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Papers In Press, published online ahead of print January 30, 2002
Dept. of Microbiology and Immunology, Thomas Jefferson University, Philadelphia, PA 19107
Corresponding Author: E_Alnemri{at}lac.jci.tju.edu
CARD domains are protein-protein interaction modules found extensively in proteins that play important roles in apoptosis, NF-
J. Biol. Chem, 10.1074/jbc.M107811200
Submitted on August 14, 2001
Revised on January 25, 2002
Accepted on January 30, 2002
CARD-8 protein, a new CARD family member that regulates caspase-1 activation and apoptosis
B activation and cytokine regulation. In this study we identified a novel human protein, CARD-8, which contains a C terminal CARD domain with high similarity to CARD domain of caspase-1/ICE. We demonstrate that CARD-8 interacts physically with caspase-1 and negatively regulates caspase-1-dependent IL-1
generation in the THP-1 monocytic cell line. CARD-8 binds also to ICEBERG and Pseudo-ICE, two other recently identified proteins, which bind to the CARD domain of caspase-1 and negatively regulate its activity. RT-PCR analysis revealed that CARD-8 is expressed mainly in monocytes, placenta, lymph nodes and spleen. This pattern of expression is consistent with caspase-1 expression in the same cells and tissues. CARD-8 was also found to negatively regulate NF-B activation by TNF-
stimulation and by ectopically expressed RICK, suggesting that this protein could control cell survival. Consistent with these results stable expression of CARD-8 in U937 or THP-1 cells sensitizes these cells to differentiation-induced apoptosis. Overexpression of CARD-8 can also induce apoptosis in transfected cells. The results suggest that CARD-8 represents a new signaling molecule involved in the regulation of caspase-1 and NF-B activation.
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