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|Title:||DECAY, a novel Drosophila caspase related to mammalian Caspase-3 and Caspase-7|
|Citation:||Journal of Biological Chemistry, 1999; 274(43):30778-30783|
|Publisher:||AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC|
|Loretta Dorstyn, Stuart H. Read, Leonie M. Quinn, Helena Richardson, and Sharad Kumar|
|Abstract:||Caspases are key effectors of programmed cell death in metazoans. In Drosophila, four caspases have been described so far. Here we describe the identification and characterization of the fifth Drosophila caspase, DECAY. DECAY shares a high degree of homology with the members of the mammalian caspase-3 subfamily, particularly caspase-3 and caspase-7. DECAY lacks a long prodomain and thus appears to be a class II effector caspase. Ectopic expression of DECAY in cultured cells induces apoptosis. Recombinant DECAY exhibited substrate specificity similar to the mammalian caspase-3 subfamily. Low levels of decay mRNA are ubiquitously expressed in Drosophila embryos during early stages of development but its expression becomes somewhat spatially restricted in some tissues. During oogenesis decay mRNA was detected in egg chambers of all stages consistent with a role for DECAY in apoptosis of nurse cells. Relatively high levels of decay mRNA are expressed in larval salivary glands and midgut, two tissues which undergo histolysis during larval/pupal metamorphosis, suggesting that DECAY may play a role in developmentally programmed cell death in Drosophila.|
|Keywords:||Digestive System; Salivary Glands; Animals; Mammals; Drosophila; Caspases; Drosophila Proteins; Recombinant Proteins; RNA, Messenger; Sequence Alignment; Evolution, Molecular; Transcription, Genetic; Gene Expression Regulation, Developmental; Gene Expression Regulation, Enzymologic; Amino Acid Sequence; Sequence Homology, Amino Acid; Larva; Molecular Sequence Data; Caspase 3; Caspase 7|
|Appears in Collections:||Genetics publications|
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