論文

査読有り
2018年2月1日

Isolation of activating factors of serotonin N-acetyltransferase from rice peptides

Journal of Functional Foods
  • Chie Moritani
  • ,
  • Kayoko Kawakami
  • ,
  • Akiko Fujita
  • ,
  • Koji Kawakami
  • ,
  • Hiroshi Shimoda
  • ,
  • Tadashi Hatanaka
  • ,
  • Seiji Tsuboi

41
開始ページ
148
終了ページ
154
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1016/j.jff.2017.12.051
出版者・発行元
Elsevier Ltd

Serotonin N-acetyltransferase (AA-NAT), which converts serotonin to N-acetylserotonin, is a rate-limiting enzyme for melatonin synthesis. We previously reported that intracellular redox conditions regulate AA-NAT activity by switching an intramolecular disulfide bridge in a glutathione (GSH)-dependent manner
thus, increased GSH levels can activate AA-NAT. Here, we found that commercially available rice peptides increased intracellular GSH levels and attenuated H2O2-induced inactivation of AA-NAT activity in COS7 cells expressing AA-NAT constitutively. Purification of the peptides using a Sep-Pak C18 cartridge and three rounds of reversed-phase HPLC, followed by sequence analysis by mass spectrometry, led to the identification of three peptides. Two of these peptides (Pep2, VVTFGPSGLTTEVK
Pep3, YQQQFQQFLPEGQSQSQK) prevented inactivation of AA-NAT activity by H2O2. Only Pep3 increased intracellular GSH levels and prevented the decrease in the reduced/oxidised GSH ratio induced by H2O2. These results suggest that Pep3 activates AA-NAT by increasing intracellular GSH levels, which switches the intramolecular disulfide bond of AA-NAT.

Web of Science ® 被引用回数 : 2

リンク情報
DOI
https://doi.org/10.1016/j.jff.2017.12.051
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000428360700018&DestApp=WOS_CPL

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