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Science 18 July 1997:
Vol. 277. no. 5324, pp. 370 - 372
DOI: 10.1126/science.277.5324.370
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Reports

Inhibition of Bax Channel-Forming Activity by Bcl-2

Bruno Antonsson, *dagger Franco Conti, *dagger AnnaMaria Ciavatta, Sylvie Montessuit, Shareta Lewis, Isabelle Martinou, Lilia Bernasconi, Alain Bernard, Jean-Jacques Mermod, Gonzalo Mazzei, Kinsey Maundrell, Franco Gambale, Rémy Sadoul, * Jean-Claude Martinou dagger

Proteins of the Bcl-2 family are intracellular membrane-associated proteins that regulate programmed cell death (apoptosis) either positively or negatively by as yet unknown mechanisms. Bax, a pro-apoptotic member of the Bcl-2 family, was shown to form channels in lipid membranes. Bax triggered the release of liposome-encapsulated carboxyfluorescein at both neutral and acidic pH. At physiological pH, release could be blocked by Bcl-2. Bcl-2, in contrast, triggered carboxyfluorescein release at acidic pH only. In planar lipid bilayers, Bax formed pH- and voltage-dependent ion-conducting channels. Thus, the pro-apoptotic effects of Bax may be elicited through an intrinsic pore-forming activity that can be antagonized by Bcl-2.

B. Antonsson, S. Montessuit, S. Lewis, I. Martinou, L. Bernasconi, A. Bernard, J.-J. Mermod, G. Mazzei, K. Maundrell, R. Sadoul, J.-C. Martinou, Geneva Biomedical Research Institute, Glaxo Wellcome R&D S.A., 1288 Plan les Ouates, Geneva, Switzerland.
F. Conti, A. M. Ciavatta, F. Gambale, Istituto di Cibernetica e Biofisica, 16149 Genoa, Italy.
*   These authors contributed equally to this study.

dagger    To whom correspondence should be addressed. E-mail: bea6063{at}ggr.co.uk (B.A.), conti{at}barolo.icb.ge.cnr.it (F.C.), and jcm26619{at}ggr.co.uk (J.-C.M.)

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S. L. Schendel, R. Azimov, A. Godzik, B. L. Kagan, and J. C. Reed (1999)
J. Biol. Chem. 274, 21932-21936
   Abstract »    Full Text »    PDF »
NH2-terminal BH4 Domain of Bcl-2 Is Functional for Heterodimerization with Bax and Inhibition of Apoptosis.
M. Hirotani, Y. Zhang, N. Fujita, M. Naito, and T. Tsuruo (1999)
J. Biol. Chem. 274, 20415-20420
   Abstract »    Full Text »    PDF »
Enhanced Apoptotic Response to Photodynamic Therapy after bcl-2 Transfection.
H.-R. Choi Kim, Y. Luo, G. Li, and D. Kessel (1999)
Cancer Res. 59, 3429-3432
   Abstract »    Full Text »    PDF »
Life and Death in Otolaryngology: Mechanisms of Apoptosis and Its Role in the Pathology and Treatment of Disease.
S. P. Mostafapour, D. M. Hockenbery, and E. W Rubel (1999)
Arch Otolaryngol Head Neck Surg 125, 729-737
   Abstract »    Full Text »    PDF »
Btf, a Novel Death-Promoting Transcriptional Repressor That Interacts with Bcl-2-Related Proteins.
G. M. Kasof, L. Goyal, and E. White (1999)
Mol. Cell. Biol. 19, 4390-4404
   Abstract »    Full Text »    PDF »
Biochemical and Genetic Control of Apoptosis: Relevance to Normal Hematopoiesis and Hematological Malignancies.
R. G. Wickremasinghe and A. V. Hoffbrand (1999)
Blood 93, 3587-3600
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Activation of a Ca2+-permeable cation channel by two different inducers of apoptosis in a human prostatic cancer cell line.
A. A Gutierrez, J. M. Arias, L. Garcia, J. Mas-Oliva, and A. Guerrero-Hernandez (1999)
J. Physiol. 517, 95-107
   Abstract »    Full Text »    PDF »
Insulin-Like Growth Factor-1 Attenuates the Detrimental Impact of Nonocclusive Coronary Artery Constriction on the Heart.
B. Li, M. Setoguchi, X. Wang, A. M. Andreoli, A. Leri, A. Malhotra, J. Kajstura, and P. Anversa (1999)
Circ. Res. 84, 1007-1019
   Abstract »    Full Text »    PDF »
Bax, but not Bcl-xL, decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentrations.
G. Basanez, A. Nechushtan, O. Drozhinin, A. Chanturiya, E. Choe, S. Tutt, K. A. Wood, Y.-T. Hsu, J. Zimmerberg, and R. J. Youle (1999)
PNAS 96, 5492-5497
   Abstract »    Full Text »    PDF »
Release of caspase-9 from mitochondria during neuronal apoptosis and cerebral ischemia.
S. Krajewski, M. Krajewska, L. M. Ellerby, K. Welsh, Z. Xie, Q. L. Deveraux, G. S. Salvesen, D. E. Bredesen, R. E. Rosenthal, G. Fiskum, et al. (1999)
PNAS 96, 5752-5757
   Abstract »    Full Text »    PDF »
Bak BH3 Peptides Antagonize Bcl-xL Function and Induce Apoptosis through Cytochrome c-independent Activation of Caspases.
E. P. Holinger, T. Chittenden, and R. J. Lutz (1999)
J. Biol. Chem. 274, 13298-13304
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Impairment of the Proapoptotic Activity of Bax by Missense Mutations Found in Gastrointestinal Cancers.
J. Gil, H. Yamamoto, J. M. Zapata, J. C. Reed, and M. Perucho (1999)
Cancer Res. 59, 2034-2037
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Nitric Oxide-Induced Apoptosis in Human Leukemic Lines Requires Mitochondrial Lipid Degradation and Cytochrome C Release.
A. Ushmorov, F. Ratter, V. Lehmann, W. Droge, V. Schirrmacher, and V. Umansky (1999)
Blood 93, 2342-2352
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The Cell Death-promoting Gene DP5, Which Interacts with the BCL2 Family, Is Induced during Neuronal Apoptosis Following Exposure to Amyloid beta  Protein.
K. Imaizumi, T. Morihara, Y. Mori, T. Katayama, M. Tsuda, T. Furuyama, A. Wanaka, M. Takeda, and M. Tohyama (1999)
J. Biol. Chem. 274, 7975-7981
   Abstract »    Full Text »    PDF »
The Release of Cytochrome c from Mitochondria during Apoptosis of NGF-deprived Sympathetic Neurons Is a Reversible Event.
I. Martinou, S. Desagher, R. Eskes, B. Antonsson, E. Andre, S. Fakan, and J.-C. Martinou (1999)
J. Cell Biol. 144, 883-889
   Abstract »    Full Text »    PDF »


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