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Volumn 145, Issue 1, 2008, Pages 111-123

Effects of the Proteasome Inhibitor Bortezomib on Gene Expression Profiles of Pancreatic Cancer Cells

Author keywords

oligonucleotide microarray; pancreatic cancer; proteasome inhibitor

Indexed keywords

BORTEZOMIB; GEMCITABINE; PROTEASOME INHIBITOR;

EID: 38949110712     PISSN: 00224804     EISSN: 10958673     Source Type: Journal    
DOI: 10.1016/j.jss.2007.03.061     Document Type: Article
Times cited : (32)

References (43)
  • 1
    • 0031826435 scopus 로고    scopus 로고
    • Ductal adenocarcinoma of the pancreas head: Survival after regional versus extended lymphadenectomy
    • Henne-Bruns D., Vogel I., Luttges J., et al. Ductal adenocarcinoma of the pancreas head: Survival after regional versus extended lymphadenectomy. Hepatogastroenterology 45 (1998) 855
    • (1998) Hepatogastroenterology , vol.45 , pp. 855
    • Henne-Bruns, D.1    Vogel, I.2    Luttges, J.3
  • 2
    • 0031892666 scopus 로고    scopus 로고
    • Lack of survival benefit of extended lymph node dissection for ductal adenocarcinoma of the head of the pancreas: Retrospective multi-institutional analysis in Japan
    • Mukaiya M., Hirata K., Satoh T., et al. Lack of survival benefit of extended lymph node dissection for ductal adenocarcinoma of the head of the pancreas: Retrospective multi-institutional analysis in Japan. World J Surg 22 (1998) 248
    • (1998) World J Surg , vol.22 , pp. 248
    • Mukaiya, M.1    Hirata, K.2    Satoh, T.3
  • 3
    • 0023626809 scopus 로고
    • Cancer of the pancreas. Fifty years of surgery
    • Gudjonsson B. Cancer of the pancreas. Fifty years of surgery. Cancer 60 (1987) 2284
    • (1987) Cancer , vol.60 , pp. 2284
    • Gudjonsson, B.1
  • 4
    • 0141888993 scopus 로고    scopus 로고
    • Treatment of pancreatic cancer: Challenge of the facts
    • Beger H.G., Rau B., Gansauge F., et al. Treatment of pancreatic cancer: Challenge of the facts. World J Surg 27 (2003) 1075
    • (2003) World J Surg , vol.27 , pp. 1075
    • Beger, H.G.1    Rau, B.2    Gansauge, F.3
  • 6
    • 0030631546 scopus 로고    scopus 로고
    • Advances in the diagnosis and treatment of adenocarcinoma of the pancreas
    • Evans D.B., Lee J.E., Pisters P.W., et al. Advances in the diagnosis and treatment of adenocarcinoma of the pancreas. Cancer Treat Res 90 (1997) 109
    • (1997) Cancer Treat Res , vol.90 , pp. 109
    • Evans, D.B.1    Lee, J.E.2    Pisters, P.W.3
  • 7
    • 0001857276 scopus 로고    scopus 로고
    • Cancer of the pancreas
    • DeVita V.T., Hellman S., and Rosenberg A.S. (Eds), J. B. Lippincott Co, Philadelphia
    • Evans D.B., Abbruzzese J.L., and Rich T.A. Cancer of the pancreas. In: DeVita V.T., Hellman S., and Rosenberg A.S. (Eds). Cancer, Principles and Practice of Oncology (1997), J. B. Lippincott Co, Philadelphia 1054
    • (1997) Cancer, Principles and Practice of Oncology , pp. 1054
    • Evans, D.B.1    Abbruzzese, J.L.2    Rich, T.A.3
  • 8
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover A. The ubiquitin-proteasome proteolytic pathway. Cell 79 (1994) 13
    • (1994) Cell , vol.79 , pp. 13
    • Ciechanover, A.1
  • 9
    • 0033152760 scopus 로고    scopus 로고
    • Proteasome inhibitors: A novel class of potent and effective antitumor agents
    • Adams J., Palombella V.J., Sausville E.A., et al. Proteasome inhibitors: A novel class of potent and effective antitumor agents. Cancer Res 59 (1999) 2615
    • (1999) Cancer Res , vol.59 , pp. 2615
    • Adams, J.1    Palombella, V.J.2    Sausville, E.A.3
  • 10
    • 0037973279 scopus 로고    scopus 로고
    • A phase 2 study of bortezomib in relapsed, refractory myeloma
    • Richardson P.G., Barlogie B., Berenson J., et al. A phase 2 study of bortezomib in relapsed, refractory myeloma. N Engl J Med 348 (2003) 2609
    • (2003) N Engl J Med , vol.348 , pp. 2609
    • Richardson, P.G.1    Barlogie, B.2    Berenson, J.3
  • 11
    • 0032919345 scopus 로고    scopus 로고
    • The role of the ubiquitin-proteasome pathway in apoptosis
    • Orlowski R.Z. The role of the ubiquitin-proteasome pathway in apoptosis. Cell Death Differ 6 (1999) 303
    • (1999) Cell Death Differ , vol.6 , pp. 303
    • Orlowski, R.Z.1
  • 13
    • 0038005018 scopus 로고    scopus 로고
    • DAVID: Database for Annotation. Visualization and Integrated Discovery
    • Dennis Jr. G., Sherman B.T., Hosack D.A., et al. DAVID: Database for Annotation. Visualization and Integrated Discovery. Genome Biol 4 (2003) P3
    • (2003) Genome Biol , vol.4
    • Dennis Jr., G.1    Sherman, B.T.2    Hosack, D.A.3
  • 14
    • 17144390205 scopus 로고    scopus 로고
    • Intrinsic chemoresistance to gemcitabine is associated with decreased expression of BNIP3 in pancreatic cancer
    • Akada M., Crnogorac-Jurcevic T., Lattimore S., et al. Intrinsic chemoresistance to gemcitabine is associated with decreased expression of BNIP3 in pancreatic cancer. Clin Cancer Res 11 (2005) 3094
    • (2005) Clin Cancer Res , vol.11 , pp. 3094
    • Akada, M.1    Crnogorac-Jurcevic, T.2    Lattimore, S.3
  • 15
    • 0142152436 scopus 로고    scopus 로고
    • Gadd45-β mediates the protective effects of CD40 costimulation against Fas-induced apoptosis
    • Zazzeroni F., Papa S., Algeciras-Schimnich A., et al. Gadd45-β mediates the protective effects of CD40 costimulation against Fas-induced apoptosis. Blood 102 (2003) 3270
    • (2003) Blood , vol.102 , pp. 3270
    • Zazzeroni, F.1    Papa, S.2    Algeciras-Schimnich, A.3
  • 16
    • 18644367141 scopus 로고    scopus 로고
    • Induction and superinduction of growth arrest and DNA damage gene 45 (GADD45)α andβ messenger RNAs by histone deacetylase inhibitors trichostatin A (TSA) and butyrate in SW620 human colon carcinoma cells
    • Chen Z., Clark S., Birkeland M., et al. Induction and superinduction of growth arrest and DNA damage gene 45 (GADD45)α andβ messenger RNAs by histone deacetylase inhibitors trichostatin A (TSA) and butyrate in SW620 human colon carcinoma cells. Cancer Lett 188 (2002) 127
    • (2002) Cancer Lett , vol.188 , pp. 127
    • Chen, Z.1    Clark, S.2    Birkeland, M.3
  • 17
    • 0035889252 scopus 로고    scopus 로고
    • Induction of gadd45-β by NF-κB down-regulates proapoptotic JNK signaling
    • De Smaele E., Zazzeroni F., Papa S., et al. Induction of gadd45-β by NF-κB down-regulates proapoptotic JNK signaling. Nature 414 (2001) 308
    • (2001) Nature , vol.414 , pp. 308
    • De Smaele, E.1    Zazzeroni, F.2    Papa, S.3
  • 18
    • 33749243499 scopus 로고    scopus 로고
    • Proteasome inhibition induces both pro- and anti-cell death pathways in prostate cancer cells
    • Yang W., Monroe J., Zhang Y., et al. Proteasome inhibition induces both pro- and anti-cell death pathways in prostate cancer cells. Cancer Lett 243 (2006) 217
    • (2006) Cancer Lett , vol.243 , pp. 217
    • Yang, W.1    Monroe, J.2    Zhang, Y.3
  • 19
    • 20444425287 scopus 로고    scopus 로고
    • NF-κB and not the MAPK signaling pathway regulates GADD45β expression during acute inflammation
    • Zhang N., Ahsan M.H., Zhu L., et al. NF-κB and not the MAPK signaling pathway regulates GADD45β expression during acute inflammation. J Biol Chem 280 (2005) 21400
    • (2005) J Biol Chem , vol.280 , pp. 21400
    • Zhang, N.1    Ahsan, M.H.2    Zhu, L.3
  • 20
    • 33846274182 scopus 로고    scopus 로고
    • Treatment of cultured myotubes with the proteasome inhibitor β-lactone increases the expression of the transcription factor c/EBPβ
    • Wei W., Yang H., Menconi M., et al. Treatment of cultured myotubes with the proteasome inhibitor β-lactone increases the expression of the transcription factor c/EBPβ. Am J Physiol Cell Physiol 292 (2007) C216
    • (2007) Am J Physiol Cell Physiol , vol.292
    • Wei, W.1    Yang, H.2    Menconi, M.3
  • 21
    • 33745190973 scopus 로고    scopus 로고
    • Selective inhibition of endoplasmic reticulum-associated degradation rescues δF508-cystic fibrosis transmembrane regulator and suppresses interleukin-8 levels: Therapeutic implications
    • Vij N., Fang S., and Zeitlin P.L. Selective inhibition of endoplasmic reticulum-associated degradation rescues δF508-cystic fibrosis transmembrane regulator and suppresses interleukin-8 levels: Therapeutic implications. J Biol Chem 281 (2006) 17369
    • (2006) J Biol Chem , vol.281 , pp. 17369
    • Vij, N.1    Fang, S.2    Zeitlin, P.L.3
  • 22
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • Obeng E.A., Carlson L.M., Gutman D.M., et al. Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells. Blood 107 (2006) 4907
    • (2006) Blood , vol.107 , pp. 4907
    • Obeng, E.A.1    Carlson, L.M.2    Gutman, D.M.3
  • 23
    • 0034622020 scopus 로고    scopus 로고
    • Proteasome inhibitor induced gene expression profiles reveal overexpression of transcriptional regulators ATF3. GADD153 and MAD1
    • Zimmermann J., Erdmann D., Lalande I., et al. Proteasome inhibitor induced gene expression profiles reveal overexpression of transcriptional regulators ATF3. GADD153 and MAD1. Oncogene 19 (2000) 2913
    • (2000) Oncogene , vol.19 , pp. 2913
    • Zimmermann, J.1    Erdmann, D.2    Lalande, I.3
  • 24
    • 0041703031 scopus 로고    scopus 로고
    • The function of GADD34 is a recovery from a shutoff of protein synthesis-induced by ER stress: Elucidation by GADD34-deficient mice
    • Kojima E., Takeuchi A., Haneda M., et al. The function of GADD34 is a recovery from a shutoff of protein synthesis-induced by ER stress: Elucidation by GADD34-deficient mice. FASEB J 17 (2003) 1573
    • (2003) FASEB J , vol.17 , pp. 1573
    • Kojima, E.1    Takeuchi, A.2    Haneda, M.3
  • 25
    • 0038641980 scopus 로고    scopus 로고
    • Human BAG-1 proteins bind to the cellular stress response protein GADD34 and interfere with GADD34 functions
    • Hung W.J., Roberson R.S., Taft J., et al. Human BAG-1 proteins bind to the cellular stress response protein GADD34 and interfere with GADD34 functions. Mol Cell Biol 23 (2003) 3477
    • (2003) Mol Cell Biol , vol.23 , pp. 3477
    • Hung, W.J.1    Roberson, R.S.2    Taft, J.3
  • 26
    • 0032722324 scopus 로고    scopus 로고
    • HSP27 inhibits cytochrome c-dependent activation of procaspase-9
    • Garrido C., Bruey J.M., Fromentin A., et al. HSP27 inhibits cytochrome c-dependent activation of procaspase-9. FASEB J 13 (1999) 2061
    • (1999) FASEB J , vol.13 , pp. 2061
    • Garrido, C.1    Bruey, J.M.2    Fromentin, A.3
  • 27
    • 0029933741 scopus 로고    scopus 로고
    • Human hsp27, drosophila hsp27, and human αB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNFα-induced cell death
    • Mehlen P., Kretz-Remy C., Preville X., et al. Human hsp27, drosophila hsp27, and human αB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNFα-induced cell death. EMBO J 15 (1996) 2695
    • (1996) EMBO J , vol.15 , pp. 2695
    • Mehlen, P.1    Kretz-Remy, C.2    Preville, X.3
  • 28
    • 0033516660 scopus 로고    scopus 로고
    • Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor α by phosphorylation
    • Rogalla T., Ehrnsperger M., Preville X., et al. Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor α by phosphorylation. J Biol Chem 274 (1999) 18947
    • (1999) J Biol Chem , vol.274 , pp. 18947
    • Rogalla, T.1    Ehrnsperger, M.2    Preville, X.3
  • 29
    • 1242315877 scopus 로고    scopus 로고
    • HSP27 and HSP70: Potentially oncogenic apoptosis inhibitors
    • Garrido C., Schmitt E., Cande C., et al. HSP27 and HSP70: Potentially oncogenic apoptosis inhibitors. Cell Cycle 2 (2003) 579
    • (2003) Cell Cycle , vol.2 , pp. 579
    • Garrido, C.1    Schmitt, E.2    Cande, C.3
  • 30
    • 0242496212 scopus 로고    scopus 로고
    • Molecular sequelae of proteasome inhibition in human multiple myeloma cells
    • Mitsiades N., Mitsiades C.S., Poulaki V., et al. Molecular sequelae of proteasome inhibition in human multiple myeloma cells. Proc Natl Acad Sci USA 99 (2002) 14374
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14374
    • Mitsiades, N.1    Mitsiades, C.S.2    Poulaki, V.3
  • 31
    • 29244454269 scopus 로고    scopus 로고
    • Bortezomib sensitizes pancreatic cancer cells to endoplasmic reticulum stress-mediated apoptosis
    • Nawrocki S.T., Carew J.S., Pino M.S., et al. Bortezomib sensitizes pancreatic cancer cells to endoplasmic reticulum stress-mediated apoptosis. Cancer Res 65 (2005) 11658
    • (2005) Cancer Res , vol.65 , pp. 11658
    • Nawrocki, S.T.1    Carew, J.S.2    Pino, M.S.3
  • 32
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers K.J., Patil C.K., Wodicka L., et al. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101 (2000) 249
    • (2000) Cell , vol.101 , pp. 249
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3
  • 33
    • 10444226462 scopus 로고    scopus 로고
    • ER stress and the unfolded protein response
    • Schroder M., and Kaufman R.J. ER stress and the unfolded protein response. Mutat Res 569 (2005) 29
    • (2005) Mutat Res , vol.569 , pp. 29
    • Schroder, M.1    Kaufman, R.J.2
  • 34
    • 0042812063 scopus 로고    scopus 로고
    • Frame switch splicing and regulated intra-membrane proteolysis: Key words to understand the unfolded protein response
    • Mori K. Frame switch splicing and regulated intra-membrane proteolysis: Key words to understand the unfolded protein response. Traffic 4 (2003) 519
    • (2003) Traffic , vol.4 , pp. 519
    • Mori, K.1
  • 35
    • 0842285401 scopus 로고    scopus 로고
    • Cytoprotection by preemptive conditional phosphorylation of translation initiation factor 2
    • Lu P.D., Jousse C., Marciniak S.J., et al. Cytoprotection by preemptive conditional phosphorylation of translation initiation factor 2. EMBO J 23 (2004) 169
    • (2004) EMBO J , vol.23 , pp. 169
    • Lu, P.D.1    Jousse, C.2    Marciniak, S.J.3
  • 36
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia R., and Braakman I. Quality control in the endoplasmic reticulum protein factory. Nature 426 (2003) 891
    • (2003) Nature , vol.426 , pp. 891
    • Sitia, R.1    Braakman, I.2
  • 37
    • 33845520806 scopus 로고    scopus 로고
    • Proteasome inhibitors: Antitumor effects and beyond
    • Nencioni A., Grunebach F., Patrone F., et al. Proteasome inhibitors: Antitumor effects and beyond. Leukemia 21 (2007) 30
    • (2007) Leukemia , vol.21 , pp. 30
    • Nencioni, A.1    Grunebach, F.2    Patrone, F.3
  • 38
    • 32944454483 scopus 로고    scopus 로고
    • Targeting heat shock response to sensitize cancer cells to proteasome and Hsp90 inhibitors
    • Zaarur N., Gabai V.L., Porco Jr. J.A., et al. Targeting heat shock response to sensitize cancer cells to proteasome and Hsp90 inhibitors. Cancer Res 66 (2006) 1783
    • (2006) Cancer Res , vol.66 , pp. 1783
    • Zaarur, N.1    Gabai, V.L.2    Porco Jr., J.A.3
  • 39
    • 0037780982 scopus 로고    scopus 로고
    • Mitogenic and antiapoptotic role of constitutive NF-κB/Rel activity in pancreatic cancer
    • Liptay S., Weber C.K., Ludwig L., et al. Mitogenic and antiapoptotic role of constitutive NF-κB/Rel activity in pancreatic cancer. Int J Cancer 105 (2003) 735
    • (2003) Int J Cancer , vol.105 , pp. 735
    • Liptay, S.1    Weber, C.K.2    Ludwig, L.3
  • 40
    • 1842850737 scopus 로고    scopus 로고
    • Increased expression of NF-κ B subunits in human pancreatic cancer cells
    • Chandler N.M., Canete J.J., and Callery M.P. Increased expression of NF-κ B subunits in human pancreatic cancer cells. J Surg Res 118 (2004) 9
    • (2004) J Surg Res , vol.118 , pp. 9
    • Chandler, N.M.1    Canete, J.J.2    Callery, M.P.3
  • 41
    • 7644223910 scopus 로고    scopus 로고
    • Nuclear factor-κB and IκB kinase are constitutively active in human pancreatic cells and their down-regulation by curcumin (diferuloyl methane) is associated with the suppression of proliferation and the induction of apoptosis
    • Li L., Aggarwal B.B., Shishodia S., et al. Nuclear factor-κB and IκB kinase are constitutively active in human pancreatic cells and their down-regulation by curcumin (diferuloyl methane) is associated with the suppression of proliferation and the induction of apoptosis. Cancer 01 (2004) 2351
    • (2004) Cancer , vol.1 , pp. 2351
    • Li, L.1    Aggarwal, B.B.2    Shishodia, S.3
  • 42
    • 0038621384 scopus 로고    scopus 로고
    • Role of NF-κB and Akt/PI3K in the resistance of pancreatic carcinoma cell lines against gemcitabine-induced cell death
    • Arlt A., Gehrz A., Muerkoster S., et al. Role of NF-κB and Akt/PI3K in the resistance of pancreatic carcinoma cell lines against gemcitabine-induced cell death. Oncogene 22 (2003) 3243
    • (2003) Oncogene , vol.22 , pp. 3243
    • Arlt, A.1    Gehrz, A.2    Muerkoster, S.3
  • 43
    • 25444493107 scopus 로고    scopus 로고
    • Molecular evidence for increased antitumor activity of gemcitabine by genistein in vitro and in vivo using an orthotopic model of pancreatic cancer
    • Banerjee S., Zhang Y., Ali S., et al. Molecular evidence for increased antitumor activity of gemcitabine by genistein in vitro and in vivo using an orthotopic model of pancreatic cancer. Cancer Res 65 (2005) 9064
    • (2005) Cancer Res , vol.65 , pp. 9064
    • Banerjee, S.1    Zhang, Y.2    Ali, S.3


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