BAD Induces Apoptosis in Cells Over-Expressing Bcl-2 or Bcl-xL without Loss of Mitochondrial Membrane Potential

References

• Pepper Bentley C. P., Hoy T. Regulation of clinical chemoresistance by bcl-2 and bax oncoproteins in B-cell chronic lymphocytic leukaemia. British Journal of Haematology 1996; 95: 513–517
   PubMed Web of Science ®Google Scholar
• Sangflet Osterborg O., Grander A., Anderbring D., Ost E., Mellstedt A., Einhorn H. S. Response to interferon therapy in patients with multiple myeloma correlates with expression of Bcl-2 oncoprotein. International Journal of Cancer 1995; 63: 190–192
   PubMed Web of Science ®Google Scholar
• Kitada Takayama S., De Kiel S., Tanaka K. S, Reed J C. Reversal of chemoresistance of lymphoma cells by antisense-mediated reduction of bcl-2 gene expression. Antisense Research and Development 1994; 4: 71–79
   PubMedGoogle Scholar
• Piche Grim A., Rancouit J., Gomez C., NavarroReed J., Curiel C. JDT. Modulation of Bcl-2 protein levels by intracellular anti-Bcl-2 single-chain antibody increases drug-induced cytotoxicity in the breast cancer cell line MCF-7. Cancer Research 1998; 58: 2134–2140
   PubMed Web of Science ®Google Scholar
• Miyashita T, Reed J. Bcl-2 oncoprotein blocks chemotherapy-induced apoptosis in a human leukemia cell line. Blood 1993; 91: 151–157
   Google Scholar
• Tang Willingham C., Reed C. M, Miyashita C. J, Ray T., Ponnnathpur S., Huang V., Mahoney Y., Bullock E. M, Bhalla G. K. High levels of p26BCL-2 oncoprotein retard taxol-induced apoptosis in human pre-B leukemia cells. Leukemia 1994; 8: 1960–1969
   PubMed Web of Science ®Google Scholar
• Maung Z, Maclean T., Reid R. F, Pearson M. M, Proctor D. A, Hamilton J. S, Hall J. PAG. The relationship between bcl-2 expression and response to chemotherapy in acute leukaemia. British Journal of Haematology 1994; 88: 105–109
   PubMed Web of Science ®Google Scholar
• Campos Rouault L., Sabido P. J, Pascale O., Roub O., Vasselon N., Archimbaud C., Magoud E., Gutotat P. JD. High expression of bcl-2 protein in acute myeloid leukemia cells is associated with poor response to chemotherapy. Blood 1993; 81: 3091–3096
   PubMed Web of Science ®Google Scholar
• Ottilie Diaz S., Home J., Chang W., Van J., Wilson W., Chang G., Weeks S., Fritz S., Oltersdoff C. LT. Dimerization properties of human, BAD. Journal of Biological Chemistry 1997; 272: 30866–30872
   PubMed Web of Science ®Google Scholar
• Yang Zha E., Jockel J., Boise J., Thompson H. L, Korsmeyer B. CS. Bad, a heterodimeric partner for Bcl-xL and Bcl-2 displaces Bax and promotes cell death. Cell 1995; 80: 285–291
   PubMed Web of Science ®Google Scholar
• Zha Harada J., Yang H., Jockel E., Korsmeyer J. S. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not Bcl-xL. Cell 1996; 87: 619–628
   PubMed Web of Science ®Google Scholar
• Elangovan B, Chinnadurai G. Functional dissection of the pro-apoptotic protein Bik. Journal of Biological Chemistry 1997; 272: 24494–24498
   PubMed Web of Science ®Google Scholar
• Hegde Srinivasula R., Ahmad S., Fernandes M., Alnemri T., Alnemri E S. Blk, a BH3-containin mouse protein that interacts with Bcl-2 and Bcl-xL, is a potent death agonist. Journal of Biological Chemistry 1998; 7783–7786
   PubMed Web of Science ®Google Scholar
• O'Connor Stasser L., O'Reilly A., Hausmann L., Adams G., Corry M. J, Huang S. DC. Bim: a novel member of the Bcl-2 family that promotes apoptosis. EMBO J 1998; 17: 384–395
   PubMed Web of Science ®Google Scholar
• Wang Yin K., Chao X., Milliman D., Korsmeyer L. CSJ. BID: a novel BH3 domain-only death agonist. Genes and Development 1996; 10: 2859–2869
   PubMed Web of Science ®Google Scholar
• Inohara Ding N., Chen L., Nunez S. G. Harakiri, a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival-promoting proteins Bcl-2 and Bcl-xL. EMBO Journal 1997; 16: 1686–1694
   PubMed Web of Science ®Google Scholar
• Kelekar Chang A., Harlan B., Fesik J., Thompson W. SCB. Bad is a BH3 domain-containing protein that forms an inactivating dimer with Bcl-xL. Molecular and Cellular Biology 1997; 17: 7040–7046
   PubMed Web of Science ®Google Scholar
• Zha Harada J., Konstantin H., Jockel O., Waksman J., Korsmeyer G. S. BH3 domain of BAD is required for heterodimerization with Bcl-xL and pro-apoptotic activity. Journal of Biological Chemistry 1997; 272: 24101–24104
   PubMed Web of Science ®Google Scholar
• Desjardins L., Mac Manus J. An adherent cell model to study different stages of apoptosis. Experiment Cell Research 1995; 216: 380–3
   PubMed Web of Science ®Google Scholar
• Sheng-Tanner Bump X., Hedley A. EDW. An oxidative stress mediated death pathway in irradiated human leukemia cells mapped using multilaser flow cytometry. Radiation Research 1998; 150: 636–647
   PubMed Web of Science ®Google Scholar
• Hakem Hakem R., Duncan A., Henderson S. G, Woo T. J, Soengas M., Elia S. M, Luis A., , Pompa Kagi J., Khoo D., Potter W., Yoshida J., Kaufman R., Lowe A. S, Penninger W. S, Mak M. JTW, et al. Differential requirement for caspase-9 in apoptotic pathways in vivo. Cell 1998; 94: 339–352
   PubMed Web of Science ®Google Scholar
• Raaphorst Mao G., Yang J., Niknafs R., Shiraz B., Yazdi H. F, Rippstein M. H, Ng P. C. Evaluation of apoptosis in four human tumour cell lines with differing sensitivities to cisplatin. Anticancer Research 1998; 18: 2945–2951
   PubMed Web of Science ®Google Scholar
• Chow A., Zhang R. Glutamine reduces heat shock-induced cell death in rat intestinal epithelial cells. Journal of Nutrition 1998; 128: 1296–1301
   PubMed Web of Science ®Google Scholar
• Khosla Oursler S., Schroeder M., Eberhardt M. NJ. Transforming growth factor-beta 1 induces growth inhibition of a human medullary thyroid carcinoma cell line despite an increase in steady state c-myc messenger ribonucleic acid levels. Endocrinology 1994; 135: 1887–1893
   PubMed Web of Science ®Google Scholar
• Soldatenkov Prasad V., Notario S., Dritschilo V. A. Radiation-induced apoptosis of Swing's sarcoma cells: DNA fragmentation and proteolysis of poly(ADP-ribose) polymerase. Cancer Research 1995; 55: 4240–4242
   PubMed Web of Science ®Google Scholar
• Benito Suva A., Grillot M., Nunez D., Fernandez G., Luna J L. Apoptosis induced by erthroid differentiation of human leukemia cell lines is inhibited by Bcl-xL. Blood 1996; 87: 3837–3843
   PubMed Web of Science ®Google Scholar
• Gommerman J L, Berger S A. Protection from apoptosis by Steel factor but not interleukin-3 is reversed through blockage of calcium influx. Blood 1998; 91: 1891–1900
   PubMed Web of Science ®Google Scholar
• Jurgensmeierr J, Xie M., Devaraux Z., Ellerby Q., Bredesen L., Reed D. J. Bax directly induces release of cytochrome c from isolated mitochondria. Proceedings of the National Academy of Science, USA 1998; 9: 4997–5002
   Web of Science ®Google Scholar
• Shimizu Narita S. M., Tsujimoto Y. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel, VDAC. Nature 1999; 6735: 483–487
   Google Scholar
• Wang Pathan H., Ethell N., Krajewski M. I, Yamaguchi S., Shibasaki Y., Mc Keon F., Bobo F., Franke T., Reed T. JC. Ca2+-induced apoptosis through calcineurin dephosphorylation of, BAD. Science 1999; 284: 339–343
   PubMed Web of Science ®Google Scholar
• Shimizu Tsujimoto S. Y. Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity. Proceedings of the National Academy of Science, USA 2000; 97: 577–582
   PubMed Web of Science ®Google Scholar
• Naita Shimizu M., Ito S., Chittenden T., Lutz T., Matsuda J. R, Tsujimoto H. Y. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proceedings of the National Academy of Science, USA 1998; 95: 14681–14686
   PubMed Web of Science ®Google Scholar
• Brenner Cadiou C., Vieira H., Zamzami A.H.L., Marzo N., Xie I., Leber Z., Andrews B., Duclohier D., Reed H., Kroemer C. JG. Bcl-2 and Bax regulate the channel activity of the mitochondrial adenine nucleotide translocator. Oncogene 2000; 19: 329–336
   PubMed Web of Science ®Google Scholar
• Li Y, Li Z., Pinto J. C, Pardee V. AAB. Release of mitochondrial cytochrome c in both apoptosis and necrosis induced by β-Lapachone in human carcinoma cells. Molecular Medicine 1999; 5: 232–239
   PubMed Web of Science ®Google Scholar
• Pastorino J, Tafani G., Rothman M., Marcineviciute J. R, Hoek A., Farber B. JJL. Functional consequences of the sustained or transient activation by Bax of the mitochondrial permeability transition pore. The Journal of Biological Chemistry 1999; 44: 31734–31739
   Web of Science ®Google Scholar
• Antonsson Conti B., Ciavatta P., Montessuit M. A, Lewis S., Martinou S., Bernasconi I., Bernard L., Mermod A., Mazzei J. J, Maundrell G., Gambale K., Sadoul F., Martinou R. JC. Inhibition of Bax channel-forming activity by Bcl-2. Science 1997; 277: 370–372
   PubMed Web of Science ®Google Scholar
• Eskes Antonsson R., Osen B., SandMontessuit A., Richter S., Sadoul C., Mazzei R., Nichols G., Martinou A. JC. Bax-induced cytochrome c release from mitochondria is independent of the permeability transition pore but highly dependent on Mg2+ ions. The Journal of Cell Biology 1998; 143: 217–224
   PubMed Web of Science ®Google Scholar
• Basanez Nechushtan G., Drozhinin A., Chanturiya O., Choe A., Titt E., Wood S., Hsu A. K, Zimmerberg T. Y, Youle J. RJ. Bax, but not Bcl-xL, decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentration. Proceedings of the National Academy of Science, USA 1999; 96: 5492–5497
   PubMed Web of Science ®Google Scholar
• Wang J, Liu L., Zhang D., Shan J. Z, Han S., Srinivasula X., Croce M. S, Alnemri M. C, Huang S. EZ. Structure based discovery of an organic compound that binds Bcl-2 protein and induces apoptosis of tumor cells. Proceedings of the National Academy of Science, USA. Proceedings of the National Academy of Science, USA 2000; 97: 7124–7129
   PubMed Web of Science ®Google Scholar
• Hollinger E, Chittenden P., Lutz T. RJ. Bak BH3 peptides antagonize Bcl-xL function and induce apoptosis through cytochrome c-independent activation of caspases. The Journal of Biological Chemistry 1999; 274: 13298–13304
   PubMed Web of Science ®Google Scholar
• Wang J, Zhang L., Choksi J. Z, Shan S., Lu S., Croce X., Alnermri M. C, Korngold S. E, Huang R. Z. Cell permeable Bcl-2 binding peptides: a chemical approach to apoptosis induction in tumor cells. Cancer Research 2000; 60: 1498–1502
   PubMed Web of Science ®Google Scholar