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(9) Bcl-xL ALTERS THE GATING PROPERTIES OF VDAC CHANNELS ISOLATED FROM RAT LIVER MITOCHONDRIA X-X. Li, M.G. Vander Heiden,
C.B. Thompson and M. Colombini
Published work clearly demonstrates that Bcl-xL is a protein that inhibits mitochondria-mediated apoptosis. However, the mechanism of action is controversial. Bcl-xL forms channels in membranes but there is general agreement that these channels do not directly influence the efflux of cytochrome c. Strong evidence has been published indicating that Bcl-xL can act by changing the properties of VDAC. Some results indicate that Bcl-xL favors VDAC closure preventing cytochrome c efflux through a VDAC-Bax complex. Others point out that it is VDAC closure that eventually leads to cytochrome c release and that Bcl-xL may work by favoring the opening of VDAC. We present clear and compelling results showing how the single and multi-channel properties of rat liver VDAC are changed by the addition of pure untruncated Bcl-xL. These findings provide strong support for one of the hypotheses.
For further information contact...Carmen Mannella: carmen@wadsworth.org |
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