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ISSN: 2155-9899

Journal of Clinical & Cellular Immunology
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Research Article

Promotion of Caspase Activation by Caspase-9-mediated Feedback Amplification of Mitochondrial Damage

Alan D. Guerrero1, Ingo Schmitz2, Min Chen1 and Jin Wang1*
1Department of Pathology and Immunology, Baylor College of Medicine, Houston, Texas 77030, USA
2Institute for Molecular and Clinical Immunology, Otto-von-Guericke-University Magdeburg and Helmholtz Center for Infection Research, D-38124, Braunschweig, Germany
Corresponding Author : Jin Wang, Ph.D
Department of Immunology, Baylor College of Medicine
One Baylor Plaza, Room N920, Houston, Texas 77030, USA
Tel: 713-798-6193
Fax: 713-798-3033
E-mail: [email protected]
Received: June 15, 2012; Accepted: August 02, 2012; Published: August 09, 2012
Citation: Guerrero AD, Schmitz I, Chen M, Wang J (2012) Promotion of Caspase Activation by Caspase-9-mediated Feedback Amplification of Mitochondrial Damage. J Clin Cell Immunol 3:126. doi:10.4172/2155-9899.1000126
Copyright: © 2012 Guerrero AD, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Abstract

Mitochondrial disruption during apoptosis results in the activation of caspase-9 and a downstream caspase cascade. Triggering this caspase cascade leads to the cleavage of anti-apoptotic Bcl-2 family proteins, resulting in feedback amplification of mitochondrial disruption. However, whether such a feedback loop plays an important role in the promotion of caspase activation and execution of apoptosis has not been well established. We observed that mutated Bcl-2 or Bcl-xL that are resistant to cleavage by caspases inhibited caspase-9-induced caspase activation in human H9 T cells. The release of Smac after the activation of caspase-9 was also inhibited by cleavage-resistant Bcl-2 or Bcl-xL. Consistently, caspase-9-deficient cells were defective in the release of Smac after induction of apoptosis. Moreover, addition of a Smac mimetic overcame the inhibitory effects of cleavage-resistant Bcl-2/Bcl-xL, and restored caspase-9-mediated cell death. Our data suggest that caspase-9-induced feedback disruption of mitochondria plays an important role in promoting the activation of caspases, while a defect in this process can be overcome by promoting Smac functions.

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