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Volumn 100, Issue 1, 2012, Pages 27-34

Transcriptomic analysis of the effect of ifosfamide on MDCK cells cultivated in microfluidic biochips

Author keywords

Cancer; Drug target; Ifosfamide; Inflammation; Kidney; PDMS microfluidic biochip; Transcriptomic

Indexed keywords

ATM PROTEIN; CYCLIN DEPENDENT KINASE INHIBITOR 1A; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; I KAPPA B ALPHA; IFOSFAMIDE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTEGRIN; MITOGEN ACTIVATED PROTEIN KINASE; MYC PROTEIN; PROTEIN P53; THIOREDOXIN REDUCTASE 1; TRANSCRIPTION FACTOR NRF2;

EID: 84862773705     PISSN: 08887543     EISSN: 10898646     Source Type: Journal    
DOI: 10.1016/j.ygeno.2012.05.001     Document Type: Article
Times cited : (29)

References (42)
  • 2
    • 0034837087 scopus 로고    scopus 로고
    • High-throughput screening approaches for investigating drug metabolism and pharmacokinetics
    • Roberts S.A. High-throughput screening approaches for investigating drug metabolism and pharmacokinetics. Xenobiotica 2001, 31:557-589.
    • (2001) Xenobiotica , vol.31 , pp. 557-589
    • Roberts, S.A.1
  • 3
  • 4
    • 13244277455 scopus 로고    scopus 로고
    • Metabolic screening in vitro: metabolic stability, CYP inhibition and induction
    • Riley R.J., Grime K. Metabolic screening in vitro: metabolic stability, CYP inhibition and induction. Drug Discov. Today Tech. 2004, 1:365-372.
    • (2004) Drug Discov. Today Tech. , vol.1 , pp. 365-372
    • Riley, R.J.1    Grime, K.2
  • 6
    • 84859635020 scopus 로고    scopus 로고
    • Analysis of transcriptomic and proteomic profiles demonstrates the improvement of the MDCK cell function in a renal microfluidic biochip
    • Choucha Snouber L., Letourneur F., Chafey P., Broussard C., Monge M., Legallais C., Leclerc E. Analysis of transcriptomic and proteomic profiles demonstrates the improvement of the MDCK cell function in a renal microfluidic biochip. Biotechnol. Prog. 2012, 28:474-484.
    • (2012) Biotechnol. Prog. , vol.28 , pp. 474-484
    • Choucha Snouber, L.1    Letourneur, F.2    Chafey, P.3    Broussard, C.4    Monge, M.5    Legallais, C.6    Leclerc, E.7
  • 7
    • 79961194518 scopus 로고    scopus 로고
    • Integrated proteomic and transcriptomic investigation highlights original insight into paracetamol toxicity in liver biochip
    • Prot J.M., Briffaut A.S., Letourneur F., Chafey P., Merlier F., Grandvalet Y., Legallais C., Leclerc E. Integrated proteomic and transcriptomic investigation highlights original insight into paracetamol toxicity in liver biochip. Plos One 2011, 6:21268.
    • (2011) Plos One , vol.6 , pp. 21268
    • Prot, J.M.1    Briffaut, A.S.2    Letourneur, F.3    Chafey, P.4    Merlier, F.5    Grandvalet, Y.6    Legallais, C.7    Leclerc, E.8
  • 8
    • 40249109853 scopus 로고    scopus 로고
    • The IkappaB kinase - a bridge between inflammation and cancer
    • Karin M. The IkappaB kinase - a bridge between inflammation and cancer. Cell Res. 2008, 18:334-342.
    • (2008) Cell Res. , vol.18 , pp. 334-342
    • Karin, M.1
  • 9
    • 34548321204 scopus 로고    scopus 로고
    • Nuclear factor-kappaB and the hepatic inflammation-fibrosis-cancer axis
    • Elsharkawy A.M., Mann D.A. Nuclear factor-kappaB and the hepatic inflammation-fibrosis-cancer axis. Hepatology 2007, 46:590-597.
    • (2007) Hepatology , vol.46 , pp. 590-597
    • Elsharkawy, A.M.1    Mann, D.A.2
  • 10
    • 66949133232 scopus 로고    scopus 로고
    • Ifosfamide nephrotoxicity in children: a mechanistic base for pharmacological prevention
    • Hanly L., Chen N., Rieder M., Koren G. Ifosfamide nephrotoxicity in children: a mechanistic base for pharmacological prevention. Expert Opin. Drug Saf. 2009, 8:155-168.
    • (2009) Expert Opin. Drug Saf. , vol.8 , pp. 155-168
    • Hanly, L.1    Chen, N.2    Rieder, M.3    Koren, G.4
  • 12
    • 34248651810 scopus 로고    scopus 로고
    • Ifosfamide toxicity in cultured proximal renal tubule cells
    • Springate J., Taub M. Ifosfamide toxicity in cultured proximal renal tubule cells. Pediatr. Nephrol. 2007, 22:358-365.
    • (2007) Pediatr. Nephrol. , vol.22 , pp. 358-365
    • Springate, J.1    Taub, M.2
  • 13
    • 77953291227 scopus 로고    scopus 로고
    • Decreased exposure to sunitinib due to concomitant administration of ifosfamide: results of a phase I and pharmacokinetic study on the combination of sunitinib and ifosfamide in patients with advanced solid malignancies
    • Hamberg P., Steeghs N., Loos W., van Biessen D., den Hollander M., Tascilar M., Verweij J., Gelderblom H., Sleijfer S. Decreased exposure to sunitinib due to concomitant administration of ifosfamide: results of a phase I and pharmacokinetic study on the combination of sunitinib and ifosfamide in patients with advanced solid malignancies. Br. J. Cancer 2010, 102:1699-1706.
    • (2010) Br. J. Cancer , vol.102 , pp. 1699-1706
    • Hamberg, P.1    Steeghs, N.2    Loos, W.3    van Biessen, D.4    den Hollander, M.5    Tascilar, M.6    Verweij, J.7    Gelderblom, H.8    Sleijfer, S.9
  • 14
    • 75549090213 scopus 로고    scopus 로고
    • KEGG for representation and analysis of molecular networks involving diseases and drugs
    • Kanehisa M., Goto S., Furumichi M., Tanabe M., Hirakawa M. KEGG for representation and analysis of molecular networks involving diseases and drugs. Nucleic Acids Res. 2010, 38:355-360.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 355-360
    • Kanehisa, M.1    Goto, S.2    Furumichi, M.3    Tanabe, M.4    Hirakawa, M.5
  • 16
    • 37549006456 scopus 로고    scopus 로고
    • Thioredoxin reductase inactivation as a pivotal mechanism of ifosfamide in cancer therapy
    • Wang X., Zhang J., Xu T. Thioredoxin reductase inactivation as a pivotal mechanism of ifosfamide in cancer therapy. Eur. J. Pharmacol. 2008, 579:66-73.
    • (2008) Eur. J. Pharmacol. , vol.579 , pp. 66-73
    • Wang, X.1    Zhang, J.2    Xu, T.3
  • 17
    • 24644441050 scopus 로고    scopus 로고
    • The thioredoxin reductase/thioredoxin system: novel redox targets for cancer therapy
    • Biaglow J.E., Miller R.A. The thioredoxin reductase/thioredoxin system: novel redox targets for cancer therapy. Cancer Biol. Ther. 2005, 4:6-13.
    • (2005) Cancer Biol. Ther. , vol.4 , pp. 6-13
    • Biaglow, J.E.1    Miller, R.A.2
  • 18
    • 33746430147 scopus 로고    scopus 로고
    • Thioredoxin reductase as a novel molecular target for cancer therapy
    • Nguyen P., Awwad R., Smart D., Spitz D., Gius David Thioredoxin reductase as a novel molecular target for cancer therapy. Cancer Lett. 2006, 236:164-174.
    • (2006) Cancer Lett. , vol.236 , pp. 164-174
    • Nguyen, P.1    Awwad, R.2    Smart, D.3    Spitz, D.4    Gius, D.5
  • 19
    • 0034605446 scopus 로고    scopus 로고
    • Role of the heat shock response and molecular chaperones in oncogenesis and cell death
    • Jolly C., Morimoto R.I. Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J. Natl. Cancer Inst. 2000, 92:1564-1572.
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 1564-1572
    • Jolly, C.1    Morimoto, R.I.2
  • 20
    • 0035989680 scopus 로고    scopus 로고
    • HSP90 as a new therapeutic target for cancer therapy: the story unfolds
    • Maloney A., Workman P. HSP90 as a new therapeutic target for cancer therapy: the story unfolds. Expert. Opin. Biol. Ther. 2002, 2:3-24.
    • (2002) Expert. Opin. Biol. Ther. , vol.2 , pp. 3-24
    • Maloney, A.1    Workman, P.2
  • 21
    • 14444277241 scopus 로고    scopus 로고
    • DnaJ/hsp40 chaperone domain of SV40 large T antigen promotes efficient viral DNA replication
    • Campbell K.S., Mullane K.P., Aksoy I.A., Studbal H., Zalvide J., Pipas J.M., et al. DnaJ/hsp40 chaperone domain of SV40 large T antigen promotes efficient viral DNA replication. Genes Dev. 1997, 11:1098-1110.
    • (1997) Genes Dev. , vol.11 , pp. 1098-1110
    • Campbell, K.S.1    Mullane, K.P.2    Aksoy, I.A.3    Studbal, H.4    Zalvide, J.5    Pipas, J.M.6
  • 22
    • 0030935256 scopus 로고    scopus 로고
    • The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the Jdomain of the Escherichia coli DnaJ molecular chaperone
    • Kelley W.L., Georgopoulos C. The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the Jdomain of the Escherichia coli DnaJ molecular chaperone. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:3679-3684.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 3679-3684
    • Kelley, W.L.1    Georgopoulos, C.2
  • 23
    • 0030842474 scopus 로고    scopus 로고
    • The amino-terminal transforming region of simian virus 40 large T and small t antigens functions as a J domain
    • Srinivasan A., McClellan A.J., Vartikar J., Marks I., Cantalupo P., Li Y., et al. The amino-terminal transforming region of simian virus 40 large T and small t antigens functions as a J domain. Mol. Cell. Biol. 1997, 17:4761-4773.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4761-4773
    • Srinivasan, A.1    McClellan, A.J.2    Vartikar, J.3    Marks, I.4    Cantalupo, P.5    Li, Y.6
  • 24
    • 0026649648 scopus 로고
    • The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53- mediated transactivation
    • Momand J., Zambetti G.P., Olson D.C., George D., Levine A.J. The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53- mediated transactivation. Cell 1992, 69:1237-1245.
    • (1992) Cell , vol.69 , pp. 1237-1245
    • Momand, J.1    Zambetti, G.P.2    Olson, D.C.3    George, D.4    Levine, A.J.5
  • 25
    • 53049108040 scopus 로고    scopus 로고
    • Targeting the MDM2-p53 interaction for cancer therapy
    • Shangary S., Wang S. Targeting the MDM2-p53 interaction for cancer therapy. Clin. Cancer Res. 2008, 14:5318-5324.
    • (2008) Clin. Cancer Res. , vol.14 , pp. 5318-5324
    • Shangary, S.1    Wang, S.2
  • 26
    • 0027222956 scopus 로고
    • Mapping of the p53 and mdm-2 interaction domains
    • Chen J., Marechal V., Levine A.J. Mapping of the p53 and mdm-2 interaction domains. Mol. Cell. Biol. 1993, 13:4107-4114.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4107-4114
    • Chen, J.1    Marechal, V.2    Levine, A.J.3
  • 27
    • 67449128222 scopus 로고    scopus 로고
    • Direct interaction between Nrf2 and p21(Cip1/WAF1) upregulates the Nrf2-mediated antioxidant response
    • Chen W., Sun Z., Wang X.J. Direct interaction between Nrf2 and p21(Cip1/WAF1) upregulates the Nrf2-mediated antioxidant response. Mol. Cell 2009, 34:663-673.
    • (2009) Mol. Cell , vol.34 , pp. 663-673
    • Chen, W.1    Sun, Z.2    Wang, X.J.3
  • 28
    • 33745563861 scopus 로고    scopus 로고
    • Decreased Mdm2 expression inhibits tumor development induced by loss of ARF
    • Wang P., Greiner T.C., Lushnikova T., Eischen C.M. Decreased Mdm2 expression inhibits tumor development induced by loss of ARF. Oncogene 2006, 22:3708-3718.
    • (2006) Oncogene , vol.22 , pp. 3708-3718
    • Wang, P.1    Greiner, T.C.2    Lushnikova, T.3    Eischen, C.M.4
  • 29
    • 0034686013 scopus 로고    scopus 로고
    • Integrin mediated RON growth factor receptor phosphorylation requires tyrosine kinase activity of both the receptor and c-Src
    • Danilkovitch-Miagkova A., Angeloni D., Skeel A., Donley S., Lerman M., Leonard E.J. Integrin mediated RON growth factor receptor phosphorylation requires tyrosine kinase activity of both the receptor and c-Src. J. Biol. Chem. 2000, 275:14783-14786.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14783-14786
    • Danilkovitch-Miagkova, A.1    Angeloni, D.2    Skeel, A.3    Donley, S.4    Lerman, M.5    Leonard, E.J.6
  • 30
    • 0035897407 scopus 로고    scopus 로고
    • Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1
    • Aplin A.E., Stewart S.A., Assoian R.K., Juliano R.L. Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1. J. Cell Biol. 2001, 153:273-282.
    • (2001) J. Cell Biol. , vol.153 , pp. 273-282
    • Aplin, A.E.1    Stewart, S.A.2    Assoian, R.K.3    Juliano, R.L.4
  • 31
    • 0036007394 scopus 로고    scopus 로고
    • Association between avB6 integrin expression, elevated p42/44 MAPK, and plasminogen-dependent matrix degradation in ovarian cancer
    • Ahmed N., Pansino F., Baker M., Rice G., Quinn M. Association between avB6 integrin expression, elevated p42/44 MAPK, and plasminogen-dependent matrix degradation in ovarian cancer. J. Cell. Biochem. 2002, 84:675-686.
    • (2002) J. Cell. Biochem. , vol.84 , pp. 675-686
    • Ahmed, N.1    Pansino, F.2    Baker, M.3    Rice, G.4    Quinn, M.5
  • 33
    • 0033151533 scopus 로고    scopus 로고
    • Constitutive activation of extracellular signal-regulated kinase in human acute leukemias: combined role of activation of MEK, hyperexpression of extracellular signal-regulated kinase, and downregulation of a phosphatase, PAC1
    • Kim S., Hahn J., Min Y., Yoo N., Ko Y., Lee W. Constitutive activation of extracellular signal-regulated kinase in human acute leukemias: combined role of activation of MEK, hyperexpression of extracellular signal-regulated kinase, and downregulation of a phosphatase, PAC1. Blood 1999, 93(3893):3899.
    • (1999) Blood , vol.93 , Issue.3893 , pp. 3899
    • Kim, S.1    Hahn, J.2    Min, Y.3    Yoo, N.4    Ko, Y.5    Lee, W.6
  • 34
    • 0030972025 scopus 로고    scopus 로고
    • Constitutive activation of mitogenactivated protein kinase pathway in acute leukemia cells
    • Towatari M., Lida H., Tanimoto M., Iwata H., Hamaguchi M., Saito H. Constitutive activation of mitogenactivated protein kinase pathway in acute leukemia cells. Leukemia 1997, 11:479-484.
    • (1997) Leukemia , vol.11 , pp. 479-484
    • Towatari, M.1    Lida, H.2    Tanimoto, M.3    Iwata, H.4    Hamaguchi, M.5    Saito, H.6
  • 36
    • 0035825597 scopus 로고    scopus 로고
    • Regulation of the expression of c-Myc by [U+F062]1 integrins in epithelial cells
    • Benaud C., Dickson R. Regulation of the expression of c-Myc by [U+F062]1 integrins in epithelial cells. Oncogene 2001, 20:759-768.
    • (2001) Oncogene , vol.20 , pp. 759-768
    • Benaud, C.1    Dickson, R.2
  • 37
    • 56949085161 scopus 로고    scopus 로고
    • Direct regulation of HSP60 expression by c-MYC induces transformation
    • Tsai Y., Teng S., Wu K. Direct regulation of HSP60 expression by c-MYC induces transformation. FEBS Lett. 2008, 582:4083-4088.
    • (2008) FEBS Lett. , vol.582 , pp. 4083-4088
    • Tsai, Y.1    Teng, S.2    Wu, K.3
  • 38
    • 39749137048 scopus 로고    scopus 로고
    • Transcriptional recapitulation and subversion of embryonic colon development by mouse colon tumor models and human colon cancer
    • Kaiser S., Park Y., Franklin J., Halberg R., et al. Transcriptional recapitulation and subversion of embryonic colon development by mouse colon tumor models and human colon cancer. Genome Biol. 2007, 8:R131.
    • (2007) Genome Biol. , vol.8
    • Kaiser, S.1    Park, Y.2    Franklin, J.3    Halberg, R.4
  • 39
    • 73149111923 scopus 로고    scopus 로고
    • Gene Expression Profiles Classify Human Osteosarcoma Xenografts According to Sensitivity to Doxorubicin, vb Cisplatin, and Ifosfamide
    • Bruheim S., Xi Y., Ju J., Fodstad O. Gene Expression Profiles Classify Human Osteosarcoma Xenografts According to Sensitivity to Doxorubicin, vb Cisplatin, and Ifosfamide. Cancer Ther. 2009, 15:7161-7169.
    • (2009) Cancer Ther. , vol.15 , pp. 7161-7169
    • Bruheim, S.1    Xi, Y.2    Ju, J.3    Fodstad, O.4


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