메뉴 건너뛰기




Volumn 313, Issue 13, 2007, Pages 2753-2765

Tyrosine kinase inhibitor, methyl 2,5-dihydromethylcinnimate, induces PML nuclear body formation and apoptosis in tumor cells

Author keywords

[No Author keywords available]

Indexed keywords

METHYL 2,5 DIHYDROMETHYLCINNIMATE; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN P53; PROTEIN TYROSINE KINASE INHIBITOR; SUMO 1 PROTEIN; UNCLASSIFIED DRUG;

EID: 34547143196     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2007.03.032     Document Type: Article
Times cited : (6)

References (55)
  • 2
    • 0028179010 scopus 로고
    • A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein
    • Dyck J.A., Maul G.G., Miller Jr. W.H., Chen J.D., Kakizuka A., and Evans R.M. A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell 76 (1994) 333-343
    • (1994) Cell , vol.76 , pp. 333-343
    • Dyck, J.A.1    Maul, G.G.2    Miller Jr., W.H.3    Chen, J.D.4    Kakizuka, A.5    Evans, R.M.6
  • 3
    • 0028158682 scopus 로고
    • Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells
    • Weis K., Rambaud S., Lavau C., Jansen J., Carvalho T., Carmo-Fonseca M., Lamond A., and Dejean A. Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells. Cell 76 (1994) 345-356
    • (1994) Cell , vol.76 , pp. 345-356
    • Weis, K.1    Rambaud, S.2    Lavau, C.3    Jansen, J.4    Carvalho, T.5    Carmo-Fonseca, M.6    Lamond, A.7    Dejean, A.8
  • 6
    • 0036966365 scopus 로고    scopus 로고
    • Mobile foci of Sp100 do not contain PML: PML bodies are immobile but PML and Sp100 proteins are not
    • Wiesmeijer K., Molenaar C., Bekeer I.M., Tanke H.J., and Dirks R.W. Mobile foci of Sp100 do not contain PML: PML bodies are immobile but PML and Sp100 proteins are not. J. Struct. Biol. 140 (2002) 180-188
    • (2002) J. Struct. Biol. , vol.140 , pp. 180-188
    • Wiesmeijer, K.1    Molenaar, C.2    Bekeer, I.M.3    Tanke, H.J.4    Dirks, R.W.5
  • 7
    • 0035969111 scopus 로고    scopus 로고
    • Pathways of retinoic acid- or arsenic trioxide-induced PML/RARalpha catabolism, role of oncogene degradation in disease remission
    • Zhu J., Lallemand-Breitenbach V., and de The H. Pathways of retinoic acid- or arsenic trioxide-induced PML/RARalpha catabolism, role of oncogene degradation in disease remission. Oncogene 20 (2001) 7257-7265
    • (2001) Oncogene , vol.20 , pp. 7257-7265
    • Zhu, J.1    Lallemand-Breitenbach, V.2    de The, H.3
  • 9
    • 0033952527 scopus 로고    scopus 로고
    • Sequestration and inhibition of Daxx-mediated transcriptional repression by PML
    • Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.J., and Chen J.D. Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol. Cell. Biol. 20 (2000) 1784-1796
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1784-1796
    • Li, H.1    Leo, C.2    Zhu, J.3    Wu, X.4    O'Neil, J.5    Park, E.J.6    Chen, J.D.7
  • 10
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • Zhong S., Salomoni P., and Pandolfi P.P. The transcriptional role of PML and the nuclear body. Nat. Cell Biol. 2 (2000) E85-E90
    • (2000) Nat. Cell Biol. , vol.2
    • Zhong, S.1    Salomoni, P.2    Pandolfi, P.P.3
  • 11
    • 0035969103 scopus 로고    scopus 로고
    • DNA viruses and viral proteins that interact with PML nuclear bodies
    • Everett R.D. DNA viruses and viral proteins that interact with PML nuclear bodies. Oncogene 20 (2001) 7266-7273
    • (2001) Oncogene , vol.20 , pp. 7266-7273
    • Everett, R.D.1
  • 12
    • 0035969127 scopus 로고    scopus 로고
    • Role and fate of PML nuclear bodies in response to interferon and viral infections
    • Regad T., and Chelbi-Alix M.K. Role and fate of PML nuclear bodies in response to interferon and viral infections. Oncogene 20 (2001) 7274-7286
    • (2001) Oncogene , vol.20 , pp. 7274-7286
    • Regad, T.1    Chelbi-Alix, M.K.2
  • 13
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppression
    • Salomoni P., and Pandolfi P.P. The role of PML in tumor suppression. Cell 108 (2002) 165-170
    • (2002) Cell , vol.108 , pp. 165-170
    • Salomoni, P.1    Pandolfi, P.P.2
  • 14
    • 0035897415 scopus 로고    scopus 로고
    • Regulation and localization of the Bloom syndrome protein in response to DNA damage
    • Bischof O., Kim S.H., Irving J., Beresten S., Ellis N.A., and Campisi J. Regulation and localization of the Bloom syndrome protein in response to DNA damage. J. Cell Biol. 153 (2001) 367-380
    • (2001) J. Cell Biol. , vol.153 , pp. 367-380
    • Bischof, O.1    Kim, S.H.2    Irving, J.3    Beresten, S.4    Ellis, N.A.5    Campisi, J.6
  • 15
    • 0037979238 scopus 로고    scopus 로고
    • PML colocalizes with and stabilizes the DNA damage response protein TopBPI
    • Xu Z.X., Timanova-Atanasova A., Zhao R.X., and Chang K.S. PML colocalizes with and stabilizes the DNA damage response protein TopBPI. Mol. Cell. Biol. 23 (2003) 4247-4256
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4247-4256
    • Xu, Z.X.1    Timanova-Atanasova, A.2    Zhao, R.X.3    Chang, K.S.4
  • 24
    • 0035265823 scopus 로고    scopus 로고
    • PUMA induces the rapid apoptosis of colorectal cancer cells
    • Yu J., Zhang L., Hwang P.M., Kinzler K.W., and Vogelstein B. PUMA induces the rapid apoptosis of colorectal cancer cells. Mol. Cell 7 (2001) 673-682
    • (2001) Mol. Cell , vol.7 , pp. 673-682
    • Yu, J.1    Zhang, L.2    Hwang, P.M.3    Kinzler, K.W.4    Vogelstein, B.5
  • 25
    • 0035265686 scopus 로고    scopus 로고
    • PUMA, a novel proapoptotic gene, is induced by p53
    • Nakano K., and Vousden K.H. PUMA, a novel proapoptotic gene, is induced by p53. Mol. Cell 7 (2001) 683-694
    • (2001) Mol. Cell , vol.7 , pp. 683-694
    • Nakano, K.1    Vousden, K.H.2
  • 28
    • 0029818553 scopus 로고    scopus 로고
    • Altered retinoic acid receptors
    • de The H. Altered retinoic acid receptors. FASEB J. 10 (1996) 955-960
    • (1996) FASEB J. , vol.10 , pp. 955-960
    • de The, H.1
  • 33
    • 15644368249 scopus 로고    scopus 로고
    • Covalent modification of PML by the sentrin family of ubiquitin-like proteins
    • Kamitani T., Nguyen H.P., Kito K., Fukuda-Kamitani T., and Yeh E.T. Covalent modification of PML by the sentrin family of ubiquitin-like proteins. J. Biol. Chem. 273 (1998) 3117-3120
    • (1998) J. Biol. Chem. , vol.273 , pp. 3117-3120
    • Kamitani, T.1    Nguyen, H.P.2    Kito, K.3    Fukuda-Kamitani, T.4    Yeh, E.T.5
  • 34
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson E.S. Protein modification by SUMO. Annu. Rev. Biochem. 73 (2004) 355-382
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 35
    • 45149137825 scopus 로고
    • Inhibition of epidermal growth factor-induced DNA synthesis by tyrosine kinase inhibitors
    • Umezawa K., Hori T., Tajima H., Imoto M., Isshiki K., and Takeuchi T. Inhibition of epidermal growth factor-induced DNA synthesis by tyrosine kinase inhibitors. FEBS Lett. 260 (1990) 198-200
    • (1990) FEBS Lett. , vol.260 , pp. 198-200
    • Umezawa, K.1    Hori, T.2    Tajima, H.3    Imoto, M.4    Isshiki, K.5    Takeuchi, T.6
  • 41
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Muller S., Matunis M.J., and Dejean A. Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17 (1998) 61-70
    • (1998) EMBO J. , vol.17 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 45
  • 46
    • 0026085376 scopus 로고
    • Induction of morphological change by tyrosine kinase inhibitors in Rous sarcoma virus-transformed rat kidney cells
    • Umezawa K., Tanaka K., Hori T., Abe S., Sekizawa R., and Imoto M. Induction of morphological change by tyrosine kinase inhibitors in Rous sarcoma virus-transformed rat kidney cells. FEBS Lett. 279 (1991) 132-136
    • (1991) FEBS Lett. , vol.279 , pp. 132-136
    • Umezawa, K.1    Tanaka, K.2    Hori, T.3    Abe, S.4    Sekizawa, R.5    Imoto, M.6
  • 47
    • 0036847998 scopus 로고    scopus 로고
    • PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2
    • Yang S., Kuo C., Bisi J.E., and Kim M.K. PML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2. Nat. Cell Biol. 4 (2002) 865-870
    • (2002) Nat. Cell Biol. , vol.4 , pp. 865-870
    • Yang, S.1    Kuo, C.2    Bisi, J.E.3    Kim, M.K.4
  • 49
    • 0034695883 scopus 로고    scopus 로고
    • Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis
    • Zhong S., Salomoni P., Ronchetti S., Guo A., Ruggero D., and Pandolfi P.P. Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis. J. Exp. Med. 191 (2000) 631-640
    • (2000) J. Exp. Med. , vol.191 , pp. 631-640
    • Zhong, S.1    Salomoni, P.2    Ronchetti, S.3    Guo, A.4    Ruggero, D.5    Pandolfi, P.P.6
  • 50
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh S.Y., Ikeda M., Taya Y., and Prives C. DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell 91 (1997) 325-334
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 52
    • 0032931517 scopus 로고    scopus 로고
    • The p53 pathway
    • Prives C., and Hall P.A. The p53 pathway. J. Pathol. 187 (1999) 112-126
    • (1999) J. Pathol. , vol.187 , pp. 112-126
    • Prives, C.1    Hall, P.A.2
  • 53
    • 0035835820 scopus 로고    scopus 로고
    • Regulation of p53 function
    • Woods D.B., and Vousden K.H. Regulation of p53 function. Exp. Cell Res. 264 (2001) 56-66
    • (2001) Exp. Cell Res. , vol.264 , pp. 56-66
    • Woods, D.B.1    Vousden, K.H.2
  • 54
    • 0032192140 scopus 로고    scopus 로고
    • The complexity of p53 modulation: emerging patterns from divergent signals
    • Giaccia A.J., and Kastan M.B. The complexity of p53 modulation: emerging patterns from divergent signals. Genes Dev. 12 (1998) 2973-2983
    • (1998) Genes Dev. , vol.12 , pp. 2973-2983
    • Giaccia, A.J.1    Kastan, M.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.