A new caspase-8 isoform caspase-8s increased sensitivity to apoptosis in Jurkat cells.

Zhifang Xu, Kejing Tang, Min Wang, Qing Rao, Bolin Liu, Jianxiang Wang

Journal: Journal of biomedicine & biotechnology 2010;2009():930462

PMID: 20150972

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Abstract

Caspase-8 is a key initiator of death receptor-induced apoptosis. Here we report a novel short isoform of caspase-8 (caspase-8s), which encodes the first (Death Effector Domain) DED and part of the second DED, missing the C-terminal caspase domain. In vivo binding assays showed that transfected caspase-8s bound to (Fas-associated death domain protein) FADD, the adaptor protein in (death-induced signal complex) DISC. To investigate the potential effects of caspase-8s on cell apoptosis, Jurkat cells were stably transfected with caspase-8s. Overexpression of caspase-8s increased sensitivity to the apoptotic stimuli, Fas-agonistic antibody CH11. These results suggest that caspase-8s may act as a promoter of apoptosis through binding to FADD and is involved in the regulation of apoptosis. In addition, the results also indicate that the first DED was an important structure mediating combination between caspase-8 and FADD.

Address: State Key Laboratory of Experimental Hematology, Institute of Hematology and Blood Disease Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Tianjin, China.

DOI: 10.1155/2009/930462

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https://assays.cancer.gov/CPTAC-369

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https://antibodies.cancer.gov/detail/CPTC-FAS-1

MeSH Terms: Amino Acid Sequence, Antibodies, Apoptosis, Base Sequence, Blotting, Western, Caspase 8, Clone Cells, DNA Fragmentation, DNA, Complementary, Electrophoresis, Polyacrylamide Gel, Fas-Associated Death Domain Protein, Gene Expression Regulation, Humans, Isoenzymes, Jurkat Cells, Membrane Potential, Mitochondrial, Molecular Sequence Data, Protein Binding, RNA, Messenger, Transfection, fas Receptor