52(P-21) 高等植物におけるシグナル伝達機構-GTP結合能を有する新規トリプシンインヒビターの単離とその機能(ポスター発表の部)

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Signal transduction in a cell is one of the most important roles for the resistance and/or the response to stimulation from outside of the cells. It is well known that GTP binding proteins (G-protein) plays particularly important role in signal transduction pathway. Recently, we found that some kinds of monoterpenes became a cause of apoptotic cell death. This phenomenon can be explained as self-defense against the stress from outside of the cells. We now have isolated a novel trypsin inhibitor (p20) having GTP-binding activity and clarified its characterization and physiological activities. (1) Purification and characterization of p20 A 20-kDa protein (p20) which has GTP-binding activity was isolated from soybean cultured cells by column chromatography. The molecular weight of p20 was determined to be 19,900±200 by TOF-MS. Total amino acid sequences was determined by cDNA cloning of p20, which was constructed by 182 amino acid residues. The amino acid sequence of p20 was homologous to the known Kunitz-type trypsin inhibitors (45-50% homology). (2) Biochemical activity of p20 Both of recombinant p20 and commercially available trypsin inhibitor showed trypsin inhibitory activity, but their inhibition mechanism were different. Using ESI-MS technique, it was found that 1 molecular of p20 binds 1 molecular of GTP, and its binding constant is about 10^5. (3) Physiological activity of p20 Northern blot analysis of mRNA from Glycine Max was examined. It was found that expression level of p20 mRNA under the stress of geraniol treatment was decreased at 6h after treatment. Therefore, it was suggested that there is a new signal transductioin pathway through protease inhibitor.
天然有機化合物討論会の論文
2000-10-01

52(P-21) 高等植物におけるシグナル伝達機構-GTP結合能を有する新規トリプシンインヒビターの単離とその機能(ポスター発表の部)

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