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Volumn 47, Issue 4, 2014, Pages 221-226

Nutlin-3 downregulates p53 phosphorylation on serine392 and induces apoptosis in hepatocellular carcinoma cells

Author keywords

Apoptosis; Human hepatocellular carcinoma; Nutlin 3; P53

Indexed keywords

ANTINEOPLASTIC AGENT; IMIDAZOLE DERIVATIVE; NUTLIN 3; PHOSPHOSERINE; PIPERAZINE DERIVATIVE; PROTEIN P53;

EID: 84899650084     PISSN: 19766696     EISSN: 1976670X     Source Type: Journal    
DOI: 10.5483/BMBRep.2014.47.4.146     Document Type: Article
Times cited : (13)

References (34)
  • 2
    • 33747830764 scopus 로고    scopus 로고
    • Hepatocellular carcinoma pathogenesis: from genes to environment
    • Farazi, P. A. and DePinho, R. A. (2006) Hepatocellular carcinoma pathogenesis: from genes to environment. Nat. Rev. Cancer 6, 674-687.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 674-687
    • Farazi, P.A.1    Depinho, R.A.2
  • 3
    • 34047207337 scopus 로고    scopus 로고
    • TP53 mutations in human cancers:functional selection and impact on cancer prognosis and outcomes
    • Petitjean, A., Achatz, M., Borresen-Dale, A., Hainaut, P. and Olivier, M. (2007) TP53 mutations in human cancers:functional selection and impact on cancer prognosis and outcomes. Oncogene 26, 2157-2165.
    • (2007) Oncogene , vol.26 , pp. 2157-2165
    • Petitjean, A.1    Achatz, M.2    Borresen-dale, A.3    Hainaut, P.4    Olivier, M.5
  • 4
    • 0035586616 scopus 로고    scopus 로고
    • Structural Origin for the Transcriptional Activity of Human p 53
    • Lee, S. H. (2001) Structural Origin for the Transcriptional Activity of Human p 53. BMB Rep. 34, 73-79.
    • (2001) BMB Rep. , vol.34 , pp. 73-79
    • Lee, S.H.1
  • 5
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt, Y., Maya, R., Kazaz, A. and Oren, M. (1997) Mdm2 promotes the rapid degradation of p53. Nature 387, 296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 6
    • 0348134742 scopus 로고    scopus 로고
    • Mono-versus polyubiquitination: differential control of p53 fate by Mdm2
    • Li, M., Brooks, C. L., Wu-Baer, F., Chen, D., Baer, R. and Gu, W. (2003) Mono-versus polyubiquitination: differential control of p53 fate by Mdm2. Science 302, 1972-1975.
    • (2003) Science , vol.302 , pp. 1972-1975
    • Li, M.1    Brooks, C.L.2    Wu-Baer, F.3    Chen, D.4    Baer, R.5    Gu, W.6
  • 8
    • 43949107925 scopus 로고    scopus 로고
    • SnapShot: p53 posttranslational modifications
    • Kruse, J. P. and Gu, W. (2008) SnapShot: p53 posttranslational modifications. Cell 133, 930.
    • (2008) Cell , vol.133 , pp. 930
    • Kruse, J.P.1    Gu, W.2
  • 9
    • 71349083173 scopus 로고    scopus 로고
    • Phosphorylation of serine 392 in p53 is a common and integral event during p53 induction by diverse stimuli
    • Cox, M. L. and Meek, D. W. (2010) Phosphorylation of serine 392 in p53 is a common and integral event during p53 induction by diverse stimuli. Cell. Signal. 22, 564-571.
    • (2010) Cell. Signal. , vol.22 , pp. 564-571
    • Cox, M.L.1    Meek, D.W.2
  • 11
    • 0030790778 scopus 로고    scopus 로고
    • Phosphorylation of serine 392 stabilizes the tetramer formation of tumor suppressor protein p53
    • Sakaguchi, K., Sakamoto, H., Lewis, M. S., Anderson, C. W., Erickson, J. W., Appella, E. and Xie, D. (1997) Phosphorylation of serine 392 stabilizes the tetramer formation of tumor suppressor protein p53. Biochemistry 36, 10117-10124.
    • (1997) Biochemistry , vol.36 , pp. 10117-10124
    • Sakaguchi, K.1    Sakamoto, H.2    Lewis, M.S.3    Anderson, C.W.4    Erickson, J.W.5    Appella, E.6    Xie, D.7
  • 12
    • 0038795317 scopus 로고    scopus 로고
    • Hypoxia attenuates the p53 response to cellular damage
    • Achison, M. and Hupp, T. R. (2003) Hypoxia attenuates the p53 response to cellular damage. Oncogene 22, 3431-3440.
    • (2003) Oncogene , vol.22 , pp. 3431-3440
    • Achison, M.1    Hupp, T.R.2
  • 13
    • 8344287553 scopus 로고    scopus 로고
    • Prognostic significance of serine 392 phosphorylation in overexpressed p53 protein in human esophageal squamous cell carcinoma
    • Matsumoto, M., Furihata, M., Kurabayashi, A., Sasaguri, S., Araki, K., Hayashi, H. and Ohtsuki, Y. (2004) Prognostic significance of serine 392 phosphorylation in overexpressed p53 protein in human esophageal squamous cell carcinoma. Oncology 67, 143-150.
    • (2004) Oncology , vol.67 , pp. 143-150
    • Matsumoto, M.1    Furihata, M.2    Kurabayashi, A.3    Sasaguri, S.4    Araki, K.5    Hayashi, H.6    Ohtsuki, Y.7
  • 14
    • 73349103766 scopus 로고    scopus 로고
    • Expression of p53 protein phosphorylated at serine 20 and serine 392 in malignant and benign ovarian neoplasms: correlation with clinicopathological parameters of tumors
    • Bar, J. K., Slomska, I., Rabczynki, J., Noga, L. and Grybos, M. (2009) Expression of p53 protein phosphorylated at serine 20 and serine 392 in malignant and benign ovarian neoplasms: correlation with clinicopathological parameters of tumors. Int. J. Gynecol. Cancer 19, 1322-1328.
    • (2009) Int. J. Gynecol. Cancer , vol.19 , pp. 1322-1328
    • Bar, J.K.1    Slomska, I.2    Rabczynki, J.3    Noga, L.4    Grybos, M.5
  • 15
    • 4143146741 scopus 로고    scopus 로고
    • Modification of serine 392 is a critical event in the regulation of p53 nuclear export and stability
    • Kim, Y. Y., Park, B. J., Kim, D. J., Kim, W. H., Kim, S., Oh, K. S., Lim, J. Y., Kim, J., Park, C. and Park, S. I. (2004) Modification of serine 392 is a critical event in the regulation of p53 nuclear export and stability. FEBS Lett. 572, 92-98.
    • (2004) FEBS Lett. , vol.572 , pp. 92-98
    • Kim, Y.Y.1    Park, B.J.2    Kim, D.J.3    Kim, W.H.4    Kim, S.5    Oh, K.S.6    Lim, J.Y.7    Kim, J.8    Park, C.9    Park, S.I.10
  • 17
    • 33644758287 scopus 로고    scopus 로고
    • CDK9 phosphorylates p53 on serine residues 33, 315 and 392
    • Radhakrishnan, S. K. and Gartel, A. L. (2006) CDK9 phosphorylates p53 on serine residues 33, 315 and 392. Cell cycle 5, 519-521.
    • (2006) Cell cycle , vol.5 , pp. 519-521
    • Radhakrishnan, S.K.1    Gartel, A.L.2
  • 18
    • 84877948994 scopus 로고    scopus 로고
    • Kinase CK2 Inhibition: An Update
    • Cozza, G., A Pinna, L. and Moro, S. (2013) Kinase CK2 Inhibition: An Update. Curr. Med. Chem. 20, 671-693.
    • (2013) Curr. Med. Chem. , vol.20 , pp. 671-693
    • Cozza, G.1    Pinna, L.A.2    Moro, S.3
  • 19
    • 65249100143 scopus 로고    scopus 로고
    • Small-molecule inhibitors of the MDM2-p53 protein-protein interaction to reactivate p53 function: a novel approach for cancer therapy
    • Shangary, S. and Wang, S. (2009) Small-molecule inhibitors of the MDM2-p53 protein-protein interaction to reactivate p53 function: a novel approach for cancer therapy. Annu. Rev. Pharmacol. 49, 223-241.
    • (2009) Annu. Rev. Pharmacol. , vol.49 , pp. 223-241
    • Shangary, S.1    Wang, S.2
  • 22
    • 0033020147 scopus 로고    scopus 로고
    • Regulation of p53 function and stability by phosphorylation
    • Ashcroft, M., Kubbutat, M. H. and Vousden, K. H. (1999) Regulation of p53 function and stability by phosphorylation. Mol. Cell. Biol. 19, 1751-1758.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1751-1758
    • Ashcroft, M.1    Kubbutat, M.H.2    Vousden, K.H.3
  • 25
    • 34047151851 scopus 로고    scopus 로고
    • p53 gene in treatment of hepatic carcinoma: status quo
    • Guan, Y.-S., La, Z., Yang, L., He, Q. and Li, P. (2007) p53 gene in treatment of hepatic carcinoma: status quo. World J. Gastroentero. 13, 985-992.
    • (2007) World J. Gastroentero. , vol.13 , pp. 985-992
    • Guan, Y.-S.1    La, Z.2    Yang, L.3    He, Q.4    Li, P.5
  • 26
    • 84855551714 scopus 로고    scopus 로고
    • Links between mutant p53 and genomic instability
    • Hanel, W. and Moll, U. M. (2012) Links between mutant p53 and genomic instability. J. Cell. Biochem. 113, 433-439.
    • (2012) J. Cell. Biochem. , vol.113 , pp. 433-439
    • Hanel, W.1    Moll, U.M.2
  • 27
    • 77953591790 scopus 로고    scopus 로고
    • Mutation at Ser392 specifically sensitizes mutant p53H175 to mdm2-mediated degradation
    • Gillotin, S., Yap, D. and Lu, X. (2010) Mutation at Ser392 specifically sensitizes mutant p53H175 to mdm2-mediated degradation. Cell Cycle 9, 1390-1398.
    • (2010) Cell Cycle , vol.9 , pp. 1390-1398
    • Gillotin, S.1    Yap, D.2    Lu, X.3
  • 29
    • 3342982324 scopus 로고    scopus 로고
    • p53 dephosphorylation and p21Cip1/Waf1 translocation correlate with caspase-3 activation in TGF-ß1-induced apoptosis of HuH-7 cells
    • Fan, G., Ma, X., Wong, P., Rodrigues, C. and Steer, C. (2004) p53 dephosphorylation and p21Cip1/Waf1 translocation correlate with caspase-3 activation in TGF-ß1-induced apoptosis of HuH-7 cells. Apoptosis 9, 211-221.
    • (2004) Apoptosis , vol.9 , pp. 211-221
    • Fan, G.1    Ma, X.2    Wong, P.3    Rodrigues, C.4    Steer, C.5
  • 30
    • 33750036122 scopus 로고    scopus 로고
    • Posttranslational phosphorylation of mutant p53 protein in tumor development
    • Matsumoto, M., Furihata, M. and Ohtsuki, Y. (2006) Posttranslational phosphorylation of mutant p53 protein in tumor development. Med. Mol. Morphol. 39, 79-87.
    • (2006) Med. Mol. Morphol. , vol.39 , pp. 79-87
    • Matsumoto, M.1    Furihata, M.2    Ohtsuki, Y.3
  • 31
    • 33745949757 scopus 로고    scopus 로고
    • Dual-site regulation of MDM2 E3-ubiquitin ligase activity
    • Wallace, M., Worrall, E., Pettersson, S., Hupp, T. R. and Ball, K. L. (2006) Dual-site regulation of MDM2 E3-ubiquitin ligase activity. Mol. cell 23, 251-263.
    • (2006) Mol. cell , vol.23 , pp. 251-263
    • Wallace, M.1    Worrall, E.2    Pettersson, S.3    Hupp, T.R.4    Ball, K.L.5
  • 32
    • 78851472178 scopus 로고    scopus 로고
    • MDM2 antagonist can inhibit tumor growth in hepatocellular carcinoma with different types of p53 in vitro
    • Wang, J., Zheng, T., Chen, X., Song, X., Meng, X., Bhatta, N., Pan, S., Jiang, H. and Liu, L. (2011) MDM2 antagonist can inhibit tumor growth in hepatocellular carcinoma with different types of p53 in vitro. J. Gastroen. Hepatol. 26, 371-377.
    • (2011) J. Gastroen. Hepatol. , vol.26 , pp. 371-377
    • Wang, J.1    Zheng, T.2    Chen, X.3    Song, X.4    Meng, X.5    Bhatta, N.6    Pan, S.7    Jiang, H.8    Liu, L.9
  • 33
    • 78649573167 scopus 로고    scopus 로고
    • Ursolic acid induces human hepatoma cell line SMMC-7721 apoptosis via p53-dependent pathway
    • Yu, Y., Gu, Z., Yin, J., Chou, W., Kwok, C., Qin, Z. and LIANG, Z. (2010) Ursolic acid induces human hepatoma cell line SMMC-7721 apoptosis via p53-dependent pathway. Chinese Med. J. 123, 1915-1923.
    • (2010) Chinese Med. J. , vol.123 , pp. 1915-1923
    • Yu, Y.1    Gu, Z.2    Yin, J.3    Chou, W.4    Kwok, C.5    Qin, Z.6    Liang, Z.7
  • 34
    • 84860408601 scopus 로고    scopus 로고
    • Luteolin induced G2 phase cell cycle arrest and apoptosis on non-small cell lung cancer cells
    • Cai, X., Ye, T., Liu, C., Lu, W., Lu, M., Zhang, J., Wang, M. and Cao, P. (2011) Luteolin induced G2 phase cell cycle arrest and apoptosis on non-small cell lung cancer cells. Toxicol. In Vitro 25, 1385-1391.
    • (2011) Toxicol. In Vitro , vol.25 , pp. 1385-1391
    • Cai, X.1    Ye, T.2    Liu, C.3    Lu, W.4    Lu, M.5    Zhang, J.6    Wang, M.7    Cao, P.8


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