122(P-78) ユビキチン翻訳後修飾系を標的とする海洋生物由来の天然有機化合物の探索(ポスター発表の部)

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The ubiquitin-proteasome proteolytic pathway plays a major role in selective protein degradation and regulates various cellular events including cell growth and apoptosis. Ubiquitin attaches to a target protein prior to degradation. The polyubiquitin chains tagged to the target protein are recognized by the 26S proteasome, an intracellular high-molecular-mass protease subunit complex, and the protein portion is degraded by the 26S proteasome. The potential of specific proteasome inhibitors, which act as anticancer agents, is now under intensive investigation. Several proteasome inhibitors show anticancer activity against various cancer cells that are resistant to conventional chemotherapeutic agents: Especially, bortezomib (Velcade[○!R]), a proteasome inhibitor approved by FDA for multiple myeloma treatment, inhibits the NF-κB signaling, leading to apoptosis. We have already reported the isolation and structures of agosterol derivatives from a marine sponge Acanthodendrilla sp. as proteasome inhibitors. In this study, we report that girolline, an anticancer compound isolated from the marine sponge Axinella brevistyla, affects the step of recruitment of polyubiquitinated p53 to the proteasome and that a new compound, himeic acid A, isolated from a culture of the marine-derived fungus of the genus Aspergillus inhibits the activity of ubiquitin-activating enzyme E1. Thus, girolline is the first compound that affects the step of recruitment of polyubiquitinated proteins to the proteasome, while himeic acid A is the second compound that inhibits E1 enzyme activity.
天然有機化合物討論会の論文
2004-10-01

122(P-78) ユビキチン翻訳後修飾系を標的とする海洋生物由来の天然有機化合物の探索(ポスター発表の部)

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