NDLI: Activation of distinct caspase-like proteases by Fas and reaper in Drosophila cells.

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Activation of distinct caspase-like proteases by Fas and reaper in Drosophila cells.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Yokokura, T. Nagata, S. Kondo, T.
Description	Author Affiliation: Kondo T ( Osaka Bioscience Institute, 6-2-4 Furuedai, Suita, Osaka 565, Japan.);
Abstract	The cytoplasmic region of Fas, a mammalian death factor receptor, shares a limited homology with reaper, an apoptosis-inducing protein in Drosophila. Expression of either the Fas cytoplasmic region (FasC) or of reaper in Drosophila cells caused cell death. The death process induced by FasC or reaper was inhibited by crmA or p35, suggesting that its death process is mediated by caspase-like proteases. Both Ac-YVAD aldehyde and Ac-DEVD aldehyde, specific inhibitors of caspase 1- and caspase 3-like proteases, respectively, inhibited the FasC-induced death of Drosophila cells. However, the cell death induced by reaper was inhibited by Ac-DEVD aldehyde, but not by Ac-YVAD aldehyde. A caspase 1-like protease activity that preferentially recognizes the YVAD sequence gradually increased in the cytosolic fraction of the FasC-activated cells, whereas the caspase 3-like protease activity recognizing the DEVD sequence was observed in the reaper-activated cells. Partial purification and biochemical characterization of the proteases indicated that there are at least three distinct caspase-like proteases in Drosophila cells, which are differentially activated by FasC and reaper. The conservation of the Fas-death signaling pathway in Drosophila cells, which is distinct from that for reaper, may indicate that cell death in Drosophila is controlled not only by the reaper suicide gene, but also by a Fas-like killer gene.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	22
Volume Number	94
Language	English
Publisher	National Academy of Sciences
Publisher Date	1997-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Antigens, CD95 Metabolism Apoptosis Caspases Cysteine Endopeptidases Drosophila Proteins Drosophila Peptides Animals Genetics Caspase 1 Caspase 3 Cysteine Proteinase Inhibitors Pharmacology Cytology Enzyme Activation Peptide Fragments Signal Transduction Comparative Study Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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