메뉴 건너뛰기




Volumn 11, Issue 4, 2011, Pages 499-502

Caspase 9b: A new target for therapy in non-small-cell lung cancer

Author keywords

alternative splicing; caspase 9; erlotinib; hnRNPL; non small cell lung cancer; oncogenesis

Indexed keywords

CASPASE 9; DAUNORUBICIN; EPIDERMAL GROWTH FACTOR RECEPTOR; ERLOTINIB; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN L; MESSENGER RNA;

EID: 79955083536     PISSN: 14737140     EISSN: 17448328     Source Type: Journal    
DOI: 10.1586/era.11.23     Document Type: Review
Times cited : (9)

References (31)
  • 1
    • 55249094584 scopus 로고    scopus 로고
    • Updates in non-small cell lung cancer
    • Walker S. Updates in non-small cell lung cancer. Clin. J. Oncol. Nurs. 12(4), 587-596 (2008).
    • (2008) Clin. J. Oncol. Nurs. , vol.12 , Issue.4 , pp. 587-596
    • Walker, S.1
  • 2
    • 18244371651 scopus 로고    scopus 로고
    • Acquired resistance of lung adenocarcinomas to gefitinib or erlotinib is associated with a second mutation in the EGFR kinase domain
    • Pao W, Miller VA, Politi KA et al. Acquired resistance of lung adenocarcinomas to gefitinib or erlotinib is associated with a second mutation in the EGFR kinase domain. PLoS Med. 2(3), e73 (2005).
    • (2005) PLoS Med. , vol.2 , Issue.3
    • Pao, W.1    Miller, V.A.2    Politi, K.A.3
  • 5
    • 7444220147 scopus 로고    scopus 로고
    • Aberrant and alternative splicing in cancer
    • DOI 10.1158/0008-5472.CAN-04-1910
    • Venables JP. Aberrant and alternative splicing in cancer. Cancer Res. 64(21), 7647-7654 (2004). (Pubitemid 39446889)
    • (2004) Cancer Research , vol.64 , Issue.21 , pp. 7647-7654
    • Venables, J.P.1
  • 7
    • 33645220093 scopus 로고    scopus 로고
    • Regulation of CD44 alternative splicing by SRm160 and its potential role in tumor cell invasion
    • Cheng C, Sharp PA. Regulation of CD44 alternative splicing by SRm160 and its potential role in tumor cell invasion. Mol. Cell Biol. 26(1), 362-370 (2006).
    • (2006) Mol. Cell Biol. , vol.26 , Issue.1 , pp. 362-370
    • Cheng, C.1    Sharp, P.A.2
  • 8
    • 61649087689 scopus 로고    scopus 로고
    • ESRP1 and ESRP2 are epithelial cell-type-specific regulators of FGFR2 splicing
    • Warzecha CC, Sato TK, Nabet B, Hogenesch JB, Carstens RP. ESRP1 and ESRP2 are epithelial cell-type-specific regulators of FGFR2 splicing. Mol. Cell 33(5), 591-601 (2009).
    • (2009) Mol. Cell , vol.33 , Issue.5 , pp. 591-601
    • Warzecha, C.C.1    Sato, T.K.2    Nabet, B.3    Hogenesch, J.B.4    Carstens, R.P.5
  • 9
    • 77957726684 scopus 로고    scopus 로고
    • Sam68 regulates EMT through alternative splicing-activated nonsense-mediated mRNA decay of the SF2/ASF proto-oncogene
    • Valacca C, Bonomi S, Buratti E et al. Sam68 regulates EMT through alternative splicing-activated nonsense-mediated mRNA decay of the SF2/ASF proto-oncogene. J. Cell Biol. 191(1), 87-99 (2010).
    • (2010) J. Cell Biol. , vol.191 , Issue.1 , pp. 87-99
    • Valacca, C.1    Bonomi, S.2    Buratti, E.3
  • 13
    • 78549234102 scopus 로고    scopus 로고
    • Alternative splicing of caspase 9 is modulated by the phosphoinositide 3-kinase/Akt pathway via phosphorylation of SRp30a
    • Shultz JC, Goehe RW, Wijesinghe DS et al. Alternative splicing of caspase 9 is modulated by the phosphoinositide 3-kinase/Akt pathway via phosphorylation of SRp30a. Cancer Res. 70(22), 9185-9196 (2010).
    • (2010) Cancer Res. , vol.70 , Issue.22 , pp. 9185-9196
    • Shultz, J.C.1    Goehe, R.W.2    Wijesinghe, D.S.3
  • 14
    • 78049448047 scopus 로고    scopus 로고
    • Hnrnp L regulates the tumorigenic capacity of lung cancer xenografts in mice via caspase-9 pre-mRNA processing
    • Goehe RW, Shultz JC, Murudkar C et al. hnRNP L regulates the tumorigenic capacity of lung cancer xenografts in mice via caspase-9 pre-mRNA processing. J. Clin. Investig. 120(11), 3923-3939 (2010).
    • (2010) J. Clin. Investig. , vol.120 , Issue.11 , pp. 3923-3939
    • Goehe, R.W.1    Shultz, J.C.2    Murudkar, C.3
  • 15
    • 11344265724 scopus 로고    scopus 로고
    • A tetracycline-regulated adenovirus encoding dominant-negative caspase-9 is regulated in rat brain and protects against neurotoxin-induced cell death in vitro, but not in vivo
    • DOI 10.1016/j.expneurol.2004.08.024, PII S0014488604003085, Neuroplasticity of the Central Nervous System
    • Ebert AD, Chen F, He X, Cryns VL, Bohn MC. A tetracycline-regulated adenovirus encoding dominant-negative caspase-9 is regulated in rat brain and protects against neurotoxin-induced cell death in vitro, but not in vivo. Exp. Neurol. 191(Suppl. 1), S80-S94 (2005). (Pubitemid 40075413)
    • (2005) Experimental Neurology , vol.191 , Issue.SUPPL. 1
    • Ebert, A.D.1    Chen, F.2    He, X.3    Cryns, V.L.4    Bohn, M.C.5
  • 16
    • 17444383660 scopus 로고    scopus 로고
    • Apoptosome dysfunction in human cancer
    • DOI 10.1023/B:APPT.0000045786.98031.1d
    • Hajra KM, Liu JR. Apoptosome dysfunction in human cancer. Apoptosis 9(6), 691-704 (2004). (Pubitemid 40941198)
    • (2004) Apoptosis , vol.9 , Issue.6 , pp. 691-704
    • Hajra, K.M.1    Liu, J.R.2
  • 17
    • 0036827535 scopus 로고    scopus 로고
    • Reovirus-induced apoptosis requires mitochondrial release of Smac/DIABLO and involves reduction of cellular inhibitor of apoptosis protein levels
    • DOI 10.1128/JVI.76.22.11414-11424.2002
    • Kominsky DJ, Bickel RJ, Tyler KL. Reovirus-induced apoptosis requires mitochondrial release of Smac/DIABLO and involves reduction of cellular inhibitor of apoptosis protein levels. J. Virol. 76(22), 11414-11424 (2002). (Pubitemid 35231297)
    • (2002) Journal of Virology , vol.76 , Issue.22 , pp. 11414-11424
    • Kominsky, D.J.1    Bickel, R.J.2    Tyler, K.L.3
  • 18
    • 4444371304 scopus 로고    scopus 로고
    • 6-Hydroxydopamine induces dopaminergic cell degeneration via a caspase-9-mediated apoptotic pathway that is attenuated by caspase-9dn expression
    • DOI 10.1002/jnr.20198
    • Liang Q, Liou AK, Ding Y et al. 6-Hydroxydopamine induces dopaminergic cell degeneration via a caspase-9-mediated apoptotic pathway that is attenuated by caspase-9dn expression. J. Neurosci. Res. 77(5), 747-761 (2004). (Pubitemid 39194617)
    • (2004) Journal of Neuroscience Research , vol.77 , Issue.5 , pp. 747-761
    • Liang, Q.1    Liou, A.K.F.2    Ding, Y.3    Cao, G.4    Xiao, X.5    Ferez, R.G.6    Chen, J.7
  • 19
    • 3242806104 scopus 로고    scopus 로고
    • Caspases and cancer: Mechanisms of inactivation and new treatment modalities
    • Philchenkov A, Zavelevich M, Kroczak TJ, Los M. Caspases and cancer: mechanisms of inactivation and new treatment modalities. Exp. Oncol. 26(2), 82-97 (2004).
    • (2004) Exp. Oncol. , vol.26 , Issue.2 , pp. 82-97
    • Philchenkov, A.1    Zavelevich, M.2    Kroczak, T.J.3    Los, M.4
  • 20
    • 0033593201 scopus 로고    scopus 로고
    • A caspase-9 variant missing the catalytic site is an endogenous inhibitor of apoptosis
    • Seol DW, Billiar TR. A caspase-9 variant missing the catalytic site is an endogenous inhibitor of apoptosis. J. Biol. Chem. 274(4), 2072-2076 (1999).
    • (1999) J. Biol. Chem. , vol.274 , Issue.4 , pp. 2072-2076
    • Seol, D.W.1    Billiar, T.R.2
  • 21
    • 0033515883 scopus 로고    scopus 로고
    • Apaf-1 and caspase-9 in p53-dependent apoptosis and tumor inhibition
    • DOI 10.1126/science.284.5411.156
    • Soengas MS, Alarcon RM, Yoshida H et al. APAF-1 and caspase-9 in p53-dependent apoptosis and tumor inhibition. Science (New York, NY) 284(5411), 156-159 (1999). (Pubitemid 29282071)
    • (1999) Science , vol.284 , Issue.5411 , pp. 156-159
    • Soengas, M.S.1    Alarcon, R.M.2    Yoshida, H.3    Giaccia, A.J.4    Hakem, R.5    Mak, T.W.6    Lowe, S.W.7
  • 23
    • 0037134511 scopus 로고    scopus 로고
    • Antiapoptotic activity of the free caspase recruitment domain of procaspase-9. A novel endogenous rescue pathway in cell death
    • DOI 10.1074/jbc.M108530200
    • Stephanou A, Scarabelli TM, Knight RA, Latchman DS. Antiapoptotic activity of the free caspase recruitment domain of procaspase-9: a novel endogenous rescue pathway in cell death. J. Biol. Chem. 277(16), 13693-13699 (2002). (Pubitemid 34967970)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.16 , pp. 13693-13699
    • Stephanou, A.1    Scarabelli, T.M.2    Knight, R.A.3    Latchman, D.S.4
  • 24
    • 0037012034 scopus 로고    scopus 로고
    • Caspase 9 is required for p53-dependent apoptosis and chemosensitivity in a human ovarian cancer cell line
    • DOI 10.1038/sj.onc.1205020
    • Wu GS, Ding Z. Caspase 9 is required for p53-dependent apoptosis and chemosensitivity in a human ovarian cancer cell line. Oncogene 21(1), 1-8 (2002). (Pubitemid 34076373)
    • (2002) Oncogene , vol.21 , Issue.1 , pp. 1-8
    • Gen, S.W.1    Ding, Z.2
  • 26
    • 1542329005 scopus 로고    scopus 로고
    • The erbB family: Targets for therapeutic development against cancer and therapeutic strategies using monoclonal antibodies and tyrosine kinase inhibitors
    • DOI 10.1146/annurev.med.55.091902.104433
    • Rowinsky EK. The erbB family: targets for therapeutic development against cancer and therapeutic strategies using monoclonal antibodies and tyrosine kinase inhibitors. Ann. Rev. Med. 55, 433-457 (2004). (Pubitemid 38316736)
    • (2004) Annual Review of Medicine , vol.55 , pp. 433-457
    • Rowinsky, E.K.1
  • 28
    • 70349475409 scopus 로고    scopus 로고
    • Saturn: A double-blind randomized phase III study of maintenance erlotinib versus placebo following nonprogression with first-line platinum-based chemotherapy in patients with advanced NSCLC
    • Cappuzzo F, Ciuleanu T, Stelmakh L et al. SATURN: a double-blind, randomized, Phase III study of maintenance erlotinib versus placebo following nonprogression with first-line platinum-based chemotherapy in patients with advanced NSCLC. J. Clin. Oncol. 27, 15s (2009).
    • (2009) J. Clin. Oncol. , vol.27
    • Cappuzzo, F.1    Ciuleanu, T.2    Stelmakh, L.3
  • 30
    • 15044356588 scopus 로고    scopus 로고
    • Detection of plasma hnRNP B1 mRNA, a new cancer biomarker, in lung cancer patients by quantitative real-time polymerase chain reaction
    • DOI 10.1016/j.lungcan.2004.10.007
    • Sueoka E, Sueoka N, Iwanaga K et al. Detection of plasma hnRNP B1 mRNA, a new cancer biomarker, in lung cancer patients by quantitative real-time polymerase chain reaction. Lung Cancer (Amsterdam, The Netherlands) 48(1), 77-83 (2005). (Pubitemid 40381002)
    • (2005) Lung Cancer , vol.48 , Issue.1 , pp. 77-83
    • Sueoka, E.1    Sueoka, N.2    Iwanaga, K.3    Sato, A.4    Suga, K.5    Hayashi, S.-I.6    Nagasawa, K.7    Nakachi, K.8
  • 31
    • 77955526422 scopus 로고    scopus 로고
    • Deregulated expression of hnRNP A/B proteins in human non-small cell lung cancer: Parallel assessment of protein and mRNA levels in paired tumour/non-tumour tissues
    • Boukakis G, Patrinou-Georgoula M, Lekarakou M, Valavanis C, Guialis A. Deregulated expression of hnRNP A/B proteins in human non-small cell lung cancer: parallel assessment of protein and mRNA levels in paired tumour/non-tumour tissues. BMC Cancer 10, 434 (2010).
    • (2010) BMC Cancer , vol.10 , pp. 434
    • Boukakis, G.1    Patrinou-Georgoula, M.2    Lekarakou, M.3    Valavanis, C.4    Guialis, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.