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Volumn 16, Issue 7, 2011, Pages 671-682

Inhibition of cathepsin L lowers the apoptotic threshold of glioblastoma cells by up-regulating p53 and transcription of caspases 3 and 7

Author keywords

Apoptosis; Caspase 3; Caspase 7; Cathepsin L; Glioblastoma; P53

Indexed keywords

CASPASE 3; CASPASE 7; CATHEPSIN L; PROTEIN P53;

EID: 80051546729     PISSN: 13608185     EISSN: 1573675X     Source Type: Journal    
DOI: 10.1007/s10495-011-0600-6     Document Type: Article
Times cited : (35)

References (42)
  • 1
    • 34250877865 scopus 로고    scopus 로고
    • Genetic pathways to primary and secondary glioblastoma
    • DOI 10.2353/ajpath.2007.070011
    • Ohgaki H, Kleihues P (2007) Genetic pathways to primary and secondary glioblastoma. Am J Pathol 170:1445-1453 (Pubitemid 47339290)
    • (2007) American Journal of Pathology , vol.170 , Issue.5 , pp. 1445-1453
    • Ohgaki, H.1    Kleihues, P.2
  • 2
    • 34648815810 scopus 로고    scopus 로고
    • Emerging roles of proteases in tumour suppression
    • DOI 10.1038/nrc2228, PII NRC2228
    • Lopez-Otin C, Matrisian LM (2007) Emerging roles of proteases in tumour suppression. Nat Rev Cancer 7:800-808 (Pubitemid 47463671)
    • (2007) Nature Reviews Cancer , vol.7 , Issue.10 , pp. 800-808
    • Lopez-Otin, C.1    Matrisian, L.M.2
  • 5
    • 0033973428 scopus 로고    scopus 로고
    • Cells producing cathepsins D, B, and L in human breast carcinoma and their association with prognosis
    • Lah TT, Kalman E, Najjar D, Gorodetsky E, Brennan P, Somers R, Daskal I (2000) Cells producing cathepsins D, B, and L in human breast carcinoma and their association with prognosis. Hum Pathol 31:149-160 (Pubitemid 30090643)
    • (2000) Human Pathology , vol.31 , Issue.2 , pp. 149-160
    • Lah, T.T.1    Kalman, E.2    Najjar, D.3    Gorodetsky, E.4    Brennan, P.5    Somers, R.6    Daskal, I.7
  • 6
    • 26044438493 scopus 로고    scopus 로고
    • Cathepsin L in glioma progression: Comparison with cathepsin B
    • DOI 10.1016/j.cdp.2005.07.006, PII S0361090X05000917
    • Strojnik T, Kavalar R, Trinkaus M, Lah TT (2005) Cathepsin L in glioma progression: comparison with cathepsin B. Cancer Detect Prev 29:448-455 (Pubitemid 41406140)
    • (2005) Cancer Detection and Prevention , vol.29 , Issue.5 , pp. 448-455
    • Strojnik, T.1    Kavalar, R.2    Trinkaus, M.3    Lah, T.T.4
  • 7
    • 1642535587 scopus 로고    scopus 로고
    • Inhibition of tumorigenicity and metastasis of human melanoma cells by anti-cathepsin L single chain variable fragment
    • DOI 10.1158/0008-5472.CAN-03-1717
    • Rousselet N, Mills L, Jean D, Tellez C, Bar-Eli M, Frade R (2004) Inhibition of tumorigenicity and metastasis of human melanoma cells by anti-cathepsin L single chain variable fragment. Cancer Res 64:146-151 (Pubitemid 38114092)
    • (2004) Cancer Research , vol.64 , Issue.1 , pp. 146-151
    • Rousselet, N.1    Mills, L.2    Jean, D.3    Tellez, C.4    Bar-Eli, M.5    Frade, R.6
  • 8
    • 0037038669 scopus 로고    scopus 로고
    • Mitochondrial stress-induced calcium signaling, phenotypic changes and invasive behavior in human lung carcinoma A549 cells
    • DOI 10.1038/sj.onc.1205983
    • Amuthan G, Biswas G, Ananadatheerthavarada HK, Vijayasarathy C, Shephard HM, Avadhani NG (2002) Mitochondrial stressinduced calcium signaling, phenotypic changes and invasive behavior in human lung carcinoma A549 cells. Oncogene 21: 7839-7849 (Pubitemid 35398842)
    • (2002) Oncogene , vol.21 , Issue.51 , pp. 7839-7849
    • Amuthan, G.1    Biswas, G.2    Ananadatheerthavarada, H.K.3    Vijayasarathy, C.4    Shephard, H.M.5    Avadhani, N.G.6
  • 9
    • 0037058622 scopus 로고    scopus 로고
    • Expression of cysteine peptidase cathepsin L and its inhibitors stefins A and B in relation to tumorigenicity of breast cancer cell lines
    • DOI 10.1016/S0304-3835(02)00452-4, PII S0304383502004524
    • Zajc I, Sever N, Bervar A, Lah TT (2002) Expression of cysteine peptidase cathepsin L and its inhibitors stefins A and B in relation to tumorigenicity of breast cancer cell lines. Cancer Lett 187:185-190 (Pubitemid 35279348)
    • (2002) Cancer Letters , vol.187 , Issue.1-2 , pp. 185-190
    • Zajc, I.1    Sever, N.2    Bervar, A.3    Lah, T.T.4
  • 10
    • 33750703157 scopus 로고    scopus 로고
    • Cathepsin L affects apoptosis of glioblastoma cells: A potential implication in the design of cancer therapeutics
    • Zajc I, Hreljac I, Lah T (2006) Cathepsin L affects apoptosis of glioblastoma cells: a potential implication in the design of cancer therapeutics. Anticancer Res 26:3357-3364 (Pubitemid 44701509)
    • (2006) Anticancer Research , vol.26 , Issue.5 A , pp. 3357-3364
    • Zajc, I.1    Hreljac, I.2    Lah, T.3
  • 11
    • 75049084598 scopus 로고    scopus 로고
    • Posttranslational regulation of cathepsin B, but not of other cysteine cathepsins, contributes to increased glioblastoma cell invasiveness in vitro
    • Gole B, Duran Alonso MB, Dolenc V, Lah T (2009) Posttranslational regulation of cathepsin B, but not of other cysteine cathepsins, contributes to increased glioblastoma cell invasiveness in vitro. Pathol Oncol Res 15:711-723
    • (2009) Pathol Oncol Res , vol.15 , pp. 711-723
    • Gole, B.1    Duran Alonso, M.B.2    Dolenc, V.3    Lah, T.4
  • 13
    • 0035793580 scopus 로고    scopus 로고
    • Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route
    • Stoka V, Turk B, Schendel SL, Kim TH, Cirman T, Snipas SJ, Ellerby LM et al (2001) Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route. J Biol Chem 276:3149-3157
    • (2001) J Biol Chem , vol.276 , pp. 3149-3157
    • Stoka, V.1    Turk, B.2    Schendel, S.L.3    Kim, T.H.4    Cirman, T.5    Snipas, S.J.6    Ellerby, L.M.7
  • 14
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC (1998) Mitochondria and apoptosis. Science 281:1309-1312 (Pubitemid 28406816)
    • (1998) Science , vol.281 , Issue.5381 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 16
    • 0037328905 scopus 로고    scopus 로고
    • Selective suppression of cathepsin L by antisense cDNA impairs human brain tumor cell invasion in vitro and promotes apoptosis
    • DOI 10.1038/sj.cgt.7700546
    • Levicar N, Dewey RA, Daley E, Bates TE, Davies D, Kos J, Pilkington GJ et al (2003) Selective suppression of cathepsin L by antisense cDNA impairs human brain tumor cell invasion in vitro and promotes apoptosis. Cancer Gene Ther 10:141-151 (Pubitemid 36228262)
    • (2003) Cancer Gene Therapy , vol.10 , Issue.2 , pp. 141-151
    • Levicar, N.1    Dewey, R.A.2    Daley, E.3    Bates, T.E.4    Davies, D.5    Kos, J.6    Pilkington, G.J.7    Lah, T.T.8
  • 17
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M, Werb Z (2002) New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2: 161-174 (Pubitemid 37328786)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.3 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 18
    • 77955389409 scopus 로고    scopus 로고
    • Spontaneous malignant transformation of human mesenchymal stem cells reflects crosscontamination: Putting the research field on track-letter
    • Torsvik A, Rosland GV, Svendsen A, Molven A, Immervoll H, McCormack E, Lonning PE et al (2010) Spontaneous malignant transformation of human mesenchymal stem cells reflects crosscontamination: putting the research field on track-letter. Cancer Res 70:6393-6396
    • (2010) Cancer Res , vol.70 , pp. 6393-6396
    • Torsvik, A.1    Rosland, G.V.2    Svendsen, A.3    Molven, A.4    Immervoll, H.5    McCormack, E.6    Lonning, P.E.7
  • 19
  • 20
    • 33746593686 scopus 로고    scopus 로고
    • An alternative method to amplify RNA without loss of signal conservation for expression analysis with a proteinase DNA microarray in the ArrayTube format
    • Schuler S, Wenz I, Wiederanders B, Slickers P, Ehricht R (2006) An alternative method to amplify RNA without loss of signal conservation for expression analysis with a proteinase DNA microarray in the ArrayTube format. BMC Genomics 7:144
    • (2006) BMC Genomics , vol.7 , pp. 144
    • Schuler, S.1    Wenz, I.2    Wiederanders, B.3    Slickers, P.4    Ehricht, R.5
  • 21
    • 77952830627 scopus 로고    scopus 로고
    • Differential role of cathepsins B and L in autophagy-associated cell death induced by arsenic trioxide in U87 human glioblastoma cells
    • Pucer A, Castino R, Mirkovic B, Falnoga I, Slejkovec Z, Isidoro C, Lah TT (2010) Differential role of cathepsins B and L in autophagy-associated cell death induced by arsenic trioxide in U87 human glioblastoma cells. Biol Chem 391:519-531
    • (2010) Biol Chem , vol.391 , pp. 519-531
    • Pucer, A.1    Castino, R.2    Mirkovic, B.3    Falnoga, I.4    Slejkovec, Z.5    Isidoro, C.6    Lah, T.T.7
  • 23
    • 0034672644 scopus 로고    scopus 로고
    • Generation and degradation of human endostatin proteins by various proteinases
    • Ferreras M, Felbor U, Lenhard T, Olsen BR, Delaisse J (2000) Generation and degradation of human endostatin proteins by various proteinases. FEBS Lett 486:247-251
    • (2000) FEBS Lett , vol.486 , pp. 247-251
    • Ferreras, M.1    Felbor, U.2    Lenhard, T.3    Olsen, B.R.4    Delaisse, J.5
  • 24
    • 1942470581 scopus 로고    scopus 로고
    • A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor
    • DOI 10.1016/S1097-2765(04)00209-6, PII S1097276504002096
    • Goulet B, Baruch A, Moon NS, Poirier M, Sansregret LL, Erickson A, Bogyo M et al (2004) A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor. Mol Cell 14:207-219 (Pubitemid 38515648)
    • (2004) Molecular Cell , vol.14 , Issue.2 , pp. 207-219
    • Goulet, B.1    Baruch, A.2    Moon, N.-S.3    Poirier, M.4    Sansregret, L.L.5    Erickson, A.6    Bogyo, M.7    Nepveu, A.8
  • 25
    • 33746055274 scopus 로고    scopus 로고
    • Cathepsin L splice variants in human breast cell lines
    • DOI 10.1515/BC.2006.080, PII BCHM3875629
    • Caserman S, Kenig S, Sloane BF, Lah TT (2006) Cathepsin L splice variants in human breast cell lines. Biol Chem 387: 629-634 (Pubitemid 44071466)
    • (2006) Biological Chemistry , vol.387 , Issue.5 , pp. 629-634
    • Caserman, S.1    Kenig, S.2    Sloane, B.F.3    Lan, T.T.4
  • 26
    • 34548689404 scopus 로고    scopus 로고
    • Increased expression and activity of nuclear cathepsin L in cancer cells suggests a novel mechanism of cell transformation
    • DOI 10.1158/1541-7786.MCR-07-0160
    • Goulet B, Sansregret L, Leduy L, Bogyo M, Weber E, Chauhan SS, Nepveu A (2007) Increased expression and activity of nuclear cathepsin L in cancer cells suggests a novel mechanism of cell transformation. Mol Cancer Res 5:899-907 (Pubitemid 47416667)
    • (2007) Molecular Cancer Research , vol.5 , Issue.9 , pp. 899-907
    • Goulet, B.1    Sansregret, L.2    Leduy, L.3    Bogyo, M.4    Weber, E.5    Chauhan, S.S.6    Nepveu, A.7
  • 27
    • 66149088069 scopus 로고    scopus 로고
    • Localization of nuclear cathepsin L and its association with disease progression and poor outcome in colorectal cancer
    • Sullivan S, Tosetto M, Kevans D, Coss A, Wang L, O'Donoghue D, Hyland J et al (2009) Localization of nuclear cathepsin L and its association with disease progression and poor outcome in colorectal cancer. Int J Cancer 125:54-61
    • (2009) Int J Cancer , vol.125 , pp. 54-61
    • Sullivan, S.1    Tosetto, M.2    Kevans, D.3    Coss, A.4    Wang, L.5    O'Donoghue, D.6    Hyland, J.7
  • 29
    • 0037418609 scopus 로고    scopus 로고
    • Redox control of hepatic cell death
    • DOI 10.1016/S0378-4274(02)00425-3, PII S0378427402004253
    • Hentze H, Latta M, Kunstle G, Lucas R, Wendel A (2003) Redox control of hepatic cell death. Toxicol Lett 139:111-118 (Pubitemid 36298969)
    • (2003) Toxicology Letters , vol.139 , Issue.2-3 , pp. 111-118
    • Hentze, H.1    Latta, M.2    Kunstle, G.3    Lucas, R.4    Wendel, A.5
  • 30
    • 2442476459 scopus 로고    scopus 로고
    • Lysosomes in cell death
    • DOI 10.1038/sj.onc.1207512
    • Guicciardi ME, Leist M, Gores GJ (2004) Lysosomes in cell death. Oncogene 23:2881-2890 (Pubitemid 38638850)
    • (2004) Oncogene , vol.23 , Issue.16 REV. ISS. 2 , pp. 2881-2890
    • Guicciardi, M.E.1    Leist, M.2    Gores, G.J.3
  • 31
    • 0347481379 scopus 로고    scopus 로고
    • Prohibitin Induces the Transcriptional Activity of p53 and Is Exported from the Nucleus upon Apoptotic Signaling
    • DOI 10.1074/jbc.M305171200
    • Fusaro G, Dasgupta P, Rastogi S, Joshi B, Chellappan S (2003) Prohibitin induces the transcriptional activity of p53 and is exported from the nucleus upon apoptotic signaling. J Biol Chem 278:47853-47861 (Pubitemid 37523233)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.48 , pp. 47853-47861
    • Fusaro, G.1    Dasgupta, P.2    Rastogi, S.3    Joshi, B.4    Chellappan, S.5
  • 32
    • 33846286148 scopus 로고    scopus 로고
    • Differential regulation of human YY1 and caspase 7 promoters by prohibitin through E2F1 and p53 binding sites
    • DOI 10.1042/BJ20060364
    • Joshi B, Rastogi S, Morris M, Carastro LM, DeCook C, Seto E, Chellappan SP (2007) Differential regulation of human YY1 and caspase 7 promoters by prohibitin through E2F1 and p53 binding sites. Biochem J 401:155-166 (Pubitemid 46114609)
    • (2007) Biochemical Journal , vol.401 , Issue.1 , pp. 155-166
    • Joshi, B.1    Rastogi, S.2    Morris, M.3    Carastro, L.M.4    DeCook, C.5    Seto, E.6    Chellappan, S.P.7
  • 36
    • 2442693040 scopus 로고    scopus 로고
    • Inhibition of p53 function diminishes androgen receptor-mediated signaling in prostate cancer cell lines
    • DOI 10.1038/sj.onc.1207346
    • Cronauer MV, Schulz WA, Burchardt T, Ackermann R, Burchardt M (2004) Inhibition of p53 function diminishes androgen receptor-mediated signaling in prostate cancer cell lines. Oncogene 23:3541-3549 (Pubitemid 38658420)
    • (2004) Oncogene , vol.23 , Issue.20 , pp. 3541-3549
    • Cronauer, M.V.1    Schulz, W.A.2    Burchardt, T.3    Ackermann, R.4    Burchardt, M.5
  • 37
    • 0034485661 scopus 로고    scopus 로고
    • Cathepsin inhibition induces apoptotic death in human leukemia and lymphoma cells
    • Zhu DM, Uckun FM (2000) Cathepsin inhibition induces apoptotic death in human leukemia and lymphoma cells. Leuk Lymphoma 39:343-354 (Pubitemid 32162371)
    • (2000) Leukemia and Lymphoma , vol.39 , Issue.3-4 , pp. 343-354
    • Zhu, D.-M.1    Uckun, F.M.2
  • 39
    • 77951599543 scopus 로고    scopus 로고
    • Targeting brain cancer: Advances in the molecular pathology of malignant glioma and medulloblastoma
    • Huse JT, Holland EC (2010) Targeting brain cancer: advances in the molecular pathology of malignant glioma and medulloblastoma. Nat Rev Cancer 10:319-331
    • (2010) Nat Rev Cancer , vol.10 , pp. 319-331
    • Huse, J.T.1    Holland, E.C.2
  • 40
    • 50649084531 scopus 로고    scopus 로고
    • Loss of responsiveness to IGF-I in cells with reduced cathepsin L expression levels
    • Navab R, Pedraza C, Fallavollita L, Wang N, Chevet E, Auguste P, Jenna S et al (2008) Loss of responsiveness to IGF-I in cells with reduced cathepsin L expression levels. Oncogene 27: 4973-4985
    • (2008) Oncogene , vol.27 , pp. 4973-4985
    • Navab, R.1    Pedraza, C.2    Fallavollita, L.3    Wang, N.4    Chevet, E.5    Auguste, P.6    Jenna, S.7
  • 42
    • 0032580334 scopus 로고    scopus 로고
    • Potential role for cathepsin D in p53-dependent tumor suppression and chemosensitivity
    • Wu GS, Saftig P, Peters C, El-Deiry WS (1998) Potential role for cathepsin D in p53-dependent tumor suppression and chemosensitivity. Oncogene 16:2177-2183 (Pubitemid 28220647)
    • (1998) Oncogene , vol.16 , Issue.17 , pp. 2177-2183
    • Wu, G.S.1    Saftig, P.2    Peters, C.3    El-Deiry, W.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.