|Budget Amount *help
¥3,400,000 (Direct Cost : ¥3,400,000)
Fiscal Year 1996 : ¥3,400,000 (Direct Cost : ¥3,400,000)
Degradative pathways of proteins and lipids are important as biological processes. However, knowledges about the processes are less than those for the sunthetic pathways of these biological compounds. In this study, we tried to establish the in vivo detection systems for reactions catalyzes by calpain and phosphoinositede-specific phospholipase C (PLC), which we had studeid by biochemical and molecular biological methods. We have developed the methods that detected expression of the activties of the enzymes and the results of the reaction catalyzed by the enzymes, using Drosophila early embryos and specific antibodies. First, we analyzed the localization of these enzymes during very early embryogenesis using anti-calpain and anti-PLC antibodies. Second, we prepared a specific antibody for the cleavage site that was generated by the hydrolytic reaction by calpain. Third, we have developed a system which made it possible to detect calpain, PLC,and their substrates during the embryogenesis. In addition, we have also analyzed the function of p122, which is a dual mediator between PLC and the cytoskeleton which is an activator of PLC.