메뉴 건너뛰기




Volumn 62, Issue 3, 2015, Pages 391-397

17-AAG enhances the cytotoxicity of flavopiridol in mantle cell lymphoma via autophagy suppression

Author keywords

17 AAG; Autophagy; Flavopiridol; MCL

Indexed keywords

ACRIDINE ORANGE; BECLIN 1; FLAVOPIRIDOL; HEAT SHOCK PROTEIN 90; MITOGEN ACTIVATED PROTEIN KINASE; TANESPIMYCIN;

EID: 84969667384     PISSN: 00282685     EISSN: 13384317     Source Type: Journal    
DOI: 10.4149/neo_2015_047     Document Type: Article
Times cited : (6)

References (33)
  • 1
    • 0032784783 scopus 로고    scopus 로고
    • World Health Organization classification of neoplastic diseases of the hematopoietic and lymphoid tissues: Report of the Clinical Advisory Committee meeting
    • HARRIS N, JAFFE E, DIEBOLD J, FLANDRIN G, MULL-ER-HERMELINK H, et al. World Health Organization classification of neoplastic diseases of the hematopoietic and lymphoid tissues: report of the Clinical Advisory Committee meeting. Journal of clinical oncology 1999; 17: 3835-3849.
    • (1999) Journal of clinical oncology , vol.17 , pp. 3835-3849
    • Harris, N.1    Jaffe, E.2    Diebold, J.3    Flandrin, G.4    Mull-Er-Hermelink, H.5
  • 2
    • 0028225201 scopus 로고
    • European Lymphoma Task Force (ELTF): Report of the workshop on Mantle Cell Lymphoma (MCL)
    • ZUCCA E, STEIN H, COIFFIER B. European Lymphoma Task Force (ELTF): Report of the workshop on Mantle Cell Lymphoma (MCL). Annals of oncology 1994; 5: 507-511.
    • (1994) Annals of oncology , vol.5 , pp. 507-511
    • Zucca, E.1    Stein, H.2    Coiffier, B.3
  • 3
    • 9244239811 scopus 로고    scopus 로고
    • G1 cell-cycle control and cancer
    • MASSAGUE J. G1 cell-cycle control and cancer. Nature 2004; 432: 298-306. http: //dx. doi. org/10. 1038/nature03094
    • (2004) Nature , vol.432 , pp. 298-306
    • Massague, J.1
  • 4
    • 4444331760 scopus 로고    scopus 로고
    • Gene profiling and the cyclin-dependent kinase inhibitor flavopiridol: What's in a name?
    • GRANT S, DENT P. Gene profiling and the cyclin-dependent kinase inhibitor flavopiridol: what's in a name? Molecular cancer therapeutics 2004; 3: 873-875.
    • (2004) Molecular cancer therapeutics , vol.3 , pp. 873-875
    • Grant, S.1    Dent, P.2
  • 5
    • 84907197386 scopus 로고    scopus 로고
    • Antitumor Effects of Flavopiridol on Human Uterine Leiomyoma In Vitro and in a Xenograft model
    • LEE H, BAEK J, SHIN S, KWON S, CHA S, et al. Antitumor Effects of Flavopiridol on Human Uterine Leiomyoma In Vitro and in a Xenograft model. Reprod Sci 2014; 21: 1153-1160. http: //dx. doi. org/10. 1177/1933719114525266
    • (2014) Reprod Sci , vol.21 , pp. 1153-1160
    • Lee, H.1    Baek, J.2    Shin, S.3    Kwon, S.4    Cha, S.5
  • 7
    • 84904768570 scopus 로고    scopus 로고
    • JUNB promotes the survival of Flavopiridol treated human breast cancer cells
    • HICKS M, HU Q, MACRAE E, DEWILLE J. JUNB promotes the survival of Flavopiridol treated human breast cancer cells. Biochemical and biophysical research communications 2014; 450: 19-24. http: //dx. doi. Org/10. 1016/j. bbrc. 2014. 05. 057
    • (2014) Biochemical and biophysical research communications , vol.450 , pp. 19-24
    • Hicks, M.1    Hu, Q.2    Macrae, E.3    Dewille, J.4
  • 8
    • 0034661538 scopus 로고    scopus 로고
    • Protein kinase inhibitors flavopiridol and 7-hydroxy-staurosporine down-regulate antiapoptosis proteins in B-cell chronic lymphocytic leukemia
    • KITADA S, ZAPATA J, ANDREEFF M, REED J. Protein kinase inhibitors flavopiridol and 7-hydroxy-staurosporine down-regulate antiapoptosis proteins in B-cell chronic lymphocytic leukemia. Blood 2000; 96: 393-397.
    • (2000) Blood , vol.96 , pp. 393-397
    • Kitada, S.1    Zapata, J.2    Andreeff, M.3    Reed, J.4
  • 9
    • 84892853268 scopus 로고    scopus 로고
    • Flavopiridol can be safely administered using a pharmacologically derived schedule and demonstrates activity in relapsed and refractory non-Hodgkin's lymphoma
    • JONES J, RUPERT A, POI M, PHELPS M, ANDRITSOS L, et al. Flavopiridol can be safely administered using a pharmacologically derived schedule and demonstrates activity in relapsed and refractory non-Hodgkin's lymphoma. American journal of hematology 2014; 89: 19-24. http: //dx. doi. org/10. 1002/aih. 23568
    • (2014) American journal of hematology , vol.89 , pp. 19-24
    • Jones, J.1    Rupert, A.2    Poi, M.3    Phelps, M.4    Andritsos, L.5
  • 10
    • 84881399114 scopus 로고    scopus 로고
    • Emerging drug profile: Cyclin-dependent kinase inhibitors
    • BLACHLY J, BYRD J. Emerging drug profile: cyclin-dependent kinase inhibitors. Leukemia & lymphoma2013; 54: 2133-2143. http: //dx. doi. org/10. 3109/10428194. 2013. 783911
    • (2013) Leukemia & lymphoma , vol.54 , pp. 2133-2143
    • Blachly, J.1    Byrd, J.2
  • 11
    • 84877323041 scopus 로고    scopus 로고
    • Autophagy and ER stress play an essential role in the mechanism of action and drug resistance of the cyclin-dependent kinase inhibitor flavopiridol
    • MAHONEY E, BYRD J, JOHNSON A. Autophagy and ER stress play an essential role in the mechanism of action and drug resistance of the cyclin-dependent kinase inhibitor flavopiridol. Autophagy 2013; 9: 434-435. http: //dx. doi. org/10. 4161/auto. 23027
    • (2013) Autophagy , vol.9 , pp. 434-435
    • Mahoney, E.1    Byrd, J.2    Johnson, A.3
  • 12
    • 84865183563 scopus 로고    scopus 로고
    • ER stress and autophagy: New discoveries in the mechanism of action and drug resistance of the cyclin-dependent kinase inhibitor flavopiridol
    • MAHONEY E, LUCAS D, GUPTA S, WAGNER A, HERMAN S, et al. ER stress and autophagy: new discoveries in the mechanism of action and drug resistance of the cyclin-dependent kinase inhibitor flavopiridol. Blood 2012; 120: 1262-1273. http: //dx. doi. org/10. 1182/blood-2011-12-400184
    • (2012) Blood , vol.120 , pp. 1262-1273
    • Mahoney, E.1    Lucas, D.2    Gupta, S.3    Wagner, A.4    Herman, S.5
  • 13
    • 0026664393 scopus 로고
    • High constitutive expression of heat shock protein 90 alpha in human acute leukemia cells
    • YUFU Y, NISHIMURA J, NAWATA H. High constitutive expression of heat shock protein 90 alpha in human acute leukemia cells. Leuk Res 1992; 16: 597-605. http: //dx. doi. org/10. 1016/0145-2126(92)90008-U
    • (1992) Leuk Res , vol.16 , pp. 597-605
    • Yufu, Y.1    Nishimura, J.2    Nawata, H.3
  • 14
    • 0026749295 scopus 로고
    • Unusual expression and localization of heat-shock proteins in human tumor cells
    • FERRARINI M, HELTAI S, ZOCCHI M, RUGARLI C. Unusual expression and localization of heat-shock proteins in human tumor cells. Int J Cancer 1992; 51: 613-619. http: // dx. doi. org/10. 1002/ijc. 2910510418
    • (1992) Int J Cancer , vol.51 , pp. 613-619
    • Ferrarini, M.1    Heltai, S.2    Zocchi, M.3    Rugarli, C.4
  • 15
    • 80051688648 scopus 로고    scopus 로고
    • Functional interaction of heat shock protein 90 and Beclin 1 modulates Toll-like receptor-mediated autophagy
    • XU C, LIU J, HSU L, LUO Y, XIANG R, et al. Functional interaction of heat shock protein 90 and Beclin 1 modulates Toll-like receptor-mediated autophagy. FASEB J 2011; 25: 2700-2710. http: //dx. doi. org/10. 1096/fj. 10-167676
    • (2011) FASEB J , vol.25 , pp. 2700-2710
    • Xu, C.1    Liu, J.2    Hsu, L.3    Luo, Y.4    Xiang, R.5
  • 16
    • 32644440045 scopus 로고    scopus 로고
    • An-tiapoptotic function of Bcl-2 in mast cells is dependent on its association with heat shock protein 90beta
    • COHEN-SAIDON C, CARMI I, KEREN A, RAZIN E. An-tiapoptotic function of Bcl-2 in mast cells is dependent on its association with heat shock protein 90beta. Blood 2006; 107: 1413-1420. http: //dx. doi. org/10. 1182/blood-2005-07-2648
    • (2006) Blood , vol.107 , pp. 1413-1420
    • Cohen-Saidon, C.1    Carmi, I.2    Keren, A.3    Razin, E.4
  • 17
    • 0029813620 scopus 로고    scopus 로고
    • Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf-1-MEK-mitogen-activated protein kinase signalling pathway
    • SCHULTE T, BLAGOSKLONNY M, ROMANOVA L, MUSHINSKI J, MONIA BP, et al. Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf-1-MEK-mitogen-activated protein kinase signalling pathway. Mol Cell Biol 1996; 16: 5839-5845.
    • (1996) Mol Cell Biol , vol.16 , pp. 5839-5845
    • Schulte, T.1    Blagosklonny, M.2    Romanova, L.3    Mushinski, J.4    Monia, B.P.5
  • 18
    • 84857048554 scopus 로고    scopus 로고
    • Identification of HSP90 as a new GABARAPL1 (GECl)-interacting protein
    • SEGUIN-PY S, CROIZIER S, CHAKRAMA F, DESPOUY G, LE GRAND J, et al. Identification of HSP90 as a new GABARAPL1 (GECl)-interacting protein. Biochimie 2012; 94: 748-758. http: //dx. doi. Org/10. 1016/j. biochi. 2011. ll. 006
    • (2012) Biochimie , vol.94 , pp. 748-758
    • Seguin-Py, S.1    Croizier, S.2    Chakrama, F.3    Despouy, G.4    Le Grand, J.5
  • 19
    • 0038404927 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 function down-regulates Akt kinase and sensitizes tumors to Taxol
    • SOLIT D, BASSO A, OLSHEN A, SCHER H, ROSEN N. Inhibition of heat shock protein 90 function down-regulates Akt kinase and sensitizes tumors to Taxol. Cancer Res 2003; 63: 2139-2144.
    • (2003) Cancer Res , vol.63 , pp. 2139-2144
    • Solit, D.1    Basso, A.2    Olshen, A.3    Scher, H.4    Rosen, N.5
  • 20
    • 55749084036 scopus 로고    scopus 로고
    • Cisplatin abrogates the geldanamycin-induced heat shock response
    • MCCOLLUM A, LUKASIEWICZ K, TENEYCK C, LINGLE W, TOFT DO, et al. Cisplatin abrogates the geldanamycin-induced heat shock response. Mol Cancer Ther 2008; 7: 3256-3264. http: //dx. doi. org/10. 1158/1535-7163. MCT-08-0157
    • (2008) Mol Cancer Ther , vol.7 , pp. 3256-3264
    • McCollum, A.1    Lukasiewicz, K.2    Teneyck, C.3    Lingle, W.4    Toft, D.O.5
  • 21
    • 74049091229 scopus 로고    scopus 로고
    • BIIB021, a novel Hsp90 inhibitor, sensitizes head and neck squamous cell carcinoma to radiotherapy
    • YIN X, ZHANG H, LUNDGREN K, WILSON L, BURROWS F, et al. BIIB021, a novel Hsp90 inhibitor, sensitizes head and neck squamous cell carcinoma to radiotherapy. Int J Cancer 2010; 126: 1216-1225.
    • (2010) Int J Cancer , vol.126 , pp. 1216-1225
    • Yin, X.1    Zhang, H.2    Lundgren, K.3    Wilson, L.4    Burrows, F.5
  • 22
    • 58149180924 scopus 로고    scopus 로고
    • A phase 1 dose-escalation study of irinotecan in combination with 17-allylamino-17-demethoxygeldanamycin in patients with solid tumors
    • TSE A, KLIMSTRA D, GONEN M, SHAH M, SHEIKH T, et al. A phase 1 dose-escalation study of irinotecan in combination with 17-allylamino-17-demethoxygeldanamycin in patients with solid tumors. Clin Cancer Res 2008; 14: 6704-6711. http: //dx. doi. org/10. 1158/1078-0432. CCR-08-1006
    • (2008) Clin Cancer Res , vol.14 , pp. 6704-6711
    • Tse, A.1    Klimstra, D.2    Gonen, M.3    Shah, M.4    Sheikh, T.5
  • 23
    • 50349093362 scopus 로고    scopus 로고
    • A phase I study of 17-allylami-no-17-demethoxygeldanamycin combined with paclitaxel in patients with advanced solid malignancies
    • RAMALINGAM S, EGORIN M, RAMANATHAN R, REMICK S, SIKORSKI R, et al. A phase I study of 17-allylami-no-17-demethoxygeldanamycin combined with paclitaxel in patients with advanced solid malignancies. Clin Cancer Res 2008; 14: 3456-3461. http: //dx. doi. org/10. 1158/1078-0432. CCR-07-5088
    • (2008) Clin Cancer Res , vol.14 , pp. 3456-3461
    • Ramalingam, S.1    Egorin, M.2    Ramanathan, R.3    Remick, S.4    Sikorski, R.5
  • 24
    • 79960985354 scopus 로고    scopus 로고
    • HSP90 inhibition is effective in breast cancer: A phase II trial oftanespimycin (17-AAG) plus trastuzumab in patients with HER2-positive metastatic breast cancer progressing on trastuzumab
    • MODI S, LINDEN H, SOLIT D, CHANDARLAPATY S, ROSEN N, et al. HSP90 inhibition is effective in breast cancer: a phase II trial oftanespimycin (17-AAG) plus trastuzumab in patients with HER2-positive metastatic breast cancer progressing on trastuzumab. Clin Cancer Res 2011; 17: 5132-5139. http: //dx. doi. org/10. 1158/1078-0432. CCR-ll-0072
    • (2011) Clin Cancer Res , vol.17 , pp. 5132-5139
    • Modi, S.1    Linden, H.2    Solit, D.3    Chandarlapaty, S.4    Rosen, N.5
  • 25
    • 77950886468 scopus 로고    scopus 로고
    • Methods for detecting autophagy and determining autophagy-induced cell death
    • CHEN Y, AZAD M, GIBSON S. Methods for detecting autophagy and determining autophagy-induced cell death. Can J Physiol Pharmacol 2010; 88: 285-295. http: //dx. doi. org/10. 1139/Y10-010
    • (2010) Can J Physiol Pharmacol , vol.88 , pp. 285-295
    • Chen, Y.1    Azad, M.2    Gibson, S.3
  • 26
    • 34250894388 scopus 로고    scopus 로고
    • BH3-only proteins and BH3 mimetics induce autophagy by competitively disrupting the interaction between Beclin 1 and Bcl-2/Bcl-X(L)
    • MAIURI M, CRIOLLO A, TASDEMIR E, VICENCIO J, TAJEDDINE N, et al. BH3-only proteins and BH3 mimetics induce autophagy by competitively disrupting the interaction between Beclin 1 and Bcl-2/Bcl-X(L). Autophagy 2007; 3: 374-376. http: //dx. doi. org/10. 4161/auto. 4237
    • (2007) Autophagy , vol.3 , pp. 374-376
    • Maiuri, M.1    Criollo, A.2    Tasdemir, E.3    Vicencio, J.4    Tajeddine, N.5
  • 27
    • 84876717451 scopus 로고    scopus 로고
    • Hsp90 inhibitors as anti-cancer agents, from basic discoveries to clinical development
    • SOGA S, AKINAGA S, SHIOTSU Y. Hsp90 inhibitors as anti-cancer agents, from basic discoveries to clinical development. Curr Pharm Des 2013; 19: 366-376. http: //dx. doi. org/10. 2174/138161213804143617
    • (2013) Curr Pharm Des , vol.19 , pp. 366-376
    • Soga, S.1    Akinaga, S.2    Shiotsu, Y.3
  • 28
    • 3342895063 scopus 로고    scopus 로고
    • Diallyl trisulfide-induced apoptosis in human prostate cancer cells involves c-Jun N-terminal kinase and extracellular-signal regulated kinase-mediated phosphorylation of Bcl-2
    • XIAO D, CHOI S, JOHNSON D, VOGEL V, JOHNSON C, et al. Diallyl trisulfide-induced apoptosis in human prostate cancer cells involves c-Jun N-terminal kinase and extracellular-signal regulated kinase-mediated phosphorylation of Bcl-2. Oncogene 2004; 23: 5594-5606. http: //dx. doi. org/10. 1038/sj. one. 1207747
    • (2004) Oncogene , vol.23 , pp. 5594-5606
    • Xiao, D.1    Choi, S.2    Johnson, D.3    Vogel, V.4    Johnson, C.5
  • 29
    • 84897846473 scopus 로고    scopus 로고
    • HCC cells with high levels of Bcl-2 are resistant to ABT-737 via activation of the ROS-JNK-autophagy pathway
    • NI Z, WANG B, DAI X, DING W, YANG T, LI X, et al. HCC cells with high levels of Bcl-2 are resistant to ABT-737 via activation of the ROS-JNK-autophagy pathway. Free Radic BiolMed2014; 70: 194-203. http: //dx. doi. Org/10. 1016/j. freeradbiomed. 2014. 02. 012
    • (2014) Free Radic BiolMed , vol.70 , pp. 194-203
    • Ni, Z.1    Wang, B.2    Dai, X.3    Ding, W.4    Yang, T.5    Li, X.6
  • 30
    • 77956404377 scopus 로고    scopus 로고
    • Eaten alive: A history of macro-autophagy
    • YANG Z, KLIONSKY D. Eaten alive: a history of macro-autophagy. Nat Cell Biol 2010; 12: 814-822. http: //dx. doi. org/10. 1038/ncb0910-814
    • (2010) Nat Cell Biol , vol.12 , pp. 814-822
    • Yang, Z.1    Klionsky, D.2
  • 31
    • 34548188741 scopus 로고    scopus 로고
    • Self-eating and self-killing: Crosstalk between autophagy and apoptosis
    • MAIURI M, ZALCKVAR E, KIMCHI A, KROEMER G. Self-eating and self-killing: crosstalk between autophagy and apoptosis. Nat Rev Mol Cell Biol 2007; 8: 741-752. http: // dx. doi. org/10. 1038/nrm2239
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 741-752
    • Maiuri, M.1    Zalckvar, E.2    Kimchi, A.3    Kroemer, G.4
  • 32
    • 0031054517 scopus 로고    scopus 로고
    • The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase
    • STANCATO L, SILVERSTEIN A, OWENS-GRILLO J, CHOW Y, JOVE R, et al. The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase. J Biol Chem 1997; 272: 4013-4020. http: //dx. doi. org/10. 1074/jbc. 272. 7. 4013
    • (1997) J Biol Chem , vol.272 , pp. 4013-4020
    • Stancato, L.1    Silverstein, A.2    Owens-Grillo, J.3    Chow, Y.4    Jove, R.5
  • 33
    • 84905679330 scopus 로고    scopus 로고
    • Disruption of autophagy by the histone deacetylase inhibitor MGCDO103 and its therapeutic implication in B-cell chronic lymphocytic leukemia
    • EL-KHOURY V, PIERSON S, SZWARCBART E, BRONS N, ROLAND O, et al. Disruption of autophagy by the histone deacetylase inhibitor MGCDO103 and its therapeutic implication in B-cell chronic lymphocytic leukemia. Leukemia 2014; 28: 1636-1646. http: //dx. doi. org/10. 1038/leu. 2014. 19
    • (2014) Leukemia , vol.28 , pp. 1636-1646
    • El-Khoury, V.1    Pierson, S.2    Szwarcbart, E.3    Brons, N.4    Roland, O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.