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Papers In Press, published online ahead of print February 6, 2002
J. Biol. Chem, 10.1074/jbc.M108029200
Submitted on August 20, 2001
Revised on February 6, 2002
Accepted on February 6, 2002

Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria

Yin Guo, Srinivasa M. Srinivasula, Anne Druilhe, Teresa Fernandes-Alnemri, and Emad S. Alnemri

Department of Microbiology and Immunology, Thomas Jefferson University, Philadelphia, PA 19107

Corresponding Author: E_Alnemri{at}lac.jci.tju.edu

Caspase-2 is one of the earliest identified caspases, but the mechanism of caspase-2-induced apoptosis remains unknown. We show here that caspase-2 engages the mitochondria-dependent apoptotic pathway by inducing the release of cytochrome c (Cyt c) and other mitochondrial apoptogenic factors into the cell cytoplasm. In support of these observations we found that Bcl-2 and Bcl-xL can block caspase-2- and CRADD/RAIDD-induced cell death. Unlike caspase-8, which can process all known caspase zymogens directly, caspase-2 is completely inactive towards other caspase zymogens. However, like caspase-8, physiological levels of purified caspase-2 can cleave cytosolic Bid protein, which in turn can trigger the release of Cyt c from isolated mitochondria. Interestingly, caspase-2 can also induce directly the release of Cyt c, AIF (apoptosis inducing factor) and Smac/Diablo from isolated mitochondria independent of Bid or other cytosolic factors. The caspase-2-released Cyt c is sufficient to activate the Apaf-caspase-9 apoptosome in vitro. Combined our data suggest that caspase-2 is a direct effector of the mitochondrial apoptotic pathway.


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