Article Abstract:
A protein interaction cloning technique helps clone the Bcl-2-binding protein BAG-1-encoding cDNAs. There is no sequence homology between BAG-1 and Bcl-2 family proteins. Coexpression of Bcl-2 and BAG-1 confers enhanced protection from cell death activated by anti-Fas antibody, saturosporine and cytolytic T cells in the human lymphoid cell line Jurkat. Cell survival in 3T3 fibroblasts after an apoptotic stimulus increases due to BAG transfection, indicating that the new anti-cell death gene bag-1 regulates some of the apoptosis activation pathways, along with Bcl-2.
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Article Abstract:
Cytochrome c is important for phosphorylation in mitochondria where it helps with production of ATP. However, one of the required factors from cytosol that induces proteolytic processing and activation of the cell death protease, caspase-3, was found to be cytochrome c. Further research showed that cytochrome c is quickly released from mitochondria into the cytosol. Vander Heiden and colleagues suggest that the release of cytochrome c is due to mitochondrial swelling and rupture of outer membranes.
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Article Abstract:
This review discusses the mechanistic aspects of BIR proteins that exhibit zinc binding fold called the BIR domain in the regulation of chromosome segregation and cytokinesis. Research reveals that these BIR domain proteins also function as apoptosis suppressors and are called survivins.
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