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タイトル セミナー開催のお知らせ(Dr. Peter Nagy) *時間変更有(再
講演者 Dr. Peter Nagy
所属 ハンガリー国立がん研究所
開催日 2019-08-16 16:30
 非常にラッキーなことに、イオウ生物学研究の第一人者であるPeter Nagy博士(ハンガリー国立がん研究所)が福岡にお立ち寄りいただけることになり、16日(金)に薬学研究院グリーンファルマ研究所にてご講演いただける運びとなりました。最先端のレドックス・イオウ代謝研究に触れる絶好の機会ですので、皆様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~ (当初お知らせしていた時間より変更がありました)

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. 

ファイル 20190816.pdf