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[Cancer Research 63, 541-546, January 15, 2003]
© 2003 American Association for Cancer Research

Tumor Biology

Bcl-2 and Bax Modulate Adenine Nucleotide Translocase Activity1

Anne-Sophie Belzacq, Helena L. A. Vieira, Florence Verrier, Grégoire Vandecasteele, Isabelle Cohen, Marie-Christine Prévost, Eric Larquet, Fabrizio Pariselli, Patrice X. Petit, Axel Kahn, Rosario Rizzuto, Catherine Brenner2,3 and Guido Kroemer2

CNRS-UMR6022, Université de Technologie de Compiègne, 60205 Compiègne, France [A-S. B., F. V., C. B.]; Centre National de la Recherche Scientifique, UMR8125, Institut Gustave Roussy, 94805 Villejuif, France [H. L. A. V., I. C., G. K.]; Department of Experimental and Diagnostic Medicine, Center for the Study of Inflammatory Diseases, University of Ferrara, Italy [G. V., R. R.]; Institut Pasteur, Plate-forme de Microscopie Electronique, 75724 Paris Cedex 15, France [M-C. P., E. L.]; and Department of Genetics, Development, and Molecular Pathology, INSERM/CNRS Institut Cochin, 75014 Paris, France [F. P., P. X. P., A. K.]

Bcl-2 is a prosurvival factor that reportedly prevents the nonspecific permeabilization of mitochondrial membranes, yet enhances specific ADP/ATP exchange by these organelles. Here, we show that Bcl-2 enhances the ADP/ATP exchange in proteoliposomes containing the purified adenine nucleotide translocase (ANT) in isolated mitochondria and mitoplasts, as well as in intact cells in which mitochondrial matrix ATP was monitored continuously using a specific luciferase-based assay system. Conversely, Bax, which displaces Bcl-2 from ANT in apoptotic cells, inhibits ADP/ATP exchange through a direct action on ANT. The Bax-mediated inhibition of ADP/ATP exchange can be separated from Bax-stimulated formation of nonspecific pores by ANT. Chemotherapy-induced apoptosis caused an inhibition of ANT activity, which preceded the loss of the mitochondrial transmembrane potential and could be prevented by overexpression of Bcl-2. These data are compatible with a model of mitochondrial apoptosis regulation in which ANT interacts with either Bax or Bcl-2, which both influence ANT function in opposing manners. Bcl-2 would maintain the translocase activity at high levels, whereas Bax would inhibit the translocase function of ANT.




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