| Budget Amount *help |
¥6,200,000 (Direct Cost: ¥6,200,000)
Fiscal Year 1993: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1992: ¥4,600,000 (Direct Cost: ¥4,600,000)
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| Research Abstract |
Calpain is an intracellular cysteine protease, possibly involved in Ca^<2+>-mediated signalling and activated by enhancement of intracellular Ca^<2+> concentration.
First, I have identified two Drosophila genes encoding calpains. Their mRNA expression was studied by Northern blotting analysis and in situ hybridization experiment, which revealed that the two Drosophila calpains belong to conventional calpain family showing ubiquitous distribution.
Next, I prepared a specific antibody against one type of the calpains. Using this antibody, cellular and subcellular localization of the calpain molecule was investigated in the early embryo. The results showed that calpain is localized with actin-related cytoskeletal structure in the very early embryo before cellularization, and in the precleavage furrows just before cellularization. These observations indicate that the Drosophila calpain is involved in univeral cellular functions, especially in the reorganization of actin-related cytoskeleton.
I also studied mode of interaction between calpain and calpastatin, an endogenous inhibitor specific for calpain, by biochemical methods, which provided useful informations for further molecular studies on in vivo functions of the Drosophila calpain-calpastatin system.
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