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M200401200v1
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Papers In Press, published online ahead of print March 27, 2002
J. Biol. Chem, 10.1074/jbc.M200401200
Submitted on January 14, 2002
Revised on March 27, 2002
Accepted on March 27, 2002

Activation of caspase-9 is required for UV-induced apoptosis of human keratinocytes

Leonid A. Sitailo, Shalini S. Tibudan, and Mitchell F. Denning

Department of Pathology, Loyola University Medical Center, Maywood, IL 60153

Corresponding Author: mdennin{at}lumc.edu

UV radiation from the sun activates both the membrane death receptor and the intrinsic or mitochondrial apoptotic signaling pathways in epidermal keratinocytes, triggering apoptosis and affording protection against skin cancer formation. We have investigated the involvement of caspase-9 in the UV death effector pathway in human keratinocytes, as this is the initiating caspase in the mitochondrial pathway required for UV-induced apoptosis in some, but not all, cell types. UV radiation triggered activation of caspase-3, caspase-9, and caspase-8 with similar kinetics, although the rank order of activation was caspase-3>caspase-9>caspase-8. Inhibition of caspase-9 with either the peptide inhibitor z-LEHD-FMK, or expression of a catalytically inactive caspase-9 by retroviral transduction, protected normal keratinocytes from UV induced apoptosis. HaCaT keratinocytes harboring mutant p53 alleles were also protected from UV-induced apoptosis by the dominant/negative caspase-9. The dominant/negative caspase-9 blocked UV-induced activation of caspase-3, caspase-9, and caspase-8, and protected from the loss of mitochondrial membrane potential. In contrast, the dominant/negative caspase-9 did not protect from anti-Fas-induced apoptosis, or caspase activation. These results identify caspase-9 as the critical upstream caspase initiating apoptosis by UV radiation in human keratinocytes, the relevant cell type for this important environmental carcinogen.


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