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Volumn 615, Issue 1-2, 2007, Pages 66-74

Inhibition of telomerase activity by reduction of poly(ADP-ribosyl)ation of TERT and TEP1/TP1 expression in HeLa cells with knocked down poly(ADP-ribose) polymerase-1 (PARP-1) gene

Author keywords

HeLa; NAD+; PAR; PARP; Poly(ADP ribosyl)ation; siRNA; Telomerase; TEP1 TP1; TERT

Indexed keywords

HOLOENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE INHIBITOR; POLY(ADENOSINE DIPHOSPHATE RIBOSE); PROTEIN; PROTEIN TEP1; PROTEIN TP1; SMALL INTERFERING RNA; TELOMERASE; TELOMERASE REVERSE TRANSCRIPTASE; UNCLASSIFIED DRUG;

EID: 33845987725     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2006.10.002     Document Type: Article
Times cited : (17)

References (28)
  • 2
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in regulation of nuclear functions
    • D'Amours D., Denoyers S., D'Silva I., and Poirier G.G. Poly(ADP-ribosyl)ation reactions in regulation of nuclear functions. Biochem. J. 342 (1999) 249-268
    • (1999) Biochem. J. , vol.342 , pp. 249-268
    • D'Amours, D.1    Denoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 4
    • 0035833257 scopus 로고    scopus 로고
    • Normal telomere length and chromosomal end capping in poly(ADP-ribose) polymerase-deficient mice and primary cells despite increased chromosomal instability
    • Samper E., Goytisolo F.A., Menissier-de Murcia J., Gonzalez-Suarez E., Cigudosa J.C., de Murcia G., and Blasco M.A. Normal telomere length and chromosomal end capping in poly(ADP-ribose) polymerase-deficient mice and primary cells despite increased chromosomal instability. J. Cell Biol. 154 (2001) 49-60
    • (2001) J. Cell Biol. , vol.154 , pp. 49-60
    • Samper, E.1    Goytisolo, F.A.2    Menissier-de Murcia, J.3    Gonzalez-Suarez, E.4    Cigudosa, J.C.5    de Murcia, G.6    Blasco, M.A.7
  • 5
    • 2042429168 scopus 로고    scopus 로고
    • Regulation of telomerase by telomeric proteins
    • Smogorzewska A., and de Lange T. Regulation of telomerase by telomeric proteins. Annu. Rev. Biochem. 73 (2004) 177-208
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 177-208
    • Smogorzewska, A.1    de Lange, T.2
  • 6
    • 33745375693 scopus 로고    scopus 로고
    • PARP1 Is a TRF2-associated poly(ADP-ribose)polymerase and protects eroded telomeres
    • (Epub 2006 January 25)
    • Gomez M., Wu J., Schreiber V., Dunlap J., Dantzer F., Wang Y., and Liu Y. PARP1 Is a TRF2-associated poly(ADP-ribose)polymerase and protects eroded telomeres. Mol. Biol. Cell. 17 April (4) (2006) 1686-1696 (Epub 2006 January 25)
    • (2006) Mol. Biol. Cell. , vol.17 , Issue.April 4 , pp. 1686-1696
    • Gomez, M.1    Wu, J.2    Schreiber, V.3    Dunlap, J.4    Dantzer, F.5    Wang, Y.6    Liu, Y.7
  • 8
    • 2942539327 scopus 로고    scopus 로고
    • Vault poly(ADP-ribose) polymerase is associated with mammalian telomerase and is dispensable for telomerase function and vault structure in vivo
    • Liu Y., Snow B.E., Kickhoefer V.A., Erdmann N., Zhou W., Wakeham A., Gomez M., Rome L.H., and Harrington L. Vault poly(ADP-ribose) polymerase is associated with mammalian telomerase and is dispensable for telomerase function and vault structure in vivo. Mol. Cell. Biol. 24 (2004) 5314-5323
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5314-5323
    • Liu, Y.1    Snow, B.E.2    Kickhoefer, V.A.3    Erdmann, N.4    Zhou, W.5    Wakeham, A.6    Gomez, M.7    Rome, L.H.8    Harrington, L.9
  • 9
    • 0036373860 scopus 로고    scopus 로고
    • Differential regulation of telomerase activity by six telomerase subunits
    • Chang J.T., Chen Y.L., Yang H.T., Chen C.Y., and Cheng A.J. Differential regulation of telomerase activity by six telomerase subunits. Eur. J. Biochem. 269 (2002) 3442-3450
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3442-3450
    • Chang, J.T.1    Chen, Y.L.2    Yang, H.T.3    Chen, C.Y.4    Cheng, A.J.5
  • 10
    • 23844466265 scopus 로고    scopus 로고
    • Benzamide and 4-amino 1,8 naphthalimide (NAP) treatment inhibit telomerase activity by down-regulating the expression of telomerase associated protein (TEP1/TP1) and inhibing the poly(ADP-ribosyl)ation of TERT in cultured cells
    • Ghosh U., and Bhattacharyya N.P. Benzamide and 4-amino 1,8 naphthalimide (NAP) treatment inhibit telomerase activity by down-regulating the expression of telomerase associated protein (TEP1/TP1) and inhibing the poly(ADP-ribosyl)ation of TERT in cultured cells. FEBS J. 272 (2005) 4237-4238
    • (2005) FEBS J. , vol.272 , pp. 4237-4238
    • Ghosh, U.1    Bhattacharyya, N.P.2
  • 12
    • 0031590739 scopus 로고    scopus 로고
    • Inhibition of telomerase activity by PKC inhibitors in human nasopharyngeal cancer cells in culture
    • Ku W.C., Cheng A.J., and Wang T.C.V. Inhibition of telomerase activity by PKC inhibitors in human nasopharyngeal cancer cells in culture. Biochem. Biophys. Res. Commun. 241 (1997) 730-736
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 730-736
    • Ku, W.C.1    Cheng, A.J.2    Wang, T.C.V.3
  • 13
    • 0032509350 scopus 로고    scopus 로고
    • Telomerase is controlled by protein kinase C alpha in human breast cancer cell
    • Li H., Zhao L.L., Yang Z.Y., Funder J.W., and Liu J.P. Telomerase is controlled by protein kinase C alpha in human breast cancer cell. J. Biol. Chem. 273 (1998) 33436-33442
    • (1998) J. Biol. Chem. , vol.273 , pp. 33436-33442
    • Li, H.1    Zhao, L.L.2    Yang, Z.Y.3    Funder, J.W.4    Liu, J.P.5
  • 14
    • 0034731455 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins
    • Pleschke J.M., Kleczkowska H.E., Strohm M., and Althaus F.R. Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins. J. Biol. Chem. 275 (2000) 40974-40980
    • (2000) J. Biol. Chem. , vol.275 , pp. 40974-40980
    • Pleschke, J.M.1    Kleczkowska, H.E.2    Strohm, M.3    Althaus, F.R.4
  • 15
    • 85047697807 scopus 로고    scopus 로고
    • TERT regulates cell survival independent of telomerase enzymatic activity
    • Cao Y., Li H., Deb S., and Liu J.P. TERT regulates cell survival independent of telomerase enzymatic activity. Oncogene 21 (2002) 3130-3138
    • (2002) Oncogene , vol.21 , pp. 3130-3138
    • Cao, Y.1    Li, H.2    Deb, S.3    Liu, J.P.4
  • 17
    • 0842324496 scopus 로고    scopus 로고
    • An enzymatic assay for poly(ADP-ribose) polymerase-1 (PARP-1) via the chemical quantitation of NAD+: application to the high-throughput screening of small molecules as potential inhibitors
    • Putt K.S., and Hergenrother P.J. An enzymatic assay for poly(ADP-ribose) polymerase-1 (PARP-1) via the chemical quantitation of NAD+: application to the high-throughput screening of small molecules as potential inhibitors. Anal. Biochem. 326 (2004) 78-86
    • (2004) Anal. Biochem. , vol.326 , pp. 78-86
    • Putt, K.S.1    Hergenrother, P.J.2
  • 18
    • 0041573041 scopus 로고    scopus 로고
    • + repletion prevents PARP-1-induced glycolytic blockade and cell death in cultured mouse astrocytes
    • + repletion prevents PARP-1-induced glycolytic blockade and cell death in cultured mouse astrocytes. Biochem. Biophys. Res. Commun. 308 (2003) 809-813
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 809-813
    • Ying, W.1    Garnier, P.2    Swanson, R.A.3
  • 19
    • 0028276094 scopus 로고
    • Nitric oxide toxicity in islet cells involves poly(ADP-ribose) polymerase activation and concomitant NAD+ depletion
    • Radons J., Heller B., and Burkle A. Nitric oxide toxicity in islet cells involves poly(ADP-ribose) polymerase activation and concomitant NAD+ depletion. Biochem. Biophys. Res. Commun. 199 (1994) 1270-1277
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 1270-1277
    • Radons, J.1    Heller, B.2    Burkle, A.3
  • 20
    • 3543058091 scopus 로고    scopus 로고
    • RNA interference directed against Poly(ADP-Ribose) polymerase 1 efficiently suppresses human immunodeficiency virus type 1 replication in human cells
    • Kameoka M., Nukuzuma S., Itaya A., Tanaka Y., Ota K., Ikuta K., and Yoshihara K. RNA interference directed against Poly(ADP-Ribose) polymerase 1 efficiently suppresses human immunodeficiency virus type 1 replication in human cells. J. Virol. 78 16 (2004) 8931-8934
    • (2004) J. Virol. , vol.78 , Issue.16 , pp. 8931-8934
    • Kameoka, M.1    Nukuzuma, S.2    Itaya, A.3    Tanaka, Y.4    Ota, K.5    Ikuta, K.6    Yoshihara, K.7
  • 21
    • 0037114679 scopus 로고    scopus 로고
    • Specific interference with gene expression and gene function mediated by long dsRNA in neural cells
    • Gan L., Anton K.E., Masterson B.A., Vincent V.A., Ye S., and Gonzalez-Zulueta M. Specific interference with gene expression and gene function mediated by long dsRNA in neural cells. J. Neurosci. Methods 121 2 (2002) 151-157
    • (2002) J. Neurosci. Methods , vol.121 , Issue.2 , pp. 151-157
    • Gan, L.1    Anton, K.E.2    Masterson, B.A.3    Vincent, V.A.4    Ye, S.5    Gonzalez-Zulueta, M.6
  • 22
    • 0038219534 scopus 로고    scopus 로고
    • Functional interaction between PARP-1 and PARP-2 in chromosome stability and embryonic development in mouse
    • de Murcia J.M., Ricoul M., and Tartier L. Functional interaction between PARP-1 and PARP-2 in chromosome stability and embryonic development in mouse. EMBO J. 22 (2003) 2255-2263
    • (2003) EMBO J. , vol.22 , pp. 2255-2263
    • de Murcia, J.M.1    Ricoul, M.2    Tartier, L.3
  • 23
    • 0034647345 scopus 로고    scopus 로고
    • 2+-dependent endonuclease in apoptosis and its inhibition by poly(ADP-ribose) polymerase
    • 2+-dependent endonuclease in apoptosis and its inhibition by poly(ADP-ribose) polymerase. J. Biol. Chem. 275 (2000) 21302-21308
    • (2000) J. Biol. Chem. , vol.275 , pp. 21302-21308
    • Yakovlev, A.G.1    Wang, G.2    Stoica, B.A.3
  • 26
    • 0037206608 scopus 로고    scopus 로고
    • Differential gene expression in γ-irradiated BALB/3T3 fibriblasts under the influence of 3-aminobenzamide, an inhibitor of parp enzyme
    • Cardoso R.S., Espanhol A.R., Passos G.A.S., and Sakamoto-Hojo E.T. Differential gene expression in γ-irradiated BALB/3T3 fibriblasts under the influence of 3-aminobenzamide, an inhibitor of parp enzyme. Mutat. Res. 508 (2002) 33-40
    • (2002) Mutat. Res. , vol.508 , pp. 33-40
    • Cardoso, R.S.1    Espanhol, A.R.2    Passos, G.A.S.3    Sakamoto-Hojo, E.T.4
  • 28
    • 0026506694 scopus 로고
    • Noncovalent interactions of poly(adenosine diphosphate ribose) with histones
    • Panzeter P.L., Realini C.A., and Althaus F.R. Noncovalent interactions of poly(adenosine diphosphate ribose) with histones. Biochemistry 31 (1992) 1379-1385
    • (1992) Biochemistry , vol.31 , pp. 1379-1385
    • Panzeter, P.L.1    Realini, C.A.2    Althaus, F.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.