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Science. 1997 Jul 18;277(5324):370-2.

Inhibition of Bax channel-forming activity by Bcl-2.

Author information

1
Geneva Biomedical Research Institute, Glaxo Wellcome R&D S. A., 1288 Plan les Ouates, Geneva, Switzerland. beau6063@ggr.co.uk

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.

PMID:
9219694
[Indexed for MEDLINE]
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