J. Cell Biol., Volume 140, Number 6, March 23, 1998 1485-1495

The Caspase-3 Precursor Has a Cytosolic and Mitochondrial Distribution: Implications for Apoptotic Signaling

Marie Mancini,^* Donald W. Nicholson,^¶ Sophie Roy,^¶ Nancy A. Thornberry,^** Erin P. Peterson,^** Livia A. Casciola-Rosen,^§ and Antony Rosen^*§

^* Department of Medicine,  Department of Dermatology, ^§ Department of Cell Biology and Anatomy,  Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205; ^¶ Department of Biochemistry and Molecular Biology, Merck Frosst Center for Therapeutic Research, Pointe Claire-Dorval, Quebec, H9R 4P8, Canada; and ^** Department of Biochemistry, Merck Research Laboratories, Rahway, New Jersey 07065

Caspase-3-mediated proteolysis is a critical element of the apoptotic process. Recent studies have demonstrated a central role for mitochondrial proteins (e.g., Bcl-2 and cytochrome c) in the activation of caspase-3, by a process that involves interaction of several protein molecules. Using antibodies that specifically recognize the precursor form of caspase-3, we demonstrate that the caspase-3 proenzyme has a mitochondrial and cytosolic distribution in nonapoptotic cells. The mitochondrial caspase-3 precursor is contained in the intermembrane space. Delivery of a variety of apoptotic stimuli is accompanied by loss of mitochondrial caspase-3 precursor staining and appearance of caspase-3 proteolytic activity. We propose that the mitochondrial subpopulation of caspase-3 precursor molecules is coupled to a distinct subset of apoptotic signaling pathways that are Bcl-2 sensitive and that are transduced through multiple mitochondrion-specific protein interactions.

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