2019年08月10日
レドックス／活性イオウ
このたび、レドックス／活性イオウ研究の第⼀線でご活躍されているPeter Nagy教授が九⼤⾺出キャンパスを訪問されることになりました。せっかくの機会ですので、セミナー御講演していただく ことに致しました。これまでのレドックス概念を越えたシステインパースルフィドの多彩な機能とその制御について最先端 の話題をご提供いただけるとのことですので、ぜひ奮ってご参加ください。
開催⽇時：２０１９年８⽉１６⽇（⾦）午後4時30分~
開催場所：薬学研究院グリーンファルマ研究所４階会議室
使⽤⾔語：英語
講演要旨:
Thioredoxin system-mediated persulfidation of Cys residues controls protein function and protects them from oxidative stress
Péter Nagy
Department of Molecular Immunology and Toxicology, National Institute of Oncology, Hungary
In the field of Redox Biology, protein cysteine persulfidation (P-Cys-SSH) and polysulfidation (P-Cys-SSxH) is gaining increasing attention as an important regulatory element of protein functions. Initially it was proposed to be mainly the result of hydrogen sulfide’s biological actions, but recently the Akaike laboratory demonstrated that these modifications can be produced enzymatically via pathways that does not require H2S.
We demonstrated that protein Cys per/polysulfidation is highly regulated via the NADPH-dependent reducing machineries, the thioredoxin and glutathione systems.
We have shown that persulfidation has a regulatory role on a number of protein functions and recently we also obtained evidence that these modifications have important protein protecting functions in cells and in vivo. In cellular systems a substantial fraction of important thiol proteins (such as peroxiredoxins, PTP1B, PTEN, KEAP1 or Hsp90) are present in their persulfidated state, which we propose is a preemptive mechanism to prevent them from overoxidation during oxidative stress. We demonstrated that protection is due to formation of perthio-sulfenic, sulfinic and sulfonic acid derivatives (Cys-SSO1-3H), which can be reduced back by the thioredoxin system to the corresponding functional native thiol forms when the stress is over.
連絡先:
薬学研究院 創薬育薬研究施設統括室 ⻄⽥基宏先生（内6556）
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ランチタイム、歓送迎会のお弁当のご予約、受付中。ご予約日は翌日以降でございます。
開催⽇時：２０１９年８⽉１６⽇（⾦）午後4時30分~
開催場所：薬学研究院グリーンファルマ研究所４階会議室
使⽤⾔語：英語
講演要旨:
Thioredoxin system-mediated persulfidation of Cys residues controls protein function and protects them from oxidative stress
Péter Nagy
Department of Molecular Immunology and Toxicology, National Institute of Oncology, Hungary
In the field of Redox Biology, protein cysteine persulfidation (P-Cys-SSH) and polysulfidation (P-Cys-SSxH) is gaining increasing attention as an important regulatory element of protein functions. Initially it was proposed to be mainly the result of hydrogen sulfide’s biological actions, but recently the Akaike laboratory demonstrated that these modifications can be produced enzymatically via pathways that does not require H2S.
We demonstrated that protein Cys per/polysulfidation is highly regulated via the NADPH-dependent reducing machineries, the thioredoxin and glutathione systems.
We have shown that persulfidation has a regulatory role on a number of protein functions and recently we also obtained evidence that these modifications have important protein protecting functions in cells and in vivo. In cellular systems a substantial fraction of important thiol proteins (such as peroxiredoxins, PTP1B, PTEN, KEAP1 or Hsp90) are present in their persulfidated state, which we propose is a preemptive mechanism to prevent them from overoxidation during oxidative stress. We demonstrated that protection is due to formation of perthio-sulfenic, sulfinic and sulfonic acid derivatives (Cys-SSO1-3H), which can be reduced back by the thioredoxin system to the corresponding functional native thiol forms when the stress is over.
連絡先:
薬学研究院 創薬育薬研究施設統括室 ⻄⽥基宏先生（内6556）
博多はつ花のボランティア修理担当が社長のブログをお借りして、発言させていただきました。
接待用高級お弁当の博多 はつ花 の商品はちょっと高級な、無農薬、無人工甘味料、無添加物を食材に使っています。配送には、冷凍車を用いております。お渡し後は、早めにお召し上がりのほど、お願い申し上げます。
ランチタイム、歓送迎会のお弁当のご予約、受付中。ご予約日は翌日以降でございます。
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