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Volumn 332, Issue 2, 2013, Pages 313-324

Targeting apoptosis pathways by Celecoxib in cancer

Author keywords

Apoptosis; Bcl 2; Celecoxib; COX 2; Mcl 1

Indexed keywords

2 AMINO N [4 [5 (2 PHENANTHRENYL) 3 TRIFLUOROMETHYL 1H PYRAZOL 1 YL]PHENYL]ACETAMIDE; 2,5 DIMETHYLCELECOXIB; ANTINEOPLASTIC AGENT; BETA CATENIN; CALCIUM ION; CASPASE 8; CELECOXIB; CYCLIN DEPENDENT KINASE INHIBITOR; CYCLINE; CYCLOOXYGENASE 2; CYCLOOXYGENASE 2 INHIBITOR; FAS ASSOCIATED DEATH DOMAIN PROTEIN; IBUPROFEN; NAPROXEN; PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN KINASE B; PROTEIN KINASE R; PROTEIN MCL 1; PROTEIN NOXA; ROFECOXIB; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; SURVIVIN; UNCLASSIFIED DRUG; VALDECOXIB;

EID: 84876078256     PISSN: 03043835     EISSN: 18727980     Source Type: Journal    
DOI: 10.1016/j.canlet.2011.01.012     Document Type: Review
Times cited : (166)

References (143)
  • 1
    • 18444408375 scopus 로고    scopus 로고
    • COX-2: a molecular target for colorectal cancer prevention
    • Brown J.R., DuBois R.N. COX-2: a molecular target for colorectal cancer prevention. J. Clin. Oncol. 2005, 23:2840-2855.
    • (2005) J. Clin. Oncol. , vol.23 , pp. 2840-2855
    • Brown, J.R.1    DuBois, R.N.2
  • 2
    • 0033590207 scopus 로고    scopus 로고
    • The role of cyclooxygenases in inflammation, cancer, and development
    • Williams C.S., Mann M., DuBois R.N. The role of cyclooxygenases in inflammation, cancer, and development. Oncogene 1999, 18:7908-7916.
    • (1999) Oncogene , vol.18 , pp. 7908-7916
    • Williams, C.S.1    Mann, M.2    DuBois, R.N.3
  • 3
    • 0033988665 scopus 로고    scopus 로고
    • Over-expression of cyclooxygenase-2 in human prostate adenocarcinoma
    • Gupta S., Srivastava M., Ahmad N., Bostwick D.G., Mukhtar H. Over-expression of cyclooxygenase-2 in human prostate adenocarcinoma. Prostate 2000, 42:73-78.
    • (2000) Prostate , vol.42 , pp. 73-78
    • Gupta, S.1    Srivastava, M.2    Ahmad, N.3    Bostwick, D.G.4    Mukhtar, H.5
  • 7
    • 70449633544 scopus 로고    scopus 로고
    • Inhibition of cyclooxygenase-2 suppresses lymph node metastasis via VEGF-C
    • Liu H., Yang Y., Xiao J., Lv Y., Liu Y., Yang H., Zhao L. Inhibition of cyclooxygenase-2 suppresses lymph node metastasis via VEGF-C. Anat. Rec. (Hoboken) 2009, 292:1577-1583.
    • (2009) Anat. Rec. (Hoboken) , vol.292 , pp. 1577-1583
    • Liu, H.1    Yang, Y.2    Xiao, J.3    Lv, Y.4    Liu, Y.5    Yang, H.6    Zhao, L.7
  • 11
    • 0034326837 scopus 로고    scopus 로고
    • Celecoxib prevents tumor growth in vivo without toxicity to normal gut: lack of correlation between in vitro and in vivo models
    • Williams C.S., Watson A.J., Sheng H., Helou R., Shao J., DuBois R.N. Celecoxib prevents tumor growth in vivo without toxicity to normal gut: lack of correlation between in vitro and in vivo models. Cancer Res. 2000, 60:6045-6051.
    • (2000) Cancer Res. , vol.60 , pp. 6045-6051
    • Williams, C.S.1    Watson, A.J.2    Sheng, H.3    Helou, R.4    Shao, J.5    DuBois, R.N.6
  • 12
    • 9444296055 scopus 로고    scopus 로고
    • Cyclooxygenase-2-dependent and -independent effects of celecoxib in pancreatic cancer cell lines
    • El-Rayes B.F., Ali S., Sarkar F.H., Philip P.A. Cyclooxygenase-2-dependent and -independent effects of celecoxib in pancreatic cancer cell lines. Mol. Cancer Ther. 2004, 3:1421-1426.
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 1421-1426
    • El-Rayes, B.F.1    Ali, S.2    Sarkar, F.H.3    Philip, P.A.4
  • 13
    • 5644294350 scopus 로고    scopus 로고
    • Cyclooxygenase-2 is expressed in neuroblastoma, and nonsteroidal anti-inflammatory drugs induce apoptosis and inhibit tumor growth in vivo
    • Johnsen J.I., Lindskog M., Ponthan F., Pettersen I., Elfman L., Orrego A., Sveinbjornsson B., Kogner P. Cyclooxygenase-2 is expressed in neuroblastoma, and nonsteroidal anti-inflammatory drugs induce apoptosis and inhibit tumor growth in vivo. Cancer Res. 2004, 64:7210-7215.
    • (2004) Cancer Res. , vol.64 , pp. 7210-7215
    • Johnsen, J.I.1    Lindskog, M.2    Ponthan, F.3    Pettersen, I.4    Elfman, L.5    Orrego, A.6    Sveinbjornsson, B.7    Kogner, P.8
  • 15
    • 0036531924 scopus 로고    scopus 로고
    • Celecoxib exhibits the greatest potency amongst cyclooxygenase (COX) inhibitors for growth inhibition of COX-2-negative hematopoietic and epithelial cell lines
    • Waskewich C., Blumenthal R.D., Li H., Stein R., Goldenberg D.M., Burton J. Celecoxib exhibits the greatest potency amongst cyclooxygenase (COX) inhibitors for growth inhibition of COX-2-negative hematopoietic and epithelial cell lines. Cancer Res. 2002, 62:2029-2033.
    • (2002) Cancer Res. , vol.62 , pp. 2029-2033
    • Waskewich, C.1    Blumenthal, R.D.2    Li, H.3    Stein, R.4    Goldenberg, D.M.5    Burton, J.6
  • 17
    • 0034026144 scopus 로고    scopus 로고
    • Cyclooxygenase-2 inhibitor induces apoptosis and enhances cytotoxicity of various anticancer agents in non-small cell lung cancer cell lines
    • Hida T., Kozaki K., Muramatsu H., Masuda A., Shimizu S., Mitsudomi T., Sugiura T., Ogawa M., Takahashi T. Cyclooxygenase-2 inhibitor induces apoptosis and enhances cytotoxicity of various anticancer agents in non-small cell lung cancer cell lines. Clin. Cancer Res. 2000, 6:2006-2011.
    • (2000) Clin. Cancer Res. , vol.6 , pp. 2006-2011
    • Hida, T.1    Kozaki, K.2    Muramatsu, H.3    Masuda, A.4    Shimizu, S.5    Mitsudomi, T.6    Sugiura, T.7    Ogawa, M.8    Takahashi, T.9
  • 19
    • 3042836326 scopus 로고    scopus 로고
    • COX-2 inhibition and lung cancer
    • Sandler A.B., Dubinett S.M. COX-2 inhibition and lung cancer. Semin. Oncol. 2004, 31:45-52.
    • (2004) Semin. Oncol. , vol.31 , pp. 45-52
    • Sandler, A.B.1    Dubinett, S.M.2
  • 20
    • 0033199927 scopus 로고    scopus 로고
    • Enhancement of tumor response to gamma-radiation by an inhibitor of cyclooxygenase-2 enzyme
    • Milas L., Kishi K., Hunter N., Mason K., Masferrer J.L., Tofilon P.J. Enhancement of tumor response to gamma-radiation by an inhibitor of cyclooxygenase-2 enzyme. J. Natl. Cancer Inst. 1999, 91:1501-1504.
    • (1999) J. Natl. Cancer Inst. , vol.91 , pp. 1501-1504
    • Milas, L.1    Kishi, K.2    Hunter, N.3    Mason, K.4    Masferrer, J.L.5    Tofilon, P.J.6
  • 21
    • 1642494834 scopus 로고    scopus 로고
    • Synergy between celecoxib and radiotherapy results from inhibition of cyclooxygenase-2-derived prostaglandin E2, a survival factor for tumor and associated vasculature
    • Davis T.W., O'Neal J.M., Pagel M.D., Zweifel B.S., Mehta P.P., Heuvelman D.M., Masferrer J.L. Synergy between celecoxib and radiotherapy results from inhibition of cyclooxygenase-2-derived prostaglandin E2, a survival factor for tumor and associated vasculature. Cancer Res. 2004, 64:279-285.
    • (2004) Cancer Res. , vol.64 , pp. 279-285
    • Davis, T.W.1    O'Neal, J.M.2    Pagel, M.D.3    Zweifel, B.S.4    Mehta, P.P.5    Heuvelman, D.M.6    Masferrer, J.L.7
  • 22
    • 34347240794 scopus 로고    scopus 로고
    • Chemical radiosensitizers for use in radiotherapy
    • Wardman P. Chemical radiosensitizers for use in radiotherapy. Clin. Oncol. (R Coll. Radiol.) 2007, 19:397-417.
    • (2007) Clin. Oncol. (R Coll. Radiol.) , vol.19 , pp. 397-417
    • Wardman, P.1
  • 23
    • 33745238704 scopus 로고    scopus 로고
    • Cyclooxygenase-2 (COX-2)-independent anticarcinogenic effects of selective COX-2 inhibitors
    • Grosch S., Maier T.J., Schiffmann S., Geisslinger G. Cyclooxygenase-2 (COX-2)-independent anticarcinogenic effects of selective COX-2 inhibitors. J. Natl. Cancer Inst. 2006, 98:736-747.
    • (2006) J. Natl. Cancer Inst. , vol.98 , pp. 736-747
    • Grosch, S.1    Maier, T.J.2    Schiffmann, S.3    Geisslinger, G.4
  • 24
    • 0041703017 scopus 로고    scopus 로고
    • Celecoxib activates a novel mitochondrial apoptosis signaling pathway
    • Jendrossek V., Handrick R., Belka C. Celecoxib activates a novel mitochondrial apoptosis signaling pathway. FASEB J. 2003, 17:1547-1549.
    • (2003) FASEB J. , vol.17 , pp. 1547-1549
    • Jendrossek, V.1    Handrick, R.2    Belka, C.3
  • 25
    • 0037123345 scopus 로고    scopus 로고
    • Cyclooxygenase-2, player or spectator in cyclooxygenase-2 inhibitor-induced apoptosis in prostate cancer cells
    • Song X., Lin H.P., Johnson A.J., Tseng P.H., Yang Y.T., Kulp S.K., Chen C.S. Cyclooxygenase-2, player or spectator in cyclooxygenase-2 inhibitor-induced apoptosis in prostate cancer cells. J. Natl. Cancer Inst. 2002, 94:585-591.
    • (2002) J. Natl. Cancer Inst. , vol.94 , pp. 585-591
    • Song, X.1    Lin, H.P.2    Johnson, A.J.3    Tseng, P.H.4    Yang, Y.T.5    Kulp, S.K.6    Chen, C.S.7
  • 26
    • 0035650943 scopus 로고    scopus 로고
    • COX-2 independent induction of cell cycle arrest and apoptosis in colon cancer cells by the selective COX-2 inhibitor celecoxib
    • Grosch S., Tegeder I., Niederberger E., Brautigam L., Geisslinger G. COX-2 independent induction of cell cycle arrest and apoptosis in colon cancer cells by the selective COX-2 inhibitor celecoxib. FASEB J. 2001, 15:2742-2744.
    • (2001) FASEB J. , vol.15 , pp. 2742-2744
    • Grosch, S.1    Tegeder, I.2    Niederberger, E.3    Brautigam, L.4    Geisslinger, G.5
  • 27
    • 0036468287 scopus 로고    scopus 로고
    • Cyclooxygenase-2 inhibition by celecoxib reduces proliferation and induces apoptosis in angiogenic endothelial cells in vivo
    • Leahy K.M., Ornberg R.L., Wang Y., Zweifel B.S., Koki A.T., Masferrer J.L. Cyclooxygenase-2 inhibition by celecoxib reduces proliferation and induces apoptosis in angiogenic endothelial cells in vivo. Cancer Res. 2002, 62:625-631.
    • (2002) Cancer Res. , vol.62 , pp. 625-631
    • Leahy, K.M.1    Ornberg, R.L.2    Wang, Y.3    Zweifel, B.S.4    Koki, A.T.5    Masferrer, J.L.6
  • 28
    • 12344290399 scopus 로고    scopus 로고
    • Growth inhibitory effects of celecoxib in human umbilical vein endothelial cells are mediated through G1 arrest via multiple signaling mechanisms
    • Lin H.P., Kulp S.K., Tseng P.H., Yang Y.T., Yang C.C., Chen C.S. Growth inhibitory effects of celecoxib in human umbilical vein endothelial cells are mediated through G1 arrest via multiple signaling mechanisms. Mol. Cancer Ther. 2004, 3:1671-1680.
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 1671-1680
    • Lin, H.P.1    Kulp, S.K.2    Tseng, P.H.3    Yang, Y.T.4    Yang, C.C.5    Chen, C.S.6
  • 30
    • 43249093771 scopus 로고    scopus 로고
    • Therapeutic targeting of death pathways in cancer: mechanisms for activating cell death in cancer cells
    • Tan T.T., White E. Therapeutic targeting of death pathways in cancer: mechanisms for activating cell death in cancer cells. Adv. Exp. Med. Biol. 2008, 615:81-104.
    • (2008) Adv. Exp. Med. Biol. , vol.615 , pp. 81-104
    • Tan, T.T.1    White, E.2
  • 31
    • 33746886979 scopus 로고    scopus 로고
    • Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy
    • Fulda S., Debatin K.M. Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy. Oncogene 2006, 25:4798-4811.
    • (2006) Oncogene , vol.25 , pp. 4798-4811
    • Fulda, S.1    Debatin, K.M.2
  • 32
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D., Weinberg R.A. The hallmarks of cancer. Cell 2000, 100:57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 34
    • 56249102048 scopus 로고    scopus 로고
    • Apoptosis and non-apoptotic deaths in cancer development and treatment response
    • de Bruin E.C., Medema J.P. Apoptosis and non-apoptotic deaths in cancer development and treatment response. Cancer Treat. Rev. 2008, 34:737-749.
    • (2008) Cancer Treat. Rev. , vol.34 , pp. 737-749
    • de Bruin, E.C.1    Medema, J.P.2
  • 35
    • 10044277941 scopus 로고    scopus 로고
    • Cyclic exposure to hypoxia and reoxygenation selects for tumor cells with defects in mitochondrial apoptotic pathways
    • (Epub 2004 Sep 28)
    • Weinmann M., Jendrossek V., Guner D., Goecke B., Belka C. Cyclic exposure to hypoxia and reoxygenation selects for tumor cells with defects in mitochondrial apoptotic pathways. FASEB J. 2004, 18:1906-1908. (Epub 2004 Sep 28).
    • (2004) FASEB J. , vol.18 , pp. 1906-1908
    • Weinmann, M.1    Jendrossek, V.2    Guner, D.3    Goecke, B.4    Belka, C.5
  • 37
    • 44349130906 scopus 로고    scopus 로고
    • COX-2 inhibition is neither necessary nor sufficient for celecoxib to suppress tumor cell proliferation and focus formation in vitro
    • Chuang H.C., Kardosh A., Gaffney K.J., Petasis N.A., Schonthal A.H. COX-2 inhibition is neither necessary nor sufficient for celecoxib to suppress tumor cell proliferation and focus formation in vitro. Mol. Cancer 2008, 7:38.
    • (2008) Mol. Cancer , vol.7 , pp. 38
    • Chuang, H.C.1    Kardosh, A.2    Gaffney, K.J.3    Petasis, N.A.4    Schonthal, A.H.5
  • 38
    • 3042562279 scopus 로고    scopus 로고
    • From the cyclooxygenase-2 inhibitor celecoxib to a novel class of 3-phosphoinositide-dependent protein kinase-1 inhibitors
    • Zhu J., Huang J.W., Tseng P.H., Yang Y.T., Fowble J., Shiau C.W., Shaw Y.J., Kulp S.K., Chen C.S. From the cyclooxygenase-2 inhibitor celecoxib to a novel class of 3-phosphoinositide-dependent protein kinase-1 inhibitors. Cancer Res. 2004, 64:4309-4318.
    • (2004) Cancer Res. , vol.64 , pp. 4309-4318
    • Zhu, J.1    Huang, J.W.2    Tseng, P.H.3    Yang, Y.T.4    Fowble, J.5    Shiau, C.W.6    Shaw, Y.J.7    Kulp, S.K.8    Chen, C.S.9
  • 39
    • 0041435754 scopus 로고    scopus 로고
    • Celecoxib induces apoptosis by inhibiting 3-phosphoinositide-dependent protein kinase-1 activity in the human colon cancer cell line HT-29
    • Arico S., Pattingre S., Bauvy C., Gane P., Barbat A., Codogno P., Ogier-Denis E. Celecoxib induces apoptosis by inhibiting 3-phosphoinositide-dependent protein kinase-1 activity in the human colon cancer cell line HT-29. J. Biol. Chem. 2002, 8:8.
    • (2002) J. Biol. Chem. , vol.8 , pp. 8
    • Arico, S.1    Pattingre, S.2    Bauvy, C.3    Gane, P.4    Barbat, A.5    Codogno, P.6    Ogier-Denis, E.7
  • 40
    • 0034646688 scopus 로고    scopus 로고
    • The cyclooxygenase-2 inhibitor celecoxib induces apoptosis by blocking Akt activation in human prostate cancer cells independently of Bcl-2
    • Hsu A.L., Ching T.T., Wang D.S., Song X., Rangnekar V.M., Chen C.S. The cyclooxygenase-2 inhibitor celecoxib induces apoptosis by blocking Akt activation in human prostate cancer cells independently of Bcl-2. J. Biol. Chem. 2000, 275:11397-11403.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11397-11403
    • Hsu, A.L.1    Ching, T.T.2    Wang, D.S.3    Song, X.4    Rangnekar, V.M.5    Chen, C.S.6
  • 41
    • 33745226982 scopus 로고    scopus 로고
    • Downregulation of survivin expression and concomitant induction of apoptosis by celecoxib and its non-cyclooxygenase-2-inhibitory analog, dimethyl-celecoxib (DMC), in tumor cells in vitro and in vivo
    • Pyrko P., Soriano N., Kardosh A., Liu Y.T., Uddin J., Petasis N.A., Hofman F.M., Chen C.S., Chen T.C., Schonthal A.H. Downregulation of survivin expression and concomitant induction of apoptosis by celecoxib and its non-cyclooxygenase-2-inhibitory analog, dimethyl-celecoxib (DMC), in tumor cells in vitro and in vivo. Mol. Cancer 2006, 5:19.
    • (2006) Mol. Cancer , vol.5 , pp. 19
    • Pyrko, P.1    Soriano, N.2    Kardosh, A.3    Liu, Y.T.4    Uddin, J.5    Petasis, N.A.6    Hofman, F.M.7    Chen, C.S.8    Chen, T.C.9    Schonthal, A.H.10
  • 42
    • 70350199628 scopus 로고    scopus 로고
    • Differential effects of anti-apoptotic Bcl-2 family members Mcl-1, Bcl-2, and Bcl-xL on celecoxib-induced apoptosis
    • Rudner J., Elsaesser S.J., Muller A.C., Belka C., Jendrossek V. Differential effects of anti-apoptotic Bcl-2 family members Mcl-1, Bcl-2, and Bcl-xL on celecoxib-induced apoptosis. Biochem. Pharmacol. 2010, 79:10-20.
    • (2010) Biochem. Pharmacol. , vol.79 , pp. 10-20
    • Rudner, J.1    Elsaesser, S.J.2    Muller, A.C.3    Belka, C.4    Jendrossek, V.5
  • 43
    • 0037106343 scopus 로고    scopus 로고
    • The cyclo-oxygenase-2 inhibitor celecoxib perturbs intracellular calcium by inhibiting endoplasmic reticulum Ca2+-ATPases: a plausible link with its anti-tumour effect and cardiovascular risks
    • Johnson A.J., Hsu A.L., Lin H.P., Song X., Chen C.S. The cyclo-oxygenase-2 inhibitor celecoxib perturbs intracellular calcium by inhibiting endoplasmic reticulum Ca2+-ATPases: a plausible link with its anti-tumour effect and cardiovascular risks. Biochem. J. 2002, 366:831-837.
    • (2002) Biochem. J. , vol.366 , pp. 831-837
    • Johnson, A.J.1    Hsu, A.L.2    Lin, H.P.3    Song, X.4    Chen, C.S.5
  • 45
    • 36448957271 scopus 로고    scopus 로고
    • Direct non-cyclooxygenase-2 targets of celecoxib and their potential relevance for cancer therapy
    • Schonthal A.H. Direct non-cyclooxygenase-2 targets of celecoxib and their potential relevance for cancer therapy. Br. J. Cancer 2007, 97:1465-1468.
    • (2007) Br. J. Cancer , vol.97 , pp. 1465-1468
    • Schonthal, A.H.1
  • 47
    • 37349122562 scopus 로고    scopus 로고
    • Celecoxib transiently inhibits cellular protein synthesis
    • Pyrko P., Kardosh A., Schonthal A.H. Celecoxib transiently inhibits cellular protein synthesis. Biochem. Pharmacol. 2008, 75:395-404.
    • (2008) Biochem. Pharmacol. , vol.75 , pp. 395-404
    • Pyrko, P.1    Kardosh, A.2    Schonthal, A.H.3
  • 48
    • 33244495918 scopus 로고    scopus 로고
    • Celecoxib upregulates endoplasmic reticulum chaperones that inhibit celecoxib-induced apoptosis in human gastric cells
    • Tsutsumi S., Namba T., Tanaka K.I., Arai Y., Ishihara T., Aburaya M., Mima S., Hoshino T., Mizushima T. Celecoxib upregulates endoplasmic reticulum chaperones that inhibit celecoxib-induced apoptosis in human gastric cells. Oncogene 2006, 25:1018-1029.
    • (2006) Oncogene , vol.25 , pp. 1018-1029
    • Tsutsumi, S.1    Namba, T.2    Tanaka, K.I.3    Arai, Y.4    Ishihara, T.5    Aburaya, M.6    Mima, S.7    Hoshino, T.8    Mizushima, T.9
  • 49
    • 9344255475 scopus 로고    scopus 로고
    • Cyclooxygenase-2 inhibitor induces apoptosis in breast cancer cells in an in vivo model of spontaneous metastatic breast cancer
    • Basu G.D., Pathangey L.B., Tinder T.L., Lagioia M., Gendler S.J., Mukherjee P. Cyclooxygenase-2 inhibitor induces apoptosis in breast cancer cells in an in vivo model of spontaneous metastatic breast cancer. Mol. Cancer Res. 2004, 2:632-642.
    • (2004) Mol. Cancer Res. , vol.2 , pp. 632-642
    • Basu, G.D.1    Pathangey, L.B.2    Tinder, T.L.3    Lagioia, M.4    Gendler, S.J.5    Mukherjee, P.6
  • 50
    • 9344225155 scopus 로고    scopus 로고
    • Regression of mouse prostatic intraepithelial neoplasia by nonsteroidal anti-inflammatory drugs in the transgenic adenocarcinoma mouse prostate model
    • Narayanan B.A., Narayanan N.K., Pittman B., Reddy B.S. Regression of mouse prostatic intraepithelial neoplasia by nonsteroidal anti-inflammatory drugs in the transgenic adenocarcinoma mouse prostate model. Clin. Cancer Res. 2004, 10:7727-7737.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 7727-7737
    • Narayanan, B.A.1    Narayanan, N.K.2    Pittman, B.3    Reddy, B.S.4
  • 52
    • 0035966107 scopus 로고    scopus 로고
    • Cyclooxygenase-2 inducing Mcl-1-dependent survival mechanism in human lung adenocarcinoma CL1.0 cells. Involvement of phosphatidylinositol 3-kinase/Akt pathway
    • Lin M.T., Lee R.C., Yang P.C., Ho F.M., Kuo M.L. Cyclooxygenase-2 inducing Mcl-1-dependent survival mechanism in human lung adenocarcinoma CL1.0 cells. Involvement of phosphatidylinositol 3-kinase/Akt pathway. J. Biol. Chem. 2001, 276:48997-49002.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48997-49002
    • Lin, M.T.1    Lee, R.C.2    Yang, P.C.3    Ho, F.M.4    Kuo, M.L.5
  • 53
    • 0037064039 scopus 로고    scopus 로고
    • Regulation of MDR-1 (P-glycoprotein) by cyclooxygenase-2
    • Patel V.A., Dunn M.J., Sorokin A. Regulation of MDR-1 (P-glycoprotein) by cyclooxygenase-2. J. Biol. Chem. 2002, 277:38915-38920.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38915-38920
    • Patel, V.A.1    Dunn, M.J.2    Sorokin, A.3
  • 54
    • 33747164537 scopus 로고    scopus 로고
    • Antitumor properties of dimethyl-celecoxib, a derivative of celecoxib that does not inhibit cyclooxygenase-2: implications for glioma therapy
    • Schonthal A.H. Antitumor properties of dimethyl-celecoxib, a derivative of celecoxib that does not inhibit cyclooxygenase-2: implications for glioma therapy. Neurosurg. Focus 2006, 20:E21.
    • (2006) Neurosurg. Focus , vol.20
    • Schonthal, A.H.1
  • 55
    • 1242271208 scopus 로고    scopus 로고
    • 3-phosphoinositide-dependent protein kinase-1/Akt signaling represents a major cyclooxygenase-2-independent target for celecoxib in prostate cancer cells
    • Kulp S.K., Yang Y.T., Hung C.C., Chen K.F., Lai J.P., Tseng P.H., Fowble J.W., Ward P.J., Chen C.S. 3-phosphoinositide-dependent protein kinase-1/Akt signaling represents a major cyclooxygenase-2-independent target for celecoxib in prostate cancer cells. Cancer Res. 2004, 64:1444-1451.
    • (2004) Cancer Res. , vol.64 , pp. 1444-1451
    • Kulp, S.K.1    Yang, Y.T.2    Hung, C.C.3    Chen, K.F.4    Lai, J.P.5    Tseng, P.H.6    Fowble, J.W.7    Ward, P.J.8    Chen, C.S.9
  • 58
    • 33947592547 scopus 로고    scopus 로고
    • Down-regulation of PGE2 by physiologic levels of celecoxib is not sufficient to induce apoptosis or inhibit cell proliferation in human colon carcinoma cell lines
    • Lev-Ari S., Kazanov D., Liberman E., Ben-Yosef R., Arber N. Down-regulation of PGE2 by physiologic levels of celecoxib is not sufficient to induce apoptosis or inhibit cell proliferation in human colon carcinoma cell lines. Dig. Dis. Sci. 2007, 52:1128-1133.
    • (2007) Dig. Dis. Sci. , vol.52 , pp. 1128-1133
    • Lev-Ari, S.1    Kazanov, D.2    Liberman, E.3    Ben-Yosef, R.4    Arber, N.5
  • 59
    • 4444314778 scopus 로고    scopus 로고
    • The cyclooxygenase-2 inhibitor celecoxib blocks phosphorylation of Akt and induces apoptosis in human cholangiocarcinoma cells
    • Wu T., Leng J., Han C., Demetris A.J. The cyclooxygenase-2 inhibitor celecoxib blocks phosphorylation of Akt and induces apoptosis in human cholangiocarcinoma cells. Mol. Cancer Ther. 2004, 3:299-307.
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 299-307
    • Wu, T.1    Leng, J.2    Han, C.3    Demetris, A.J.4
  • 61
    • 0037081194 scopus 로고    scopus 로고
    • Cyclooxygenase 2- and prostaglandin E(2) receptor EP(2)-dependent angiogenesis in Apc(Delta716) mouse intestinal polyps
    • Seno H., Oshima M., Ishikawa T.O., Oshima H., Takaku K., Chiba T., Narumiya S., Taketo M.M. Cyclooxygenase 2- and prostaglandin E(2) receptor EP(2)-dependent angiogenesis in Apc(Delta716) mouse intestinal polyps. Cancer Res. 2002, 62:506-511.
    • (2002) Cancer Res. , vol.62 , pp. 506-511
    • Seno, H.1    Oshima, M.2    Ishikawa, T.O.3    Oshima, H.4    Takaku, K.5    Chiba, T.6    Narumiya, S.7    Taketo, M.M.8
  • 63
    • 10644257370 scopus 로고    scopus 로고
    • Death receptor regulation and celecoxib-induced apoptosis in human lung cancer cells
    • Liu X., Yue P., Zhou Z., Khuri F.R., Sun S.Y. Death receptor regulation and celecoxib-induced apoptosis in human lung cancer cells. J. Natl. Cancer Inst. 2004, 96:1769-1780.
    • (2004) J. Natl. Cancer Inst. , vol.96 , pp. 1769-1780
    • Liu, X.1    Yue, P.2    Zhou, Z.3    Khuri, F.R.4    Sun, S.Y.5
  • 64
    • 11944270441 scopus 로고    scopus 로고
    • Celecoxib derivatives induce apoptosis via the disruption of mitochondrial membrane potential and activation of caspase 9
    • Ding H., Han C., Zhu J., Chen C.S., D'Ambrosio S.M. Celecoxib derivatives induce apoptosis via the disruption of mitochondrial membrane potential and activation of caspase 9. Int. J. Cancer 2005, 113:803-810.
    • (2005) Int. J. Cancer , vol.113 , pp. 803-810
    • Ding, H.1    Han, C.2    Zhu, J.3    Chen, C.S.4    D'Ambrosio, S.M.5
  • 68
    • 33645813833 scopus 로고    scopus 로고
    • Celecoxib inhibits interleukin-12 alphabeta and beta2 folding and secretion by a novel COX2-independent mechanism involving chaperones of the endoplasmic reticulum
    • Alloza I., Baxter A., Chen Q., Matthiesen R., Vandenbroeck K. Celecoxib inhibits interleukin-12 alphabeta and beta2 folding and secretion by a novel COX2-independent mechanism involving chaperones of the endoplasmic reticulum. Mol. Pharmacol. 2006, 69:1579-1587.
    • (2006) Mol. Pharmacol. , vol.69 , pp. 1579-1587
    • Alloza, I.1    Baxter, A.2    Chen, Q.3    Matthiesen, R.4    Vandenbroeck, K.5
  • 70
    • 38849191201 scopus 로고    scopus 로고
    • Aggravated endoplasmic reticulum stress as a basis for enhanced glioblastoma cell killing by bortezomib in combination with celecoxib or its non-coxib analogue, 2,5-dimethyl-celecoxib
    • Kardosh A., Golden E.B., Pyrko P., Uddin J., Hofman F.M., Chen T.C., Louie S.G., Petasis N.A., Schonthal A.H. Aggravated endoplasmic reticulum stress as a basis for enhanced glioblastoma cell killing by bortezomib in combination with celecoxib or its non-coxib analogue, 2,5-dimethyl-celecoxib. Cancer Res. 2008, 68:843-851.
    • (2008) Cancer Res. , vol.68 , pp. 843-851
    • Kardosh, A.1    Golden, E.B.2    Pyrko, P.3    Uddin, J.4    Hofman, F.M.5    Chen, T.C.6    Louie, S.G.7    Petasis, N.A.8    Schonthal, A.H.9
  • 71
    • 33645156429 scopus 로고    scopus 로고
    • From acute ER stress to physiological roles of the unfolded protein respons
    • Wu J., Kaufman R.J. From acute ER stress to physiological roles of the unfolded protein respons. Cell Death Differ. 2006, 13:374-384.
    • (2006) Cell Death Differ. , vol.13 , pp. 374-384
    • Wu, J.1    Kaufman, R.J.2
  • 72
    • 68149136657 scopus 로고    scopus 로고
    • Cellular responses to endoplasmic reticulum stress and apoptosis
    • Rasheva V.I., Domingos P.M. Cellular responses to endoplasmic reticulum stress and apoptosis. Apoptosis 2009, 14:996-1007.
    • (2009) Apoptosis , vol.14 , pp. 996-1007
    • Rasheva, V.I.1    Domingos, P.M.2
  • 76
    • 34250365663 scopus 로고    scopus 로고
    • P-glycoprotein mediates celecoxib-induced apoptosis in multiple drug-resistant cell lines
    • Fantappie O., Solazzo M., Lasagna N., Platini F., Tessitore L., Mazzanti R. P-glycoprotein mediates celecoxib-induced apoptosis in multiple drug-resistant cell lines. Cancer Res. 2007, 67:4915-4923.
    • (2007) Cancer Res. , vol.67 , pp. 4915-4923
    • Fantappie, O.1    Solazzo, M.2    Lasagna, N.3    Platini, F.4    Tessitore, L.5    Mazzanti, R.6
  • 77
    • 33847328289 scopus 로고    scopus 로고
    • The Bcl-2 apoptotic switch in cancer development and therapy
    • Adams J.M., Cory S. The Bcl-2 apoptotic switch in cancer development and therapy. Oncogene 2007, 26:1324-1337.
    • (2007) Oncogene , vol.26 , pp. 1324-1337
    • Adams, J.M.1    Cory, S.2
  • 78
  • 79
    • 33745957572 scopus 로고    scopus 로고
    • Proapoptotic multidomain Bcl-2/Bax-family proteins: mechanisms, physiological roles, and therapeutic opportunities
    • Reed J.C. Proapoptotic multidomain Bcl-2/Bax-family proteins: mechanisms, physiological roles, and therapeutic opportunities. Cell Death Differ. 2006, 13:1378-1386.
    • (2006) Cell Death Differ. , vol.13 , pp. 1378-1386
    • Reed, J.C.1
  • 82
    • 15244342640 scopus 로고    scopus 로고
    • A novel celecoxib derivative, OSU03012, induces cytotoxicity in primary CLL cells and transformed B-cell lymphoma cell line via a caspase- and Bcl-2-independent mechanism
    • Johnson A.J., Smith L.L., Zhu J., Heerema N.A., Jefferson S., Mone A., Grever M., Chen C.S., Byrd J.C. A novel celecoxib derivative, OSU03012, induces cytotoxicity in primary CLL cells and transformed B-cell lymphoma cell line via a caspase- and Bcl-2-independent mechanism. Blood 2005, 105:2504-2509.
    • (2005) Blood , vol.105 , pp. 2504-2509
    • Johnson, A.J.1    Smith, L.L.2    Zhu, J.3    Heerema, N.A.4    Jefferson, S.5    Mone, A.6    Grever, M.7    Chen, C.S.8    Byrd, J.C.9
  • 84
    • 33745935358 scopus 로고    scopus 로고
    • Unraveling MCL-1 degradation
    • Opferman J.T. Unraveling MCL-1 degradation. Cell Death Differ. 2006, 13:1260-1262.
    • (2006) Cell Death Differ. , vol.13 , pp. 1260-1262
    • Opferman, J.T.1
  • 86
    • 22244464818 scopus 로고    scopus 로고
    • Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins
    • Willis S.N., Chen L., Dewson G., Wei A., Naik E., Fletcher J.I., Adams J.M., Huang D.C. Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Genes Dev. 2005, 19:1294-1305.
    • (2005) Genes Dev. , vol.19 , pp. 1294-1305
    • Willis, S.N.1    Chen, L.2    Dewson, G.3    Wei, A.4    Naik, E.5    Fletcher, J.I.6    Adams, J.M.7    Huang, D.C.8
  • 87
    • 21244472965 scopus 로고    scopus 로고
    • Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis
    • Zhong Q., Gao W., Du F., Wang X. Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis. Cell 2005, 121:1085-1095.
    • (2005) Cell , vol.121 , pp. 1085-1095
    • Zhong, Q.1    Gao, W.2    Du, F.3    Wang, X.4
  • 88
    • 0036234124 scopus 로고    scopus 로고
    • MCL1 provides a window on the role of the BCL2 family in cell proliferation, differentiation and tumorigenesis
    • Craig R.W. MCL1 provides a window on the role of the BCL2 family in cell proliferation, differentiation and tumorigenesis. Leukemia 2002, 16:444-454.
    • (2002) Leukemia , vol.16 , pp. 444-454
    • Craig, R.W.1
  • 89
    • 0035825596 scopus 로고    scopus 로고
    • The involvement of PI 3-K/Akt-dependent up-regulation of Mcl-1 in the prevention of apoptosis of Hep3B cells by interleukin-6
    • Kuo M.L., Chuang S.E., Lin M.T., Yang S.Y. The involvement of PI 3-K/Akt-dependent up-regulation of Mcl-1 in the prevention of apoptosis of Hep3B cells by interleukin-6. Oncogene 2001, 20:677-685.
    • (2001) Oncogene , vol.20 , pp. 677-685
    • Kuo, M.L.1    Chuang, S.E.2    Lin, M.T.3    Yang, S.Y.4
  • 90
    • 33644855216 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1
    • Maurer U., Charvet C., Wagman A.S., Dejardin E., Green D.R. Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1. Mol. Cell 2006, 21:749-760.
    • (2006) Mol. Cell , vol.21 , pp. 749-760
    • Maurer, U.1    Charvet, C.2    Wagman, A.S.3    Dejardin, E.4    Green, D.R.5
  • 91
    • 67650510705 scopus 로고    scopus 로고
    • Context-dependent Bcl-2/Bak interactions regulate lymphoid cell apoptosis
    • Dai H., Meng X.W., Lee S.H., Schneider P.A., Kaufmann S.H. Context-dependent Bcl-2/Bak interactions regulate lymphoid cell apoptosis. J. Biol. Chem. 2009, 284:18311-18322.
    • (2009) J. Biol. Chem. , vol.284 , pp. 18311-18322
    • Dai, H.1    Meng, X.W.2    Lee, S.H.3    Schneider, P.A.4    Kaufmann, S.H.5
  • 92
    • 33744507693 scopus 로고    scopus 로고
    • Interrelated roles for Mcl-1 and BIM in regulation of TRAIL-mediated mitochondrial apoptosis
    • Han J., Goldstein L.A., Gastman B.R., Rabinowich H. Interrelated roles for Mcl-1 and BIM in regulation of TRAIL-mediated mitochondrial apoptosis. J. Biol. Chem. 2006, 281:10153-10163.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10153-10163
    • Han, J.1    Goldstein, L.A.2    Gastman, B.R.3    Rabinowich, H.4
  • 93
    • 0032211158 scopus 로고    scopus 로고
    • Mcl-1 in transgenic mice promotes survival in a spectrum of hematopoietic cell types and immortalization in the myeloid lineage
    • Zhou P., Qian L., Bieszczad C.K., Noelle R., Binder M., Levy N.B., Craig R.W. Mcl-1 in transgenic mice promotes survival in a spectrum of hematopoietic cell types and immortalization in the myeloid lineage. Blood 1998, 92:3226-3239.
    • (1998) Blood , vol.92 , pp. 3226-3239
    • Zhou, P.1    Qian, L.2    Bieszczad, C.K.3    Noelle, R.4    Binder, M.5    Levy, N.B.6    Craig, R.W.7
  • 94
  • 95
    • 0035958578 scopus 로고    scopus 로고
    • Cleavage of Bcl-2 in oxidant- and cisplatin-induced apoptosis of human melanoma cells
    • Del Bello B., Valentini M.A., Zunino F., Comporti M., Maellaro E. Cleavage of Bcl-2 in oxidant- and cisplatin-induced apoptosis of human melanoma cells. Oncogene 2001, 20:4591-4595.
    • (2001) Oncogene , vol.20 , pp. 4591-4595
    • Del Bello, B.1    Valentini, M.A.2    Zunino, F.3    Comporti, M.4    Maellaro, E.5
  • 96
    • 0033499801 scopus 로고    scopus 로고
    • BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M
    • Yamamoto K., Ichijo H., Korsmeyer S.J. BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M. Mol. Cell Biol. 1999, 19:8469-8478.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 8469-8478
    • Yamamoto, K.1    Ichijo, H.2    Korsmeyer, S.J.3
  • 97
    • 44949237240 scopus 로고    scopus 로고
    • JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy
    • Wei Y., Pattingre S., Sinha S., Bassik M., Levine B. JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy. Mol. Cell 2008, 30:678-688.
    • (2008) Mol. Cell , vol.30 , pp. 678-688
    • Wei, Y.1    Pattingre, S.2    Sinha, S.3    Bassik, M.4    Levine, B.5
  • 99
    • 1342306819 scopus 로고    scopus 로고
    • Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3
    • Lin B., Kolluri S.K., Lin F., Liu W., Han Y.H., Cao X., Dawson M.I., Reed J.C., Zhang X.K. Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3. Cell 2004, 116:527-540.
    • (2004) Cell , vol.116 , pp. 527-540
    • Lin, B.1    Kolluri, S.K.2    Lin, F.3    Liu, W.4    Han, Y.H.5    Cao, X.6    Dawson, M.I.7    Reed, J.C.8    Zhang, X.K.9
  • 100
    • 43549097825 scopus 로고    scopus 로고
    • Nur77 family proteins translocate to mitochondria where they associate with Bcl-2 and expose its proapoptotic BH3 domain
    • Thompson J., Winoto A. Nur77 family proteins translocate to mitochondria where they associate with Bcl-2 and expose its proapoptotic BH3 domain. J. Exp. Med. 2008, 205:1029-1036.
    • (2008) J. Exp. Med. , vol.205 , pp. 1029-1036
    • Thompson, J.1    Winoto, A.2
  • 101
    • 19344375948 scopus 로고    scopus 로고
    • Anti-proliferative and apoptotic effects of celecoxib on human chronic myeloid leukemia in vitro
    • Subhashini J., Mahipal S.V., Reddanna P. Anti-proliferative and apoptotic effects of celecoxib on human chronic myeloid leukemia in vitro. Cancer Lett. 2005, 224:31-43.
    • (2005) Cancer Lett. , vol.224 , pp. 31-43
    • Subhashini, J.1    Mahipal, S.V.2    Reddanna, P.3
  • 102
    • 34547763340 scopus 로고    scopus 로고
    • Celecoxib increased expression of 14-3-3sigma and induced apoptosis of glioma cells
    • Chen J.C., Chen Y., Su Y.H., Tseng S.H. Celecoxib increased expression of 14-3-3sigma and induced apoptosis of glioma cells. Anticancer Res. 2007, 27:2547-2554.
    • (2007) Anticancer Res. , vol.27 , pp. 2547-2554
    • Chen, J.C.1    Chen, Y.2    Su, Y.H.3    Tseng, S.H.4
  • 104
    • 0348014686 scopus 로고    scopus 로고
    • DNA damage response and MCL-1 destruction initiate apoptosis in adenovirus-infected cells
    • Cuconati A., Mukherjee C., Perez D., White E. DNA damage response and MCL-1 destruction initiate apoptosis in adenovirus-infected cells. Genes Dev. 2003, 17:2922-2932.
    • (2003) Genes Dev. , vol.17 , pp. 2922-2932
    • Cuconati, A.1    Mukherjee, C.2    Perez, D.3    White, E.4
  • 105
    • 44349182097 scopus 로고    scopus 로고
    • Differential regulation of Bax and Bak by anti-apoptotic Bcl-2 family proteins Bcl-B and Mcl-1
    • Zhai D., Jin C., Huang Z., Satterthwait A.C., Reed J.C. Differential regulation of Bax and Bak by anti-apoptotic Bcl-2 family proteins Bcl-B and Mcl-1. J. Biol. Chem. 2008, 283:9580-9586.
    • (2008) J. Biol. Chem. , vol.283 , pp. 9580-9586
    • Zhai, D.1    Jin, C.2    Huang, Z.3    Satterthwait, A.C.4    Reed, J.C.5
  • 109
    • 77953530983 scopus 로고    scopus 로고
    • Celecoxib-induced apoptosis is enhanced by ABT-737 and by inhibition of autophagy in human colorectal cancer cells
    • Huang S., Sinicrope F.A. Celecoxib-induced apoptosis is enhanced by ABT-737 and by inhibition of autophagy in human colorectal cancer cells. Autophagy 2010, 6:255-269.
    • (2010) Autophagy , vol.6 , pp. 255-269
    • Huang, S.1    Sinicrope, F.A.2
  • 110
    • 34548662444 scopus 로고    scopus 로고
    • Reduced survivin expression and tumor cell survival during chronic hypoxia and further cytotoxic enhancement by the cyclooxygenase-2 inhibitor celecoxib
    • Kardosh A., Soriano N., Pyrko P., Liu Y.T., Jabbour M., Hofman F.M., Schonthal A.H. Reduced survivin expression and tumor cell survival during chronic hypoxia and further cytotoxic enhancement by the cyclooxygenase-2 inhibitor celecoxib. J. Biomed. Sci. 2007, 14:647-662.
    • (2007) J. Biomed. Sci. , vol.14 , pp. 647-662
    • Kardosh, A.1    Soriano, N.2    Pyrko, P.3    Liu, Y.T.4    Jabbour, M.5    Hofman, F.M.6    Schonthal, A.H.7
  • 111
    • 34250774915 scopus 로고    scopus 로고
    • Activation of p38 mitogen-activated protein kinase by celecoxib oppositely regulates survivin and gamma-H2AX in human colorectal cancer cells
    • Hsiao P.W., Chang C.C., Liu H.F., Tsai C.M., Chiu T.H., Chao J.I. Activation of p38 mitogen-activated protein kinase by celecoxib oppositely regulates survivin and gamma-H2AX in human colorectal cancer cells. Toxicol. Appl. Pharmacol. 2007, 222:97-104.
    • (2007) Toxicol. Appl. Pharmacol. , vol.222 , pp. 97-104
    • Hsiao, P.W.1    Chang, C.C.2    Liu, H.F.3    Tsai, C.M.4    Chiu, T.H.5    Chao, J.I.6
  • 115
    • 54249129774 scopus 로고    scopus 로고
    • New wirings in the survivin networks
    • Altieri D.C. New wirings in the survivin networks. Oncogene 2008, 27:6276-6284.
    • (2008) Oncogene , vol.27 , pp. 6276-6284
    • Altieri, D.C.1
  • 116
    • 74749083984 scopus 로고    scopus 로고
    • Prostaglandin E2 upregulates survivin expression via the EP1 receptor in hepatocellular carcinoma cells
    • Bai X.M., Jiang H., Ding J.X., Peng T., Ma J., Wang Y.H., Zhang L., Zhang H., Leng J. Prostaglandin E2 upregulates survivin expression via the EP1 receptor in hepatocellular carcinoma cells. Life Sci. 2010, 86:214-223.
    • (2010) Life Sci. , vol.86 , pp. 214-223
    • Bai, X.M.1    Jiang, H.2    Ding, J.X.3    Peng, T.4    Ma, J.5    Wang, Y.H.6    Zhang, L.7    Zhang, H.8    Leng, J.9
  • 117
    • 40849126882 scopus 로고    scopus 로고
    • The effects of cyclooxygenase-2 expression in prostate cancer cells: modulation of response to cytotoxic agents
    • Mehar A., Macanas-Pirard P., Mizokami A., Takahashi Y., Kass G.E., Coley H.M. The effects of cyclooxygenase-2 expression in prostate cancer cells: modulation of response to cytotoxic agents. J. Pharmacol. Exp. Ther. 2008, 324:1181-1187.
    • (2008) J. Pharmacol. Exp. Ther. , vol.324 , pp. 1181-1187
    • Mehar, A.1    Macanas-Pirard, P.2    Mizokami, A.3    Takahashi, Y.4    Kass, G.E.5    Coley, H.M.6
  • 118
    • 67649976957 scopus 로고    scopus 로고
    • Synergistic inhibition effect of tumor growth by using celecoxib in combination with oxaliplatin
    • Zhao S., Cai J., Bian H., Gui L., Zhao F. Synergistic inhibition effect of tumor growth by using celecoxib in combination with oxaliplatin. Cancer Invest. 2009, 27:636-640.
    • (2009) Cancer Invest. , vol.27 , pp. 636-640
    • Zhao, S.1    Cai, J.2    Bian, H.3    Gui, L.4    Zhao, F.5
  • 119
    • 48149106737 scopus 로고    scopus 로고
    • TRAIL-mediated apoptosis in malignant glioma cells is augmented by celecoxib through proteasomal degradation of survivin
    • Gaiser T., Becker M.R., Habel A., Reuss D.E., Ehemann V., Rami A., Siegelin M.D. TRAIL-mediated apoptosis in malignant glioma cells is augmented by celecoxib through proteasomal degradation of survivin. Neurosci. Lett. 2008, 442:109-113.
    • (2008) Neurosci. Lett. , vol.442 , pp. 109-113
    • Gaiser, T.1    Becker, M.R.2    Habel, A.3    Reuss, D.E.4    Ehemann, V.5    Rami, A.6    Siegelin, M.D.7
  • 120
    • 23444442691 scopus 로고    scopus 로고
    • Targeting the beta-catenin/APC pathway: a novel mechanism to explain the cyclooxygenase-2-independent anticarcinogenic effects of celecoxib in human colon carcinoma cells
    • Maier T.J., Janssen A., Schmidt R., Geisslinger G., Grosch S. Targeting the beta-catenin/APC pathway: a novel mechanism to explain the cyclooxygenase-2-independent anticarcinogenic effects of celecoxib in human colon carcinoma cells. FASEB J. 2005, 19:1353-1355.
    • (2005) FASEB J. , vol.19 , pp. 1353-1355
    • Maier, T.J.1    Janssen, A.2    Schmidt, R.3    Geisslinger, G.4    Grosch, S.5
  • 125
    • 33847740988 scopus 로고    scopus 로고
    • Wnt/beta-catenin signaling in cancer stemness and malignant behavior
    • Fodde R., Brabletz T. Wnt/beta-catenin signaling in cancer stemness and malignant behavior. Curr. Opin. Cell Biol. 2007, 19:150-158.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 150-158
    • Fodde, R.1    Brabletz, T.2
  • 127
    • 0038604334 scopus 로고    scopus 로고
    • Activation of c-Jun-N-terminal-kinase is crucial for the induction of a cell cycle arrest in human colon carcinoma cells caused by flurbiprofen enantiomers
    • Grosch S., Tegeder I., Schilling K., Maier T.J., Niederberger E., Geisslinger G. Activation of c-Jun-N-terminal-kinase is crucial for the induction of a cell cycle arrest in human colon carcinoma cells caused by flurbiprofen enantiomers. FASEB J. 2003, 17:1316-1318.
    • (2003) FASEB J. , vol.17 , pp. 1316-1318
    • Grosch, S.1    Tegeder, I.2    Schilling, K.3    Maier, T.J.4    Niederberger, E.5    Geisslinger, G.6
  • 129
    • 0035934070 scopus 로고    scopus 로고
    • Risk of cardiovascular events associated with selective COX-2 inhibitors
    • Mukherjee D., Nissen S.E., Topol E.J. Risk of cardiovascular events associated with selective COX-2 inhibitors. Jama 2001, 286:954-959.
    • (2001) Jama , vol.286 , pp. 954-959
    • Mukherjee, D.1    Nissen, S.E.2    Topol, E.J.3
  • 130
    • 6044274282 scopus 로고    scopus 로고
    • Coxibs and cardiovascular disease
    • Fitzgerald G.A. Coxibs and cardiovascular disease. N. Engl. J. Med. 2004, 351:1709-1711.
    • (2004) N. Engl. J. Med. , vol.351 , pp. 1709-1711
    • Fitzgerald, G.A.1
  • 132
    • 33846947152 scopus 로고    scopus 로고
    • COX-2 inhibition: a possible role in the management of prostate cancer?
    • Sooriakumaran P., Langley S.E., Laing R.W., Coley H.M. COX-2 inhibition: a possible role in the management of prostate cancer?. J. Chemother. 2007, 19:21-32.
    • (2007) J. Chemother. , vol.19 , pp. 21-32
    • Sooriakumaran, P.1    Langley, S.E.2    Laing, R.W.3    Coley, H.M.4
  • 133
    • 39049101494 scopus 로고    scopus 로고
    • Celecoxib analogs that lack COX-2 inhibitory function: preclinical development of novel anticancer drugs
    • Schonthal A.H., Chen T.C., Hofman F.M., Louie S.G., Petasis N.A. Celecoxib analogs that lack COX-2 inhibitory function: preclinical development of novel anticancer drugs. Expert Opin. Investig. Drugs 2008, 17:197-208.
    • (2008) Expert Opin. Investig. Drugs , vol.17 , pp. 197-208
    • Schonthal, A.H.1    Chen, T.C.2    Hofman, F.M.3    Louie, S.G.4    Petasis, N.A.5
  • 134
    • 33749339372 scopus 로고    scopus 로고
    • Cardiovascular risk and inhibition of cyclooxygenase: a systematic review of the observational studies of selective and nonselective inhibitors of cyclooxygenase 2
    • McGettigan P., Henry D. Cardiovascular risk and inhibition of cyclooxygenase: a systematic review of the observational studies of selective and nonselective inhibitors of cyclooxygenase 2. Jama 2006, 296:1633-1644.
    • (2006) Jama , vol.296 , pp. 1633-1644
    • McGettigan, P.1    Henry, D.2
  • 135
    • 0037021658 scopus 로고    scopus 로고
    • Using cyclooxygenase-2 inhibitors as molecular platforms to develop a new class of apoptosis-inducing agents
    • Zhu J., Song X., Lin H.P., Young D.C., Yan S., Marquez V.E., Chen C.S. Using cyclooxygenase-2 inhibitors as molecular platforms to develop a new class of apoptosis-inducing agents. J. Natl. Cancer Inst. 2002, 94:1745-1757.
    • (2002) J. Natl. Cancer Inst. , vol.94 , pp. 1745-1757
    • Zhu, J.1    Song, X.2    Lin, H.P.3    Young, D.C.4    Yan, S.5    Marquez, V.E.6    Chen, C.S.7
  • 136
    • 28844442877 scopus 로고    scopus 로고
    • Multitarget inhibition of drug-resistant multiple myeloma cell lines by dimethyl-celecoxib (DMC), a non-COX-2 inhibitory analog of celecoxib
    • (Epub 2005 Aug 25)
    • Kardosh A., Soriano N., Liu Y.T., Uddin J., Petasis N.A., Hofman F.M., Chen T.C., Schonthal A.H. Multitarget inhibition of drug-resistant multiple myeloma cell lines by dimethyl-celecoxib (DMC), a non-COX-2 inhibitory analog of celecoxib. Blood 2005, 106:4330-4338. (Epub 2005 Aug 25).
    • (2005) Blood , vol.106 , pp. 4330-4338
    • Kardosh, A.1    Soriano, N.2    Liu, Y.T.3    Uddin, J.4    Petasis, N.A.5    Hofman, F.M.6    Chen, T.C.7    Schonthal, A.H.8
  • 137
    • 1842425625 scopus 로고    scopus 로고
    • Prognostic impact of cyclooxygenase-2 in breast cancer
    • Denkert C., Winzer K.J., Hauptmann S. Prognostic impact of cyclooxygenase-2 in breast cancer. Clin. Breast Cancer 2004, 4:428-433.
    • (2004) Clin. Breast Cancer , vol.4 , pp. 428-433
    • Denkert, C.1    Winzer, K.J.2    Hauptmann, S.3
  • 138
    • 24944591396 scopus 로고    scopus 로고
    • Potential use of COX-2-aromatase inhibitor combinations in breast cancer
    • Bundred N.J., Barnes N.L. Potential use of COX-2-aromatase inhibitor combinations in breast cancer. Br. J. Cancer 2005, 93:S10-S15.
    • (2005) Br. J. Cancer , vol.93
    • Bundred, N.J.1    Barnes, N.L.2
  • 139
    • 38149029210 scopus 로고    scopus 로고
    • Prognostic significance of cyclooxygenase-2 expression and nuclear p53 accumulation in patients with colorectal cancer
    • Lim S.C., Lee T.B., Choi C.H., Ryu S.Y., Min Y.D., Kim K.J. Prognostic significance of cyclooxygenase-2 expression and nuclear p53 accumulation in patients with colorectal cancer. J. Surg. Oncol. 2008, 97:51-56.
    • (2008) J. Surg. Oncol. , vol.97 , pp. 51-56
    • Lim, S.C.1    Lee, T.B.2    Choi, C.H.3    Ryu, S.Y.4    Min, Y.D.5    Kim, K.J.6
  • 140
    • 0036682406 scopus 로고    scopus 로고
    • Overexpression of cyclooxygenase-2 is associated with a poor prognosis in patients with squamous cell carcinoma of the uterine cervix treated with radiation and concurrent chemotherapy
    • Kim Y.B., Kim G.E., Cho N.H., Pyo H.R., Shim S.J., Chang S.K., Park H.C., Suh C.O., Park T.K., Kim B.S. Overexpression of cyclooxygenase-2 is associated with a poor prognosis in patients with squamous cell carcinoma of the uterine cervix treated with radiation and concurrent chemotherapy. Cancer 2002, 95:531-539.
    • (2002) Cancer , vol.95 , pp. 531-539
    • Kim, Y.B.1    Kim, G.E.2    Cho, N.H.3    Pyo, H.R.4    Shim, S.J.5    Chang, S.K.6    Park, H.C.7    Suh, C.O.8    Park, T.K.9    Kim, B.S.10
  • 141
    • 20044372741 scopus 로고    scopus 로고
    • Prediction of poor survival by cyclooxygenase-2 in patients with T4 nasopharyngeal cancer treated by radiation therapy: clinical and in vitro studies
    • Chen W.C., McBride W.H., Chen S.M., Lee K.F., Hwang T.Z., Jung S.M., Shau H., Liao S.K., Hong J.H., Chen M.F. Prediction of poor survival by cyclooxygenase-2 in patients with T4 nasopharyngeal cancer treated by radiation therapy: clinical and in vitro studies. Head Neck 2005, 27:503-512.
    • (2005) Head Neck , vol.27 , pp. 503-512
    • Chen, W.C.1    McBride, W.H.2    Chen, S.M.3    Lee, K.F.4    Hwang, T.Z.5    Jung, S.M.6    Shau, H.7    Liao, S.K.8    Hong, J.H.9    Chen, M.F.10
  • 142
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: opposing activities that mediate cell death
    • Youle R.J., Strasser A. The BCL-2 protein family: opposing activities that mediate cell death. Nat. Rev. Mol. Cell Biol. 2008, 9:47-59.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 143
    • 13944277343 scopus 로고    scopus 로고
    • BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly
    • Kuwana T., Bouchier-Hayes L., Chipuk J.E., Bonzon C., Sullivan B.A., Green D.R., Newmeyer D.D. BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. Mol. Cell 2005, 17:525-535.
    • (2005) Mol. Cell , vol.17 , pp. 525-535
    • Kuwana, T.1    Bouchier-Hayes, L.2    Chipuk, J.E.3    Bonzon, C.4    Sullivan, B.A.5    Green, D.R.6    Newmeyer, D.D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.