Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/9138
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Type: Journal article
Title: DRONC, an ecdysone-inducible Drosophila caspase
Author: Dorstyn, L.
Colussi, P.
Quinn, L.
Richardson, H.
Kumar, S.
Citation: Proceedings of the National Academy of Sciences of the United States of America, 1999; 96(36251):4307-4312
Publisher: NATL ACAD SCIENCES
Issue Date: 1999
ISSN: 0027-8424
1091-6490
Statement of
Responsibility: 
Loretta Dorstyn, Paul A. Colussi, Leonie M. Quinn, Helena Richardson and Sharad Kumar
Abstract: Caspases play an essential role in the execution of programmed cell death in metazoans. Although 14 caspases are known in mammals, only a few have been described in other organisms. Here we describe the identification and characterization of a Drosophila caspase, DRONC, that contains an amino terminal caspase recruitment domain. Ectopic expression of DRONC in cultured cells resulted in apoptosis, which was inhibited by the caspase inhibitors p35 and MIHA. DRONC exhibited a substrate specificity similar to mammalian caspase-2. DRONC is ubiquitously expressed in Drosophila embryos during early stages of development. In late third instar larvae, dronc mRNA is dramatically up-regulated in salivary glands and midgut before histolysis of these tissues. Exposure of salivary glands and midgut isolated from second instar larvae to ecdysone resulted in a massive increase in dronc mRNA levels. These results suggest that DRONC is an effector of steroid-mediated apoptosis during insect metamorphosis.
Keywords: 3T3 Cells; Embryo, Nonmammalian; Animals; Mammals; Mice; Drosophila; Ecdysone; Caspases; Drosophila Proteins; Recombinant Proteins; Transfection; Sequence Alignment; Transcription, Genetic; Gene Expression Regulation, Developmental; Gene Expression Regulation, Enzymologic; Enzyme Induction; Amino Acid Sequence; Sequence Homology, Amino Acid; Substrate Specificity; Larva; Pupa; Expressed Sequence Tags; Molecular Sequence Data; Caspase 2
Description: Copyright © 1999, The National Academy of Sciences
RMID: 0030004760
DOI: 10.1073/pnas.96.8.4307
Published version: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=16328&tool=pmcentrez&rendertype=abstract
Appears in Collections:Medicine publications

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