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,¶
*
Research Center and
Nephrology Service, Notre-Dame Hospital, Center hospitalier universitaire de l’Université de Montréal, University of Montreal, Montreal, Canada;
Montreal General Hospital, Montreal, Canada;
Institute of Molecular Virology, St. Louis University Medical Center, St. Louis, MO 63110; and
¶ Department of Surgery, McGill University, Montreal, Canada
The mechanism underlying apoptosis induced by proteasome inhibition in leukemic Jurkat and Namalwa cells was investigated in this study. The proteasome inhibitor lactacystin differentially regulated the protein levels of proapoptotic Bcl-2 family members and Bik was accumulated at the mitochondria. Bik overexpression sufficed to induce apoptosis in these cells. Detailed examination along the respiration chain showed that lactacystin compromised a step after complex III, and exogenous cytochrome c could overcome this compromise. Probably as a result, the succinate-stimulated generation of mitochondrial membrane potential was significantly diminished. Bcl-xL interacted with Bik in the cells, and Bcl-xL overexpression prevented cytochrome c leakage out of the mitochondria, corrected the mitochondrial membrane potential defect, and protected the cells from apoptosis. These results show that proteasomes can modulate apoptosis of lymphocytes by affecting the half-life of Bcl-2 family members, Bik being one of them.
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