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Apoptosis is an active process that plays a key role in many physiological and pathological conditions. One of the most important organelles involved in apoptosis regulation is the mitochondrion. An increase in intracellular Ca 2+  is a general mechanism of toxicity in neurons which occurs in response to different noxious stimuli like excitotoxicity and ischemia producing apoptotic and necrotic cell death through mitochondria-dependent mechanisms. The Bcl-2 family of proteins modulate the release of pro-apoptotic factors from the mitochondrial intermembrane space during cell death induction by different stimuli. In this work, we have studied, using single-cell imaging and patch-clamp single channel recording, the mitochondrial mechanisms involved in the neuroprotective effect of Bcl-x L  on Ca 2+  overload-mediated cell death in human neuroblastoma SH-SY5Y cells. We have found that Bcl-x L  neuroprotective actions take place at mitochondria where this antiapoptotic protein delays both mitochondrial potential collapse and opening of the permeability transition pore by preventing Ca 2+ -mediated mitochondrial multiple conductance channel opening. Bcl-x L  neuroprotective actions were antagonized by the Bcl-x L  inhibitor ABT-737 and potentiated by the Ca 2+  chelator BAPTA-AM. As a consequence, this would prevent free radical production, mitochondrial membrane permeabilization, release from mitochondria of pro-apoptotic molecules, caspase activation and cellular death.

Bcl-xL Blocks a Mitochondrial Inner Membrane Channel and Prevents Ca2+ Overload-Mediated Cell Death