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Volumn 6, Issue 10, 2007, Pages 2747-2756

Treatment of colon cancer cells using the cytosine deaminase/5- fluorocytosine suicide system induces apoptosis, modulation of the proteome, and Hsp90β phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSINE DEAMINASE; FLUCYTOSINE; HEAT SHOCK PROTEIN 90; PROTEOME;

EID: 35848962534     PISSN: 15357163     EISSN: None     Source Type: Journal    
DOI: 10.1158/1535-7163.MCT-07-0040     Document Type: Article
Times cited : (25)

References (50)
  • 3
    • 0028108469 scopus 로고
    • Metabolism of 5-fluorocytosine to 5-fluorouracil in human colorectal tumor cells transduced with the cytosine deaminase gene: Significant antitumor effects when only a small percentage oftumor cells express cytosine deaminase
    • Huber BE, Austin EA, Richards CA, Davis ST, Good SS. Metabolism of 5-fluorocytosine to 5-fluorouracil in human colorectal tumor cells transduced with the cytosine deaminase gene: significant antitumor effects when only a small percentage oftumor cells express cytosine deaminase. Proc Natl Acad Sci U S A 1994;91:8302-6.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 8302-8306
    • Huber, B.E.1    Austin, E.A.2    Richards, C.A.3    Davis, S.T.4    Good, S.S.5
  • 4
    • 0027483695 scopus 로고
    • The "bystander effect": Tumor regression when a fraction of the tumor mass is genetically modified
    • Freeman SM, Abboud CN, Whartenby KA, et al. The "bystander effect": tumor regression when a fraction of the tumor mass is genetically modified. Cancer Res 1993;53:5274-83.
    • (1993) Cancer Res , vol.53 , pp. 5274-5283
    • Freeman, S.M.1    Abboud, C.N.2    Whartenby, K.A.3
  • 6
    • 0030668915 scopus 로고    scopus 로고
    • A "distant" bystander effect ofsuicide gene therapy: Regression of nontransduced tumors together with a distant transduced tumor
    • Kianmanesh AR, Perrin H, Panis Y, et al. A "distant" bystander effect ofsuicide gene therapy: regression of nontransduced tumors together with a distant transduced tumor. Hum Gene Ther 1997;8:1807-14.
    • (1997) Hum Gene Ther , vol.8 , pp. 1807-1814
    • Kianmanesh, A.R.1    Perrin, H.2    Panis, Y.3
  • 7
    • 0034145764 scopus 로고    scopus 로고
    • Regression of experimental liver tumor after distant intra-hepatic injection of cytosine deaminase-expressing tumor cells and 5-fluorocytosine treatment
    • Pierrefite-Carle V, Baque P, Gavelli A, et al. Regression of experimental liver tumor after distant intra-hepatic injection of cytosine deaminase-expressing tumor cells and 5-fluorocytosine treatment. Int J Mol Med 2000;5:275-8.
    • (2000) Int J Mol Med , vol.5 , pp. 275-278
    • Pierrefite-Carle, V.1    Baque, P.2    Gavelli, A.3
  • 8
    • 0034654491 scopus 로고    scopus 로고
    • Pierrefite-Carle V, Gavelli A, Brossette N, et al. Re: Cytosine deaminase/5-fluorocytosine-based vaccination against liver tumors: evidence of distant bystander effect. J Natl Cancer Inst 2000;92:494-5.
    • Pierrefite-Carle V, Gavelli A, Brossette N, et al. Re: Cytosine deaminase/5-fluorocytosine-based vaccination against liver tumors: evidence of distant bystander effect. J Natl Cancer Inst 2000;92:494-5.
  • 9
    • 0036181483 scopus 로고    scopus 로고
    • Subcutaneous or intrahepatic injection ofsu icide gene modified tumour cells induces a systemic antitumour response in a metastatic model of colon carcinoma in rats
    • Pierrefite-Carle V, Baque P, Gavelli A, et al. Subcutaneous or intrahepatic injection ofsu icide gene modified tumour cells induces a systemic antitumour response in a metastatic model of colon carcinoma in rats. Gut 2002;50:387-91.
    • (2002) Gut , vol.50 , pp. 387-391
    • Pierrefite-Carle, V.1    Baque, P.2    Gavelli, A.3
  • 10
    • 33645959208 scopus 로고    scopus 로고
    • Heat shock proteins in immunity
    • Multhoff G. Heat shock proteins in immunity. Handb Exp Pharmacol 2006:279-304.
    • (2006) Handb Exp Pharmacol , pp. 279-304
    • Multhoff, G.1
  • 11
    • 0036512171 scopus 로고    scopus 로고
    • Roles of heat-shock proteins in innate and adaptive immunity
    • Srivastava P. Roles of heat-shock proteins in innate and adaptive immunity. Nat Rev Immunol 2002;2:185-94.
    • (2002) Nat Rev Immunol , vol.2 , pp. 185-194
    • Srivastava, P.1
  • 12
    • 0036892577 scopus 로고    scopus 로고
    • Stressed apoptotic tumor cells stimulate dendritic cells and induce specific cytotoxic T cells
    • Feng H, Zeng Y, Graner MW, Katsanis E. Stressed apoptotic tumor cells stimulate dendritic cells and induce specific cytotoxic T cells. Blood 2002;100:4108-15.
    • (2002) Blood , vol.100 , pp. 4108-4115
    • Feng, H.1    Zeng, Y.2    Graner, M.W.3    Katsanis, E.4
  • 13
    • 33645916426 scopus 로고    scopus 로고
    • A role for the Hsp90 molecular chaperone family in antigen presentation to T lymphocytes via major histocompatibility complex class II molecules
    • Rajagopal D, Bal V, Mayor S, George A, Rath S. A role for the Hsp90 molecular chaperone family in antigen presentation to T lymphocytes via major histocompatibility complex class II molecules. Eur J Immunol 2006;36:828-41.
    • (2006) Eur J Immunol , vol.36 , pp. 828-841
    • Rajagopal, D.1    Bal, V.2    Mayor, S.3    George, A.4    Rath, S.5
  • 14
    • 18744416943 scopus 로고    scopus 로고
    • Heat shock protein 90 expression in Epstein-Barr virus-infected B cells promotes γδ T-cell proliferation in vitro
    • Kotsiopriftis M, Tanner JE, Alfieri C. Heat shock protein 90 expression in Epstein-Barr virus-infected B cells promotes γδ T-cell proliferation in vitro. J Virol 2005;79:7255-61.
    • (2005) J Virol , vol.79 , pp. 7255-7261
    • Kotsiopriftis, M.1    Tanner, J.E.2    Alfieri, C.3
  • 15
    • 27744479712 scopus 로고    scopus 로고
    • Modulating molecular chaperone Hsp90 functions through reversible acetylation
    • Aoyagi S, Archer TK. Modulating molecular chaperone Hsp90 functions through reversible acetylation. Trends Cell Biol 2005;15:565-7.
    • (2005) Trends Cell Biol , vol.15 , pp. 565-567
    • Aoyagi, S.1    Archer, T.K.2
  • 16
    • 0035980061 scopus 로고    scopus 로고
    • Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein
    • Zhao YG, Gilmore R, Leone G, Coffey MC, Weber B, Lee PW. Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein. J Biol Chem 2001;276:32822-7.
    • (2001) J Biol Chem , vol.276 , pp. 32822-32827
    • Zhao, Y.G.1    Gilmore, R.2    Leone, G.3    Coffey, M.C.4    Weber, B.5    Lee, P.W.6
  • 17
    • 0021050381 scopus 로고
    • Selection by trypsin of two sublines of rat colon cancer cells forming progressive or regressive tumors
    • Martin F, Caignard A, Jeannin JF, Leclerc A, Martin M. Selection by trypsin of two sublines of rat colon cancer cells forming progressive or regressive tumors. Int J Cancer 1983;32:623-7.
    • (1983) Int J Cancer , vol.32 , pp. 623-627
    • Martin, F.1    Caignard, A.2    Jeannin, J.F.3    Leclerc, A.4    Martin, M.5
  • 18
    • 33746762097 scopus 로고    scopus 로고
    • A mass spectrometric approach to identify arbuscular mycorrhiza-related proteins in root plasma membrane fractions
    • Valot B, Negroni L, Zivy M, Gianinazzi S, Dumas-Gaudot E. A mass spectrometric approach to identify arbuscular mycorrhiza-related proteins in root plasma membrane fractions. Proteomics 2006;6 Suppl 1:S145-55.
    • (2006) Proteomics , vol.6 , Issue.SUPPL. 1
    • Valot, B.1    Negroni, L.2    Zivy, M.3    Gianinazzi, S.4    Dumas-Gaudot, E.5
  • 19
    • 0029944880 scopus 로고    scopus 로고
    • Sequential acquisition of mitochondrial and plasma membrane alterations during early lymphocyte apoptosis
    • Castedo M, Hirsch T, Susin SA, et al. Sequential acquisition of mitochondrial and plasma membrane alterations during early lymphocyte apoptosis. J Immunol 1996;157:512-21.
    • (1996) J Immunol , vol.157 , pp. 512-521
    • Castedo, M.1    Hirsch, T.2    Susin, S.A.3
  • 21
    • 3042602196 scopus 로고    scopus 로고
    • Mitochondrial thioredoxin system: Effects of TrxR2 overexpression on redox balance, cell growth, and apoptosis
    • Patenaude A, Ven Murthy MR, Mirault ME. Mitochondrial thioredoxin system: effects of TrxR2 overexpression on redox balance, cell growth, and apoptosis. J Biol Chem 2004;279:27302-14.
    • (2004) J Biol Chem , vol.279 , pp. 27302-27314
    • Patenaude, A.1    Ven Murthy, M.R.2    Mirault, M.E.3
  • 22
    • 0033796101 scopus 로고    scopus 로고
    • The role of the redox protein thioredoxin in cell growth and cancer
    • Powis G, Mustacich D, Coon A. The role of the redox protein thioredoxin in cell growth and cancer. Free Radic Biol Med 2000;29:312-22.
    • (2000) Free Radic Biol Med , vol.29 , pp. 312-322
    • Powis, G.1    Mustacich, D.2    Coon, A.3
  • 23
    • 1842854941 scopus 로고    scopus 로고
    • Cellular mechanisms of cyclophosphamide resistance: Model studies in human medulloblastoma cell lines
    • Friedman HS, Johnson SP, Colvin OM. Cellular mechanisms of cyclophosphamide resistance: model studies in human medulloblastoma cell lines. Cancer Treat Res 2002;112:199-209.
    • (2002) Cancer Treat Res , vol.112 , pp. 199-209
    • Friedman, H.S.1    Johnson, S.P.2    Colvin, O.M.3
  • 24
    • 1842833110 scopus 로고    scopus 로고
    • Leukemic cell insensitivity to cyclophosphamide and other oxazaphosphorines mediated by aldehyde dehydrogenase(s)
    • Sladek NE. Leukemic cell insensitivity to cyclophosphamide and other oxazaphosphorines mediated by aldehyde dehydrogenase(s). Cancer Treat Res 2002;112:161-75.
    • (2002) Cancer Treat Res , vol.112 , pp. 161-175
    • Sladek, N.E.1
  • 25
    • 0842328715 scopus 로고    scopus 로고
    • Pharmacogenetics of neoplastic diseases: New trends
    • Di Paolo A, Danesi R, Del Tacca M. Pharmacogenetics of neoplastic diseases: new trends. Pharmacol Res 2004;49:331-42.
    • (2004) Pharmacol Res , vol.49 , pp. 331-342
    • Di Paolo, A.1    Danesi, R.2    Del Tacca, M.3
  • 26
    • 26444551223 scopus 로고    scopus 로고
    • Disorders of purine and pyrimidine metabolism
    • Nyhan WL. Disorders of purine and pyrimidine metabolism. Mol Genet Metab 2005;86:25-33.
    • (2005) Mol Genet Metab , vol.86 , pp. 25-33
    • Nyhan, W.L.1
  • 28
    • 27644484968 scopus 로고    scopus 로고
    • Clinging to life: Cell to matrix adhesion and cell survival
    • Reddig PJ, Juliano RL. Clinging to life: cell to matrix adhesion and cell survival. Cancer Metastasis Rev 2005;24:425-39.
    • (2005) Cancer Metastasis Rev , vol.24 , pp. 425-439
    • Reddig, P.J.1    Juliano, R.L.2
  • 29
    • 1542618024 scopus 로고    scopus 로고
    • Improvement of an in vitro stem cell assay for developmental toxicity: The use of molecular endpoints in the embryonic stem cell test
    • Seiler A, Visan A, Buesen R, Genschow E, Spielmann H. Improvement of an in vitro stem cell assay for developmental toxicity: the use of molecular endpoints in the embryonic stem cell test. Reprod Toxicol 2004;18:231-40.
    • (2004) Reprod Toxicol , vol.18 , pp. 231-240
    • Seiler, A.1    Visan, A.2    Buesen, R.3    Genschow, E.4    Spielmann, H.5
  • 30
    • 0038513535 scopus 로고    scopus 로고
    • Identification of drug-regulated genes in osteosarcoma cells
    • Fellenberg J, Dechant MJ, Ewerbeck V, Mau H. Identification of drug-regulated genes in osteosarcoma cells. Int J Cancer 2003;105:636-43.
    • (2003) Int J Cancer , vol.105 , pp. 636-643
    • Fellenberg, J.1    Dechant, M.J.2    Ewerbeck, V.3    Mau, H.4
  • 31
    • 2642522810 scopus 로고    scopus 로고
    • A role for ezrin in a neglected metastatic tumor function
    • Fais S. A role for ezrin in a neglected metastatic tumor function. Trends Mol Med 2004;10:249-50.
    • (2004) Trends Mol Med , vol.10 , pp. 249-250
    • Fais, S.1
  • 32
    • 0034597013 scopus 로고    scopus 로고
    • CD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: A novel regulatory mechanism ofthe CD95 apoptotic pathway
    • Parlato S, Giammarioli AM, Logozzi M, et al. CD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: a novel regulatory mechanism ofthe CD95 apoptotic pathway. EMBO J 2000;19:5123-34.
    • (2000) EMBO J , vol.19 , pp. 5123-5134
    • Parlato, S.1    Giammarioli, A.M.2    Logozzi, M.3
  • 33
    • 0037079711 scopus 로고    scopus 로고
    • P-glycoprotein-actin association through ERM family proteins: A role in P-glycoprotein function in human cells oflymphoid origin
    • Luciani F, Molinari A, Lozupone F, et al. P-glycoprotein-actin association through ERM family proteins: a role in P-glycoprotein function in human cells oflymphoid origin. Blood 2002;99:641-8.
    • (2002) Blood , vol.99 , pp. 641-648
    • Luciani, F.1    Molinari, A.2    Lozupone, F.3
  • 34
    • 0033961896 scopus 로고    scopus 로고
    • Brain microvascular P-glycoprotein and a revised model ofmultidrug resistance in brain
    • Golden PL, Pardridge WM. Brain microvascular P-glycoprotein and a revised model ofmultidrug resistance in brain. Cell Mol Neurobiol 2000;20:165-81.
    • (2000) Cell Mol Neurobiol , vol.20 , pp. 165-181
    • Golden, P.L.1    Pardridge, W.M.2
  • 35
    • 17144424622 scopus 로고    scopus 로고
    • Translational control in stress and apoptosis
    • Holcik M, Sonenberg N. Translational control in stress and apoptosis. Nat Rev Mol Cell Biol 2005;6:318-27.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 318-327
    • Holcik, M.1    Sonenberg, N.2
  • 36
    • 0141594606 scopus 로고    scopus 로고
    • Not just for housekeeping: Protein initiation and elongation factors in cell growth and tumorigenesis
    • Thornton S, Anand N, Purcell D, Lee J. Not just for housekeeping: protein initiation and elongation factors in cell growth and tumorigenesis. J Mol Med 2003;81:536-48.
    • (2003) J Mol Med , vol.81 , pp. 536-548
    • Thornton, S.1    Anand, N.2    Purcell, D.3    Lee, J.4
  • 38
    • 24344460521 scopus 로고    scopus 로고
    • 14-3-3 proteins - an update
    • Mhawech P. 14-3-3 proteins - an update. Cell Res 2005;15:228-36.
    • (2005) Cell Res , vol.15 , pp. 228-236
    • Mhawech, P.1
  • 40
    • 33645528750 scopus 로고    scopus 로고
    • Identification of 14-3-3 as a contributor to drug resistance in human breast cancer cells using functional proteomic analysis
    • Liu Y, Liu H, Han B, Zhang J. Identification of 14-3-3 as a contributor to drug resistance in human breast cancer cells using functional proteomic analysis. Cancer Res 2006;66:3248-55.
    • (2006) Cancer Res , vol.66 , pp. 3248-3255
    • Liu, Y.1    Liu, H.2    Han, B.3    Zhang, J.4
  • 41
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer 2005;5:761-72.
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 42
    • 0345169713 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of HSP-90 during mammalian sperm capacitation
    • Ecroyd H, Jones RC, Aitken RJ. Tyrosine phosphorylation of HSP-90 during mammalian sperm capacitation. Biol Reprod 2003;69:1801-7.
    • (2003) Biol Reprod , vol.69 , pp. 1801-1807
    • Ecroyd, H.1    Jones, R.C.2    Aitken, R.J.3
  • 43
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • Kim SC, Sprung R, Chen Y, et al. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell 2006;23:607-18.
    • (2006) Mol Cell , vol.23 , pp. 607-618
    • Kim, S.C.1    Sprung, R.2    Chen, Y.3
  • 44
  • 46
    • 17444413094 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of synaptosomes from human cerebral cortex
    • DeGiorgis JA, Jaffe H, Moreira JE, et al. Phosphoproteomic analysis of synaptosomes from human cerebral cortex. J Proteome Res 2005;4:306-15.
    • (2005) J Proteome Res , vol.4 , pp. 306-315
    • DeGiorgis, J.A.1    Jaffe, H.2    Moreira, J.E.3
  • 47
    • 33646485094 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites
    • Hoffert JD, Pisitkun T, Wang G, Shen RF, Knepper MA. Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites. Proc Natl Acad Sci U S A 2006;103:7159-64.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7159-7164
    • Hoffert, J.D.1    Pisitkun, T.2    Wang, G.3    Shen, R.F.4    Knepper, M.A.5
  • 48
    • 0024548919 scopus 로고
    • Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II
    • Lees-Miller SP, Anderson CW. Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II. J Biol Chem 1989;264:2431-7.
    • (1989) J Biol Chem , vol.264 , pp. 2431-2437
    • Lees-Miller, S.P.1    Anderson, C.W.2
  • 49
    • 21144458164 scopus 로고    scopus 로고
    • Immunoaffinity profiling of tyrosine phosphorylation in cancer cells
    • Rush J, Moritz A, Lee KA, et al. Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol 2005;23:94-101.
    • (2005) Nat Biotechnol , vol.23 , pp. 94-101
    • Rush, J.1    Moritz, A.2    Lee, K.A.3
  • 50
    • 2942538330 scopus 로고    scopus 로고
    • ProteoMod: A new tool to quantitate protein post-translational modifications
    • Kumar Y, Khachane A, Belwal M, Das S, Somsundaram K, Tatu U. ProteoMod: a new tool to quantitate protein post-translational modifications. Proteomics 2004;4:1672-83.
    • (2004) Proteomics , vol.4 , pp. 1672-1683
    • Kumar, Y.1    Khachane, A.2    Belwal, M.3    Das, S.4    Somsundaram, K.5    Tatu, U.6


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