Cell death induced by 2-phenylethynesulfonamide uncovers a pro-survival function of BAX

Cancer Letters

Volumn 354, Issue 1, 2014, Pages 115-121

  Mattiolo, Paolo ^a   Barbero Farran, Ares ^a   Amigó, Josep ^a   Ripamonti, Marta ^a   Ribas, Judit ^a   Boix, Jacint ^a  

^a UNIVERSITY OF LLEIDA   (Spain)

Author keywords

BAK; BAX; Cell death; Mdivi 1; Mitochondrial dynamics; Pifithrin

Indexed keywords

2 PHENYLETHYNESULFONAMIDE; ANTINEOPLASTIC AGENT; PROTEIN BAX; UNCLASSIFIED DRUG; 2 PHENYLACETYLENESULFONAMIDE; 2 PHENYLETHYLENESULFONAMIDE; 2-PHENYLACETYLENESULFONAMIDE; 2-PHENYLETHYLENESULFONAMIDE; 3 (2,4 DICHLORO 5 METHOXYPHENYL) 2 SULFANYL 4(3H) QUINAZOLINONE; 3-(2,4-DICHLORO-5-METHOXYPHENYL)-2-SULFANYL-4(3H)-QUINAZOLINONE; BAX PROTEIN, MOUSE; CASPASE; PROTEIN P53; QUINAZOLINONE DERIVATIVE; SULFONAMIDE;

ANIMAL CELL; ANTINEOPLASTIC ACTIVITY; APOPTOSIS; ARTICLE; AUTOPHAGOSOME; CELL DEATH; CELL VIABILITY; CONTROLLED STUDY; ELECTRON MICROSCOPY; MEMBRANE PERMEABILITY; MITOCHONDRIAL DYNAMICS; MORPHOLOGY; MOUSE; NONHUMAN; PHENOTYPE; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN LOCALIZATION; SURVIVAL RATE; ANIMAL; BAK; BAX; CELL SURVIVAL; CHEMISTRY; CYTOLOGY; DRUG EFFECT; FIBROBLAST; HELA CELL LINE; HUMAN; KNOCKOUT MOUSE; MDIVI-1; METABOLISM; MITOCHONDRIAL MEMBRANE; MITOCHONDRION; MUTATION; PIFITHRIN-Μ;

BAK; BAX; CELL DEATH; MDIVI-1; MITOCHONDRIAL DYNAMICS; PIFITHRIN-Μ;

ANIMALS; ANTINEOPLASTIC AGENTS; APOPTOSIS; BCL-2-ASSOCIATED X PROTEIN; CASPASES; CELL DEATH; CELL SURVIVAL; FIBROBLASTS; HELA CELLS; HUMANS; MICE; MICE, KNOCKOUT; MITOCHONDRIA; MITOCHONDRIAL MEMBRANES; MUTATION; PHENOTYPE; QUINAZOLINONES; SULFONAMIDES; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84910018393     PISSN: 03043835     EISSN: 18727980     Source Type: Journal    
DOI: 10.1016/j.canlet.2014.07.037     Document Type: Article

References (31)

1. Komarov P.G., Komarova E.A., Kondratov R.V., Christov-Tselkov K., Coon J.S., Chernov M.V., et al. A chemical inhibitor of p53 that protects mice from the side effects of cancer therapy. Science 1999, 285:1733-1737.
2. Speidel D. Transcription-independent p53 apoptosis: an alternative route to death. Trends Cell Biol 2010, 20:14-24.
3. Strom E., Sathe S., Komarov P.G., Chernova O.B., Pavlovska I., Shyshynova I., et al. Small-molecule inhibitor of p53 binding to mitochondria protects mice from gamma radiation. Nat. Chem. Biol 2006, 2:474-479.
4. Leu J.I., Pimkina J., Frank A., Murphy M.E., George D.L. A small molecule inhibitor of inducible heat shock protein 70. Mol. Cell 2009, 36:15-27.
5. Balaburski G.M., Leu J.I.-J., Beeharry N., Hayik S., Andrake M.D., Zhang G., et al. A modified HSP70 inhibitor shows broad activity as an anticancer agent. Mol. Cancer Res 2013, 11:219-229.
6. Leu J.I.-J., Pimkina J., Pandey P., Murphy M.E., George D.L. HSP70 inhibition by the small-molecule 2-phenylethynesulfonamide impairs protein clearance pathways in tumor cells. Mol. Cancer Res 2011, 9:936-947.
7. Granato M., Lacconi V., Peddis M., Lotti L.V., Renzo L.D., Gonnella R., et al. HSP70 inhibition by 2-phenylethynesulfonamide induces lysosomal cathepsin D release and immunogenic cell death in primary effusion lymphoma. Cell Death Dis 2013, 4:e730.
8. Zeng F., Tee C., Liu M., Sherry J.P., Dixon B., Duncker B.P., et al. The p53/HSP70 inhibitor, 2-phenylethynesulfonamide, causes oxidative stress, unfolded protein response and apoptosis in rainbow trout cells. Aquat. Toxicol 2014, 146:45-51.
9. Steele A.J., Prentice A.G., Hoffbrand A.V., Yogashangary B.C., Hart S.M., Lowdell M.W., et al. 2-Phenylacetylenesulfonamide (PAS) induces p53-independent apoptotic killing of B-chronic lymphocytic leukemia (CLL) cells. Blood 2009, 114:1217-1225.
10. Monma H., Harashima N., Inao T., Okano S., Tajima Y., Harada M. The HSP70 and autophagy inhibitor pifithrin-μ enhances the antitumor effects of TRAIL on human pancreatic cancer. Mol. Cancer Ther 2013, 12:341-351.
11. Lindsten T., Ross A.J., King A., Zong W.X., Rathmell J.C., Shiels H.A., et al. The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues. Mol. Cell 2000, 6:1389-1399.
12. Wei M.C., Zong W.X., Cheng E.H., Lindsten T., Panoutsakopoulou V., Ross A.J., et al. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 2001, 292:727-730.
13. Garrofe-Ochoa X., Melero-Fernandez de Mera R.M., Fernandez-Gomez F.J., Ribas J., Jordan J., Boix J. BAX and BAK proteins are required for cyclin-dependent kinase inhibitory drugs to cause apoptosis. Mol. Cancer Ther 2008, 7:3800-3806.
14. Ribas J., Yuste V.J., Garrofe-Ochoa X., Meijer L., Esquerda J.E., Boix J. 7-Bromoindirubin-3'-oxime uncovers a serine protease-mediated paradigm of necrotic cell death. Biochem. Pharmacol 2008, 76:39-52.
15. Ribas J., Boix J. Cell differentiation, caspase inhibition, and macromolecular synthesis blockage, but not BCL-2 or BCL-XL proteins, protect SH-SY5Y cells from apoptosis triggered by two CDK inhibitory drugs. Exp. Cell Res 2004, 295:9-24.
16. Ribas J., Gomez-Arbones X., Boix J. Caspase 8/10 are not mediating apoptosis in neuroblastoma cells treated with CDK inhibitory drugs. Eur. J. Pharmacol 2005, 524:49-52.
17. Nechushtan A., Smith C.L., Hsu Y.T., Youle R.J. Conformation of the Bax C-terminus regulates subcellular location and cell death. EMBO J. 1999, 18:2330-2341.
18. Tanaka A., Youle R.J. A chemical inhibitor of DRP1 uncouples mitochondrial fission and apoptosis. Mol. Cell 2008, 29:409-410.
19. Knudson C.M., Tung K.S., Tourtellotte W.G., Brown G.A., Korsmeyer S.J. Bax-deficient mice with lymphoid hyperplasia and male germ cell death. Science 1995, 270:96-99.
20. Lewis J., Oyler G.A., Ueno K., Fannjiang Y.R., Chau B.N., Vornov J., et al. Inhibition of virus-induced neuronal apoptosis by Bax. Nat. Med 1999, 5:832-835.
21. Middleton G., Nunez G., Davies A.M. Bax promotes neuronal survival and antagonises the survival effects of neurotrophic factors. Development 1996, 122:695-701.
22. Oh J.H., O'Malley K.L., Krajewski S., Reed J.C., Oh Y.J. Bax accelerates staurosporine-induced but suppresses nigericin-induced neuronal cell death. Neuroreport 1997, 8:1851-1856.
23. Oh J.H., Choi W.S., Kim J.E., Seo J.W., O'Malley K.L., Oh Y.J. Overexpression of HA-Bax but not Bcl-2 or Bcl-XL attenuates 6-hydroxydopamine-induced neuronal apoptosis. Exp. Neurol 1998, 154:193-198.
24. Karbowski M., Norris K.L., Cleland M.M., Jeong S.-Y., Youle R.J. Role of Bax and Bak in mitochondrial morphogenesis. Nature 2006, 443:658-662.
25. Karbowski M., Lee Y.-J., Gaume B., Jeong S.-Y., Frank S., Nechushtan A., et al. Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis. J. Cell Biol 2002, 159:931-938.
26. Sheridan C., Delivani P., Cullen S.P., Martin S.J. Bax- or Bak-induced mitochondrial fission can be uncoupled from cytochrome C release. Mol. Cell 2008, 31:570-585.
27. Autret A., Martin S.J. Emerging role for members of the Bcl-2 family in mitochondrial morphogenesis. Mol. Cell 2009, 36:355-363.
28. Brooks C., Wei Q., Feng L., Dong G., Tao Y., Mei L., et al. Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins. Proc. Natl Acad. Sci. U.S.A. 2007, 104:11649-11654.
29. Delivani P., Adrain C., Taylor R.C., Duriez P.J., Martin S.J. Role for CED-9 and Egl-1 as regulators of mitochondrial fission and fusion dynamics. Mol. Cell 2006, 21:761-773.
30. Whelan R.S., Konstantinidis K., Wei A.-C., Chen Y., Reyna D.E., Jha S., et al. Bax regulates primary necrosis through mitochondrial dynamics. Proc. Natl Acad. Sci. U.S.A. 2012, 109:6566-6571.
31. Chonghaile T.N., Letai A. Mimicking the BH3 domain to kill cancer cells. Oncogene 2008, 27(Suppl. 1):S149-S157.