The proto-oncogene Bcl-2 and its role in regulating apoptosis (original) (raw)
References
Thompson, C.B. Apoptosis in the pathogenesis and treatment of disease. Science267, 1456–1462 (1995). ArticleCASPubMed Google Scholar
Kroemer, G., Petit, P.X. Zamzami, N. Vayssière, J.-L. & Mignotte, B. The biochemistry of apoptosis. FASEB J.9, 1277–1287 (1995). ArticleCASPubMed Google Scholar
Yang, E. & Korsmeyer, S.J. Molecular thanatopsis: A discourse on the Bcl-2 family and cell death. Blood88, 386–401 (1996). CASPubMed Google Scholar
Zoratti, M. & Szabd, I. The mitochondrial permeability transition. Biochim. Biophys. Ada – Rev. Biomembr.1241, 139–176 (1996). Article Google Scholar
Kroemer, G., Zamzami, N. & Susin, S.A. Mitochondrial control of apoptosis. Immunol. Today18, 44–51 (1997). ArticleCASPubMed Google Scholar
Carayon, P. et al. Involvement of peripheral benzodiazepine receptors in the protection of hematopoietic cells against oxygen radical species. Blood87, 3170–3178 (1996). CASPubMed Google Scholar
Tanaka, S., Saito, K. & Reed, J.C. Structure-function analysis of the Bcl-2 oncoprotein: Addition of a heterologous transmembrane domain to portions of the Bcl-2p protein restores function as a regulator of cell survival. J. Biol. Chem.268, 10920–10926 (1993). CASPubMed Google Scholar
Hockenbery, D.M., Oltvai, Z.N., Yin, X.-M., Milliman, C.L. & Korsmeyer, S.J. Bcl-2 functions in an antioxidant pathway to prevent apoptosis. Cell75, 241–251 (1993). ArticleCASPubMed Google Scholar
Wang, H.-C., Rapp, U.R. & Reed, J. C. Bcl-2 targets the protein kinase raf-1 to mitochondria. Cell87, 629–638 (1996). ArticleCASPubMed Google Scholar
Wu, D., Wallen, H.D. & Nu–ez, C. Interaction and regulation of subcellular localization of CED-4 by CED-9. Science275, 1126–1129 (1997). ArticleCASPubMed Google Scholar
Zhu, W. Bcl-2 mutants with restricted subcellular localization reveal spatially distinct pathways for apoptosis in different cell types. EMBO J.15, 4130–4141 (1996). ArticleCASPubMedPubMed Central Google Scholar
Zha, H. et al. Structure-function comparisons of the pro-apoptotic protein Bax in yeast and mammalian cells. Mol. Cell. Biol.16, 6494–6508 (1996). ArticleCASPubMedPubMed Central Google Scholar
Chinnaiyan, A.M., O'Rourke, K., Lane, B.R. & Dixit, V.M. Interaction of CED-4 with CED-3 and CED-9: A molecular frame for cell death. Science275, 1122–1126 (1997). ArticleCASPubMed Google Scholar
Cheng, E.H.-Y., Levine, B., Boise, L.H., Thompson, C.B. & Hardwick, J.M. Bax-independent inhibition of apoptosis by Bcl-XL . Nature, 379, 554–556 (1996). ArticleCASPubMed Google Scholar
Kane, D. J. et al. Bcl-2 inhibition of neural death: Decreased generation of reactive oxygen species. Science262, 1274–1277 (1993). ArticleCASPubMed Google Scholar
Zha, H., Aime-Sempre, C., Sato, T. & Reed, J.C. Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2. J. Biol. Chem.271, 7440–7444 (1996). ArticleCASPubMed Google Scholar
Hunter, J.J. & Parslow, T.G. A peptide sequence from Bax that converts Bcl-2 into an activator of apoptosis. J. Biol. Chem.271, 8521–8524 (1996). ArticleCASPubMed Google Scholar
Sattler, M. Structure of Bcl-x(L)-Bak peptide complex: Recognition between regulators of apoptosis. Science275, 983–986 (1997). ArticleCASPubMed Google Scholar
Boyd, J.M. et al. (1995) Bik, a novel death-inducing protein shares a distinct sequence motif with Bcl-2 family proteins and interacts with viral and cellular survival-promoting proteins. Oncogene11, 1921–1928. CASPubMed Google Scholar
Wang, K., Yin, X.M., Chao, D.T., Milliman, C.L. & Korsmeyer, S.J. BID: A novel BH3 domain-only death agonist. Genes & Development10, 2859–2869 (1996). ArticleCAS Google Scholar
Hanada, M., Aimesempe, C., Sato, T. & Reed, J.C. Structure-function analysis of Bcl-2 protein identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax J. Biol. Chem.270, 11962–11969 (1995). ArticleCASPubMed Google Scholar
Hunter, J.J., Bond, B.L. & Parslow, T.C. Functional dissection of the human Bcl2 protein: Sequence requirements for inhibition of apoptosis. Mol. Cell. Biol.16, 877–883 (1996). ArticleCASPubMedPubMed Central Google Scholar
Wang, H.G., Takayama, S., Rapp, U.R. & Reed, J.C. Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1. Proc. Natl. Acad. Sci. USA93, 7063–7068 (1996). ArticleCASPubMedPubMed Central Google Scholar
Shibasaki, F., Kondo, E., Akagi, T. & McKeon, F. Suppression of signalling through transcription factor NF-AT by interaction between calcineurin and Bcl-2. Nature386, 728–731 (1996). Article Google Scholar
Strack, P.R. et al. Apoptosis mediated by HIV protease is preceded by cleavage of Bcl-2. Proc. Natl. Acad. Sci. USA93, 9571–9576 (1996). ArticleCASPubMedPubMed Central Google Scholar
Haldar, S., Chintapalli, J. & Croce, CM. Taxol induces bcl-2 phosphorylation and death of prostate cancer cells. Cancer Research56, 1253–1255 (1996). CASPubMed Google Scholar
Uhlmann, E.J. et al. Deletion of a nonconserved region of Bcl-2 confers a novel gain of function: Suppression of apoptosis with concomitant cell proliferation. Cancer Res.56, 2506–2509 (1996). CASPubMed Google Scholar
Zha, J.P., Harada, H., Yang, E., Jockel, J. & Korsmeyer, S.J. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BGL-X(L). Cell87, 619–628 (1996). ArticleCASPubMed Google Scholar
Bardelli, A. et al. HGF receptor associates with the anti-apoptotic protein BAG-1 and prevents cell death. EMBO Journal15, 6205–6212 (1996). ArticleCASPubMedPubMed Central Google Scholar
Muchmore, S.W. et al. X-ray and NMR structure of human Bcl-XL, and inhibitor of programmed cell death. Nature381, 335–341 (1996). ArticleCASPubMed Google Scholar
Minn, A.J. et al. Bcl-XL form an ion channel in synthetic lipid membranes. Nature385, 353–357 (1997). ArticleCASPubMed Google Scholar
Lam, M. et al. Evidence that BCL-2 represses apoptosis by regulating endoplasmic reticulum-associated Ca2+ fluxes. Proc. Natl. Acad. Sci. USA85, 6569–6573 (1994). Article Google Scholar
Marin, M.C. et al. Apoptosis suppression by bcl-2 is correlated with the regulation of nuclear and cytosolic Ca2+. Oncogene12, 2259–2266 (1996). CASPubMed Google Scholar
Baffy, G., Miyashati, T., Williamson, J.R. & Reed, J.C. Apoptosis induced by withdrawal of interleukin-3 (IL-3) dependent hematopoietic cell line is associated with repartitioning of intracellular calcium and is blocked by enforced Bcl-2 oncogene production. J. Biol. Chem.268, 6511–6519 (1993). CASPubMed Google Scholar
Murphy, A.N., Bredesen, D.E., Cortopassi, G., Wang, E. & Fiskum, G. Bcl-2 potentiates the maximal calcium uptake capacity of neural cell mitochondria. Proc. Natl. Acad. Sci. USA93, 9893–9898 (1996). ArticleCASPubMedPubMed Central Google Scholar
Reynolds, J.E. & Eastman, A. Intracellular calcium stores are not required for Bcl-2-mediated protection from apoptosis. J. Biol. Chem.271, 27739–27743 (1996). ArticleCASPubMed Google Scholar
Chinnaiyan, A.M. et al. Molecular ordering of the cell death pathway — Bcl-2 and Bcl-X(L) function upstream of the CED-3-like apoptotic proteases. J. Biol. Chem.271, 4573–4576 (1996). ArticleCASPubMed Google Scholar
Zamzami, N. et al. Sequential reduction of mitochondrial transmembrane potential and generation of reactive oxygen species in early programmed cell death. J. Exp. Med.182, 367–377 (1995). ArticleCASPubMed Google Scholar
Liu, X., Kim, C.N., Yang, J., Jemmerson, R. & Wang, X. Induction of apoptic program in cell-free extracts: Requirement for dATP and cytochrome c. Cell86, 147–157 (1996). ArticleCASPubMed Google Scholar
Yang, J. et al. Prevention of apoptosis by Bcl-2: Release of cytochrome cfrom mitochondria blocked. Science275, 1129–1132 (1997). ArticleCASPubMed Google Scholar
Kluck, R.M., Bossy-Wetzel, E., Green, D.R. & Newmeyer, D.D. The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis. Science275,,1132–1136 (1997). ArticleCASPubMed Google Scholar
Zamzami, N. et al. Mitochondrial control of nuclear apoptosis. J. Exp. Med.183, 1533–1544 (1996). ArticleCASPubMed Google Scholar
Shimizu, S. et al. Bcl-2 blocks loss of mitochondrial membrane potential while ICE inhibitors act at a different step during inhibition of death induced by respiratory chain inhibitors. Oncogene13, 21–29. (1996). CASPubMed Google Scholar
Kantrow, S.P. & Piantadosi, C.A. Release of cytochrome cfrom liver mitochondria during permeability transition. Biochem. Biophys. Res. Commun.232, 669–671 (1997). ArticleCAS Google Scholar
Xiang, J., Chao, D.T. & Korsmeyer, S.J. Bax-induced cell death may not require interleukin 1 beta-converting enzyme-like proteases. Proc. Natl. Acad. Sci. USA93, 14559–14563 (1996). ArticleCASPubMedPubMed Central Google Scholar
Shimizu, S. et al. Prevention of hypoxia-induced cell death by Bcl-2 and Bcl-XL. Nature374, 811–813 (1995). ArticleCASPubMed Google Scholar
Newmeyer, D.D., Farschon, D.M. & Reed, C. Cell-free apoptosis in Xenopus egg extracts: Inhibition by Bcl-2 and requirement for an organelle fraction enriched in mitochondria. Cell79, 353––364 (1994). ArticleCASPubMed Google Scholar
Susin, S.A. et al. Bcl-2 inhibits the mitochondrial release of an apoptogenic protease. J. Exp. Med.84, 1331–1342 (1996). Article Google Scholar
Weil, M. et al. Constitutive expression of the machinery for programmed cell death. J. Cell Biol.133, 1053–1059 (1996). ArticleCASPubMed Google Scholar
Martinou, J.C. et al. Overexpression of Bcl-2 in transgenic mice protects neurons from naturally occurring cell death and experimental ischemia. Neuron13, 1017–1030 (1994). ArticleCASPubMed Google Scholar
Chen, D.F., Schneider, G.E., Martinou, J.-C. & Tonegawa, S. Bcl-2 promotes regeneration of severed axons in mammalian CNS. Nature385, 434–439 (1997). ArticleCASPubMed Google Scholar
Lawrence, M.S., Ho, D.Y., Sun, G.H., Steinberg, G.K. & Sapolsky, R.M. Over-expression of bcl-2 with herpes simplex virus vectors protects CNS neurons against neurological insults in vitro and in vivo. J. Neurosci.16, 486–496 (1996). ArticleCASPubMedPubMed Central Google Scholar
McCarthy, N.J., Whyte, M. K.B., Gilbert, C.S. & Evan, G.I. Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak. J. Cell Biol.136, 215–227 (1997). ArticleCASPubMedPubMed Central Google Scholar
Strobel, T., Swanson, L., Korsmeyer, S. & Cannistra, S.A. BAX enhances paclitaxel-induced apoptosis through a p53-independent pathway. Proc. Natl. Acad. Sci. USA93, 14094–14099 (1996). ArticleCASPubMedPubMed Central Google Scholar
Brady, H.J.M., Salomons, G.S., Bobeldijk, R.C. & Berns, A.J.M. T cells from bax alpha transgenic mice show accelerated apoptosis in response to stimuli but do not show restored DNA damage-induced cell death in the absence of p53. EMBO J.15, 1221–1230 (1996). ArticleCASPubMedPubMed Central Google Scholar
Huang, D.C.S., Cory, S. & Strasser, A. Bcl-2, Bcl-XL, and adenovirus protein E1B19kD are functionally equivalent in their ability to inhibit cell death. Oncogene14, 405–414 (1997). ArticleCASPubMed Google Scholar
Evtodienki, Y.V., Teplova, V.V., Sidashi, S.S., Ichas, F. & Mazat, J.-P. Microtubule-active drugs suppress the closure of the permeability transition pore in tumour mitochondria. FEBS Lett.393, 86–88 (1996). Article Google Scholar
Jacobson, M.D., Burne, J.F. & Raff, M.C. Programmed cell death and Bcl-2 protection in the absence of a nucleus. EMBO J.13, 1899–1910 (1994). ArticleCASPubMedPubMed Central Google Scholar
Tsao, N. & Lei, H.Y. Activation of the Na+/H+ antiporter, Na+/HCO3−/CO32− cotrans-porter, or CI−/HCO3− exchanger in spontaneous thymocyte apoptosis. J. Immunol.157, 1107–1116 (1996). CASPubMed Google Scholar
Martin, S.J. et al. Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: Inhibition by overexpression of Bcl-2 and Abl. J. Exp. Med.182, 1545–1556 (1995). ArticleCASPubMed Google Scholar
Ellerby, L.M. etal. Shift of the cellular oxidation-reduction potential in neural cells expressing bcl-2. J. Neurochem.67, 1259–1267 (1996). ArticleCASPubMed Google Scholar
Reynolds, J.E., Li, J.F., Craig, R.W. & Eastman, A. Bcl-2 and Mcl-1 expression in Chinese hamster ovary cells inhibits intracellular acidification and apoptosis induced by staurosporine. Exp. Cell Res.225, 430–436 (1996). ArticleCASPubMed Google Scholar
Hennet, T., Bertoni, G., Richter, C. & Peterhans, E. Expression of BCL-2 protein enhances the survival of mouse fibrosarcoid cells in tumor necrosis factor-mediated cytotoxicity. Cancer Res.53, 1456–1460 (1993). CASPubMed Google Scholar