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

      Science (New York, N.Y.)
      Animals, Apoptosis, Cell Membrane Permeability, Cells, Cultured, Erythrocytes, cytology, Fluoresceins, metabolism, Hemolysis, Humans, Hydrogen-Ion Concentration, Ion Channels, physiology, Lipid Bilayers, Liposomes, Membrane Potentials, Neurons, Patch-Clamp Techniques, Proto-Oncogene Proteins, pharmacology, Proto-Oncogene Proteins c-bcl-2, antagonists & inhibitors, Sheep, Sympathetic Nervous System, bcl-2-Associated X Protein

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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.

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