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Characterization of Bc1-2, Bc1-xL, and Bax Pore Formation and Their Role in Apoptosis Regulation

Characterization of Bc1-2, Bc1-xL, and Bax Pore Formation and Their Role in Apoptosis Regulation

Authors :
BURNHAM INST LA JOLLA CA
Stenner-Liewen, Frank
Schendel, Sharon
Reed, John C.
BURNHAM INST LA JOLLA CA
Stenner-Liewen, Frank
Schendel, Sharon
Reed, John C.
Source :
DTIC
Publication Year :
2002

Abstract

Bcl-2-family proteins are central regulators of apoptosis and their expression often becomes deregulated in breast cancers. The biochemical mechanisms by which Bcl-2 family proteins control cell life and death decisions are unknown. Recent evidence that certain Bcl-2 family proteins bear structural similarity to the pore-forming domains of bacterial toxin proteins suggest a function for these apoptosis regulators as ion-channels. Using eletrophysiological techniques, we demonstrated that the cytoprotective protein Bcl-2 and the cell death proteins Bax and Bid possess intrinsic ion-channel activity. A variety of structure-function studies demonstrated that channel formation by the Bcl-2 family proteins is important for some but not all of their bioactivities. This finding suggests novel ways to screen for drug inhibitors of Bcl-2, so that tumor cell resistance to cell death can be overcome and sensitivity to anticancer drugs restored

Details

Database :
OAIster
Journal :
DTIC
Notes :
text/html, English
Publication Type :
Electronic Resource
Accession number :
edsoai.ocn834241272
Document Type :
Electronic Resource