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Inhibition of Bax Channel-Forming Activity by Bcl-2

Science  18 Jul 1997:
Vol. 277, Issue 5324, pp. 370-372
DOI: 10.1126/science.277.5324.370

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Abstract

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.

  • * These authors contributed equally to this study.

  • 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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