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Inhibition of Bax Channel-Forming Activity by Bcl-2
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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Metadata
- Authors
- Antonsson, B., Conti, F., Ciavatta, A., Montessuit, S., Lewis, S., Martinou, I., Bernasconi, L., Bernard, A., Mermod, J.-J., Mazzei, G., Maundrell, K., Gambale, F., Sadoul, R., & Martinou, J.-C.
- Venue
- Science
- Published
- 1997-07-18
- Volume
- 277
- Issue
- 5324
- Pages
- 370-372
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2161641464
- Cited by
- 1,028
- References
- 1
- FWCI
- 32.06
- Type
- journal article
- Language
- en
- Open access
- closed
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