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Volumn 294, Issue 1, 2010, Pages 82-90

The ubiquitin-proteasome system is inhibited by p53 protein expression in human ovarian cancer cells

Author keywords

EGFPu; Ovarian cancer; P53; Proteasome activity; UPS function

Indexed keywords

PROTEASOME; PROTEIN P53; UBIQUITIN;

EID: 77953001887     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.canlet.2010.01.025     Document Type: Article
Times cited : (3)

References (53)
  • 2
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: paradigm of a self-compartmentalizing protease
    • Baumeister W., Walz J., Zuhl F., Seemuller E. The proteasome: paradigm of a self-compartmentalizing protease. Cell 1998, 92:367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 3
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock K.L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., Hwang D., Goldberg A.L. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 1994, 78:761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 4
  • 5
    • 61449156563 scopus 로고    scopus 로고
    • Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology
    • Schwartz A.L., Ciechanover A. Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology. Annual Review of Pharmacology and Toxicology 2009, 49:73-96.
    • (2009) Annual Review of Pharmacology and Toxicology , vol.49 , pp. 73-96
    • Schwartz, A.L.1    Ciechanover, A.2
  • 8
    • 37349084533 scopus 로고    scopus 로고
    • Phase I trial of the proteasome inhibitor bortezomib in combination with carboplatin in patients with platinum- and taxane-resistant ovarian cancer
    • Ramirez P.T., Landen C.N., Coleman R.L., Milam M.R., Levenback C., Johnston T.A., Gershenson D.M. Phase I trial of the proteasome inhibitor bortezomib in combination with carboplatin in patients with platinum- and taxane-resistant ovarian cancer. Gynecologic Oncology 2008, 108:68-71.
    • (2008) Gynecologic Oncology , vol.108 , pp. 68-71
    • Ramirez, P.T.1    Landen, C.N.2    Coleman, R.L.3    Milam, M.R.4    Levenback, C.5    Johnston, T.A.6    Gershenson, D.M.7
  • 9
    • 0142054051 scopus 로고    scopus 로고
    • Bortezomib (PS-341): a novel, first-in-class proteasome inhibitor for the treatment of multiple myeloma and other cancers
    • Richardson P.G., Hideshima T., Anderson K.C. Bortezomib (PS-341): a novel, first-in-class proteasome inhibitor for the treatment of multiple myeloma and other cancers. Cancer Control 2003, 10:361-369.
    • (2003) Cancer Control , vol.10 , pp. 361-369
    • Richardson, P.G.1    Hideshima, T.2    Anderson, K.C.3
  • 10
  • 11
    • 0035496607 scopus 로고    scopus 로고
    • Rescuing the function of mutant p53
    • Bullock A.N., Fersht A.R. Rescuing the function of mutant p53. Nature Reviews 2001, 1:68-76.
    • (2001) Nature Reviews , vol.1 , pp. 68-76
    • Bullock, A.N.1    Fersht, A.R.2
  • 13
    • 43649108895 scopus 로고    scopus 로고
    • The (1-63) region of the p53 transactivation domain aggregates in vitro into cytotoxic amyloid assemblies
    • Rigacci S., Bucciantini M., Relini A., Pesce A., Gliozzi A., Berti A., Stefani M. The (1-63) region of the p53 transactivation domain aggregates in vitro into cytotoxic amyloid assemblies. Biophysical Journal 2008, 94:3635-3646.
    • (2008) Biophysical Journal , vol.94 , pp. 3635-3646
    • Rigacci, S.1    Bucciantini, M.2    Relini, A.3    Pesce, A.4    Gliozzi, A.5    Berti, A.6    Stefani, M.7
  • 14
    • 0035336658 scopus 로고    scopus 로고
    • Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release
    • Jana N.R., Zemskov E.A., Wang G.-h., Nukina N. Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Human Molecular Genetics 2001, 10:1049-1059.
    • (2001) Human Molecular Genetics , vol.10 , pp. 1049-1059
    • Jana, N.R.1    Zemskov, E.A.2    Wang, G.-H.3    Nukina, N.4
  • 17
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 2001, 292:1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 18
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors
    • (erratum appears in Gene. 1992 May 1; 114(1): 81-3; PMID: 1375182)
    • Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 1985, 33:103-119. (erratum appears in Gene. 1992 May 1; 114(1): 81-3; PMID: 1375182).
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 21
    • 0021185050 scopus 로고
    • Experimental model systems of ovarian cancer: applications to the design and evaluation of new treatment approaches
    • Hamilton T.C., Young R.C., Ozols R.F. Experimental model systems of ovarian cancer: applications to the design and evaluation of new treatment approaches. Seminars in Oncology 1984, 11:285-298.
    • (1984) Seminars in Oncology , vol.11 , pp. 285-298
    • Hamilton, T.C.1    Young, R.C.2    Ozols, R.F.3
  • 22
    • 0003104964 scopus 로고
    • New human tumor cell lines
    • Plenum press, New York, J. Fogh (Ed.)
    • Fogh J., Trempe G. New human tumor cell lines. Human Tumor Cells In Vitro 1975, 115-159. Plenum press, New York. J. Fogh (Ed.).
    • (1975) Human Tumor Cells In Vitro , pp. 115-159
    • Fogh, J.1    Trempe, G.2
  • 23
    • 0029952441 scopus 로고    scopus 로고
    • In vivo ubiquitination and proteasome-mediated degradation of p53
    • Maki C.G., Huibregtse J.M., Howley P.M. In vivo ubiquitination and proteasome-mediated degradation of p53. Cancer Research 1996, 56:2649-2654.
    • (1996) Cancer Research , vol.56 , pp. 2649-2654
    • Maki, C.G.1    Huibregtse, J.M.2    Howley, P.M.3
  • 24
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward C.L., Omura S., Kopito R.R. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 1995, 83:121-127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 28
    • 27644518292 scopus 로고    scopus 로고
    • Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates
    • Academic Press
    • Kisselev A.F., Goldberg A.L., Raymond J.D. Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates. Methods in Enzymology 2005, Academic Press, pp. 364-378.
    • (2005) Methods in Enzymology , pp. 364-378
    • Kisselev, A.F.1    Goldberg, A.L.2    Raymond, J.D.3
  • 29
    • 0026760566 scopus 로고
    • Abnormal structure and expression of the p53 gene in human ovarian carcinoma cell lines
    • Yaginuma Y., Westphal H. Abnormal structure and expression of the p53 gene in human ovarian carcinoma cell lines. Cancer Research 1992, 52:4196-4199.
    • (1992) Cancer Research , vol.52 , pp. 4196-4199
    • Yaginuma, Y.1    Westphal, H.2
  • 30
    • 0030865104 scopus 로고    scopus 로고
    • Characterization of the p53 tumor suppressor pathway in cell lines of the National Cancer Institute anticancer drug screen and correlations with the growth-inhibitory potency of 123 anticancer agents
    • O'Connor P., Jackman J., Bae I., Myers T., Fan S., Mutoh M., Scudiero D., Monks A., Sausville E., Weinstein J., Friend S., Fornace A., Kohn K. Characterization of the p53 tumor suppressor pathway in cell lines of the National Cancer Institute anticancer drug screen and correlations with the growth-inhibitory potency of 123 anticancer agents. Cancer Research 1997, 57:4285-4300.
    • (1997) Cancer Research , vol.57 , pp. 4285-4300
    • O'Connor, P.1    Jackman, J.2    Bae, I.3    Myers, T.4    Fan, S.5    Mutoh, M.6    Scudiero, D.7    Monks, A.8    Sausville, E.9    Weinstein, J.10    Friend, S.11    Fornace, A.12    Kohn, K.13
  • 31
    • 77952995445 scopus 로고    scopus 로고
    • The role of transforming growth factor beta in epithelial ovarian cancer, Obstetrics and Gynaecology, 261 leaves
    • D.M. Richardson, The role of transforming growth factor beta in epithelial ovarian cancer, Obstetrics and Gynaecology, University of Auckland, 2008 (pp. xxvii, 261 leaves).
    • (2008) University of Auckland , pp. 27
    • Richardson, D.M.1
  • 32
    • 28844485595 scopus 로고    scopus 로고
    • Monitoring of Ubiquitin - dependent proteolysis with green fluorescent protein substrates
    • Academic Press
    • Menendez-Benito V., Heessen S., Dantuma N.P., Raymond J.D. Monitoring of Ubiquitin - dependent proteolysis with green fluorescent protein substrates. Methods in Enzymology 2005, Academic Press, pp. 490-511.
    • (2005) Methods in Enzymology , pp. 490-511
    • Menendez-Benito, V.1    Heessen, S.2    Dantuma, N.P.3    Raymond, J.D.4
  • 33
    • 34248547813 scopus 로고    scopus 로고
    • Soluble protein oligomers as emerging toxins in alzheimer's and other amyloid diseases
    • Ferreira S.T., Vieira M.N.N., De Felice F.G. Soluble protein oligomers as emerging toxins in alzheimer's and other amyloid diseases. IUBMB Life 2007, 59:332-345.
    • (2007) IUBMB Life , vol.59 , pp. 332-345
    • Ferreira, S.T.1    Vieira, M.N.N.2    De Felice, F.G.3
  • 34
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • Bennett E.J., Bence N.F., Jayakumar R., Kopito R.R. Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Molecular Cell 2005, 17:351-365.
    • (2005) Molecular Cell , vol.17 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3    Kopito, R.R.4
  • 36
    • 0035890265 scopus 로고    scopus 로고
    • Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53
    • King F.W., Wawrzynow A., Hohfeld J., Zylicz M. Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53. EMBO Journal 2001, 20:6297-6305.
    • (2001) EMBO Journal , vol.20 , pp. 6297-6305
    • King, F.W.1    Wawrzynow, A.2    Hohfeld, J.3    Zylicz, M.4
  • 38
    • 0035801391 scopus 로고    scopus 로고
    • Hsp70 interactions with the p53 tumour suppressor protein
    • Zylicz M., King F.W., Wawrzynow A. Hsp70 interactions with the p53 tumour suppressor protein. EMBO Journal 2001, 20:4634-4638.
    • (2001) EMBO Journal , vol.20 , pp. 4634-4638
    • Zylicz, M.1    King, F.W.2    Wawrzynow, A.3
  • 39
    • 44149124776 scopus 로고    scopus 로고
    • Chaperone-dependent stabilization and degradation of p53 mutants
    • Muller P., Hrstka R., Coomber D., Lane D.P., Vojtesek B. Chaperone-dependent stabilization and degradation of p53 mutants. Oncogene 2008, 27:3371-3383.
    • (2008) Oncogene , vol.27 , pp. 3371-3383
    • Muller, P.1    Hrstka, R.2    Coomber, D.3    Lane, D.P.4    Vojtesek, B.5
  • 40
    • 34347205250 scopus 로고    scopus 로고
    • MDM2 binding induces a conformational change in p53 that is opposed by heat-shock protein 90 and precedes p53 proteasomal degradation
    • Sasaki M., Nie L., Maki C.G. MDM2 binding induces a conformational change in p53 that is opposed by heat-shock protein 90 and precedes p53 proteasomal degradation. Journal of Biological Chemistry 2007, 282:14626-14634.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 14626-14634
    • Sasaki, M.1    Nie, L.2    Maki, C.G.3
  • 42
    • 34347263061 scopus 로고    scopus 로고
    • Regulation of p53 nuclear export through sequential changes in conformation and ubiquitination
    • Nie L., Sasaki M., Maki C.G. Regulation of p53 nuclear export through sequential changes in conformation and ubiquitination. Journal of Biological Chemistry 2007, 282:14616-14625.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 14616-14625
    • Nie, L.1    Sasaki, M.2    Maki, C.G.3
  • 44
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein D.C. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 2006, 443:780-786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 46
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine B., Kroemer G. Autophagy in the pathogenesis of disease. Cell 2008, 132:27-42.
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 51
    • 0028352980 scopus 로고
    • Purification and characterization of an endogenous inhibitor specific to the Z-Leu-Leu-Leu-MCA degrading activity in proteasome and its identification as heat-shock protein 90
    • Tsubuki S., Saito Y., Kawashima S. Purification and characterization of an endogenous inhibitor specific to the Z-Leu-Leu-Leu-MCA degrading activity in proteasome and its identification as heat-shock protein 90. FEBS Letters 1994, 344:229-233.
    • (1994) FEBS Letters , vol.344 , pp. 229-233
    • Tsubuki, S.1    Saito, Y.2    Kawashima, S.3
  • 52
    • 0030586350 scopus 로고    scopus 로고
    • Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat-shock protein 90
    • Conconi M., Szweda L.I., Levine R.L., Stadtman E.R., Friguet B. Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat-shock protein 90. Archives of Biochemistry and Biophysics 1996, 331:232-240.
    • (1996) Archives of Biochemistry and Biophysics , vol.331 , pp. 232-240
    • Conconi, M.1    Szweda, L.I.2    Levine, R.L.3    Stadtman, E.R.4    Friguet, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.