782 scopus 로고
    • Sequence-specific DNA binding by p53: Identification of target sites and lack of binding to p53-MDM2 complexes
    • Zauberman A, Barak Y, Ragimov N, Levy N, Oren M. Sequence-specific DNA binding by p53: identification of target sites and lack of binding to p53-MDM2 complexes. The EMBO journal 1993; 12:2799-808.
    • (1993) The EMBO journal , vol.12 , pp. 2799-2808
    • Zauberman, A.1    Barak, Y.2    Ragimov, N.3    Levy, N.4    Oren, M.5
  • 25
    • 25444513462 scopus 로고    scopus 로고
    • Steady states and oscillations in the p53/Mdm2 network
    • Ciliberto A, Novak B, Tyson JJ. Steady states and oscillations in the p53/Mdm2 network. Cell Cycle 2005; 4:488-93.
    • (2005) Cell Cycle , vol.4 , pp. 488-493
    • Ciliberto, A.1    Novak, B.2    Tyson, J.J.3
  • 26
    • 13144294031 scopus 로고    scopus 로고
    • Dynamics in the p53-Mdm2 ubiquitination pathway
    • Brooks CL, Gu W. Dynamics in the p53-Mdm2 ubiquitination pathway. Cell Cycle 2004; 3:895-9.
    • (2004) Cell Cycle , vol.3 , pp. 895-899
    • Brooks, C.L.1    Gu, W.2
  • 27
    • 0029849620 scopus 로고    scopus 로고
    • Cancer cell cycles
    • Sherr CJ. Cancer cell cycles. Science 1996; 274:1672.
    • (1996) Science , vol.274 , pp. 1672
    • Sherr, C.J.1
  • 28
    • 0032191393 scopus 로고    scopus 로고
    • Tumor surveillance via the ARF-p53 pathway
    • Sherr CJ. Tumor surveillance via the ARF-p53 pathway. Genes Dev 1998; 12:2984.
    • (1998) Genes Dev , vol.12 , pp. 2984
    • Sherr, C.J.1
  • 30
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones SN, Roe AE, Donehower LA, Bradley A. Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53. Nature 1995; 378:206-8.
    • (1995) Nature , vol.378 , pp. 206-208
    • Jones, S.N.1    Roe, A.E.2    Donehower, L.A.3    Bradley, A.4
  • 31
    • 0029824669 scopus 로고    scopus 로고
    • Alternatively spliced mdm2 transcripts with loss of p53 binding domain sequences: Transforming ability and frequent detection in human cancer
    • Sigalas I, Calvert AH, Anderson JJ, Neal DE, Lunec J. Alternatively spliced mdm2 transcripts with loss of p53 binding domain sequences: transforming ability and frequent detection in human cancer. Nature medicine 1996; 2:912-7.
    • (1996) Nature medicine , vol.2 , pp. 912-917
    • Sigalas, I.1    Calvert, A.H.2    Anderson, J.J.3    Neal, D.E.4    Lunec, J.5
  • 32
    • 0029590161 scopus 로고
    • MDM2 transformation in the absence of p53 and abrogation of the p107 G1 cell cycle arrest
    • Dubs-Poterszman MC, Tocque B, Wasylyk B. MDM2 transformation in the absence of p53 and abrogation of the p107 G1 cell cycle arrest. Oncogene 1995; 11:2445-9.
    • (1995) Oncogene , vol.11 , pp. 2445-2449
    • Dubs-Poterszman, M.C.1    Tocque, B.2    Wasylyk, B.3
  • 33
  • 34
    • 0036655060 scopus 로고    scopus 로고
    • Alternative and aberrant splicing of MDM2 mRNA in human cancer
    • Bartel F, Taubert H, Harris LC. Alternative and aberrant splicing of MDM2 mRNA in human cancer. Cancer Cell 2002; 2:9-15.
    • (2002) Cancer Cell , vol.2 , pp. 9-15
    • Bartel, F.1    Taubert, H.2    Harris, L.C.3
  • 36
    • 33750378188 scopus 로고    scopus 로고
    • Genotoxic stress induces coordinately regulated alternative splicing of the p53 modulators MDM2 and MDM4
    • Chandler DS, Singh RK, Caldwell LC, Bitler JL, Lozano G. Genotoxic stress induces coordinately regulated alternative splicing of the p53 modulators MDM2 and MDM4. Cancer research 2006; 66:9502-8.
    • (2006) Cancer research , vol.66 , pp. 9502-9508
    • Chandler, D.S.1    Singh, R.K.2    Caldwell, L.C.3    Bitler, J.L.4    Lozano, G.5
  • 42
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • Fang S, Jensen JP, Ludwig RL, Vousden KH, Weissman AM. Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J Biol Chem 2000; 275:8945-51.
    • (2000) J Biol Chem , vol.275 , pp. 8945-8951
    • Fang, S.1    Jensen, J.P.2    Ludwig, R.L.3    Vousden, K.H.4    Weissman, A.M.5
  • 43
    • 0032512057 scopus 로고    scopus 로고
    • Mdm2 association with p53 targets its ubiquitination
    • Fuchs SY, Adler V, Buschmann T, Wu X, Ronai Z. Mdm2 association with p53 targets its ubiquitination. Oncogene 1998; 17:2543-7.
    • (1998) Oncogene , vol.17 , pp. 2543-2547
    • Fuchs, S.Y.1    Adler, V.2    Buschmann, T.3    Wu, X.4    Ronai, Z.5
  • 44
    • 0021672811 scopus 로고
    • Cardiac actin is the major actin gene product in skeletal muscle cell differentiation in vitro
    • Bains W, Ponte P, Blau H, Kedes L. Cardiac actin is the major actin gene product in skeletal muscle cell differentiation in vitro. Mol Cell Biol 1984; 4:1449-53.
    • (1984) Mol Cell Biol , vol.4 , pp. 1449-1453
    • Bains, W.1    Ponte, P.2    Blau, H.3    Kedes, L.4
  • 46
    • 0026794026 scopus 로고
    • Transferrin conjugates of adriamycin are cytotoxic without intercalating nuclear DNA
    • Barabas K, Sizensky JA, Faulk WP. Transferrin conjugates of adriamycin are cytotoxic without intercalating nuclear DNA. J Biol Chem 1992; 267:9437-42.
    • (1992) J Biol Chem , vol.267 , pp. 9437-9442
    • Barabas, K.1    Sizensky, J.A.2    Faulk, W.P.3
  • 47
    • 0025220562 scopus 로고
    • Inhibition of transcription by adriamycin is a consequence of the loss of negative superhelicity in DNA mediated by topoisomerase II
    • Tarr M, van Helden PD. Inhibition of transcription by adriamycin is a consequence of the loss of negative superhelicity in DNA mediated by topoisomerase II. Molecular and cellular biochemistry 1990; 93:141-6.
    • (1990) Molecular and cellular biochemistry , vol.93 , pp. 141-146
    • Tarr, M.1    van Helden, P.D.2
  • 48
    • 0023693619 scopus 로고
    • Relationships between physicochemical and biological properties in a series of oxazolopyridocarbazole derivatives (OPCd); comparison with related anti-tumor agents
    • Auclair C, Schwaller MA, Rene B, Banoun H, Saucier JM, Larsen AK. Relationships between physicochemical and biological properties in a series of oxazolopyridocarbazole derivatives (OPCd); comparison with related anti-tumor agents. Anti-cancer drug design 1988; 3:133-44.
    • (1988) Anti-cancer drug design , vol.3 , pp. 133-144
    • Auclair, C.1    Schwaller, M.A.2    Rene, B.3    Banoun, H.4    Saucier, J.M.5    Larsen, A.K.6
  • 49
    • 0031926679 scopus 로고    scopus 로고
    • Actinomycin D inhibits human immunodeficiency virus type 1 minus-strand transfer in in vitro and endogenous reverse transcriptase assays
    • Guo J, Wu T, Bess J, Henderson LE, Levin JG. Actinomycin D inhibits human immunodeficiency virus type 1 minus-strand transfer in in vitro and endogenous reverse transcriptase assays. Journal of virology 1998; 72:6716-24.
    • (1998) Journal of virology , vol.72 , pp. 6716-6724
    • Guo, J.1    Wu, T.2    Bess, J.3    Henderson, L.E.4    Levin, J.G.5
  • 50
    • 0029879748 scopus 로고    scopus 로고
    • Sequence-specific actinomycin D binding to single-stranded DNA inhibits HIV reverse transcriptase and other polymerases
    • Rill RL, Hecker KH. Sequence-specific actinomycin D binding to single-stranded DNA inhibits HIV reverse transcriptase and other polymerases. Biochemistry 1996; 35:3525-33.
    • (1996) Biochemistry , vol.35 , pp. 3525-3533
    • Rill, R.L.1    Hecker, K.H.2
  • 51
    • 0034956117 scopus 로고    scopus 로고
    • Actinomycin D binding to unstructured, single-stranded DNA
    • Yoo H, Rill RL. Actinomycin D binding to unstructured, single-stranded DNA. J Mol Recognit 2001; 14:145-50.
    • (2001) J Mol Recognit , vol.14 , pp. 145-150
    • Yoo, H.1    Rill, R.L.2
  • 52
    • 0032403061 scopus 로고    scopus 로고
    • The mechanism of actinomycin Dmediated inhibition of HIV-1 reverse transcription
    • Jeeninga RE, Huthoff HT, Gultyaev AP, Berkhout B. The mechanism of actinomycin Dmediated inhibition of HIV-1 reverse transcription. Nucleic Acids Res 1998; 26:5472-9.
    • (1998) Nucleic Acids Res , vol.26 , pp. 5472-5479
    • Jeeninga, R.E.1    Huthoff, H.T.2    Gultyaev, A.P.3    Berkhout, B.4
  • 53
    • 0032491180 scopus 로고    scopus 로고
    • Actinomycin D inhibition of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase and nucleocapsid protein
    • Davis WR, Gabbara S, Hupe D, Peliska JA. Actinomycin D inhibition of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase and nucleocapsid protein. Biochemistry 1998; 37:14213-21.
    • (1998) Biochemistry , vol.37 , pp. 14213-14221
    • Davis, W.R.1    Gabbara, S.2    Hupe, D.3    Peliska, J.A.4
  • 54
    • 0018803120 scopus 로고
    • Qualitative and quantitative aspects of intercalator-induced DNA strand breaks
    • Ross WE, Glaubiger D, Kohn KW. Qualitative and quantitative aspects of intercalator-induced DNA strand breaks. Biochimica et biophysica acta 1979; 562:41-50.
    • (1979) Biochimica et biophysica acta , vol.562 , pp. 41-50
    • Ross, W.E.1    Glaubiger, D.2    Kohn, K.W.3
  • 55
    • 0016785079 scopus 로고
    • Continuous induction of chromatid lesions by DNA-intercalating compounds
    • Hsu TC, Pathak S, Kusyk CJ. Continuous induction of chromatid lesions by DNA-intercalating compounds. Mutation research 1975; 33:417-20.
    • (1975) Mutation research , vol.33 , pp. 417-420
    • Hsu, T.C.1    Pathak, S.2    Kusyk, C.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.