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How much H 2 O 2 is produced by recombinant D-Amino acid oxidase in mammalian cells?статья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 21 мая 2019 г.
- Авторы: Matlashov M.E., Belousov V.V., Enikolopov G.
- Журнал: Antioxidants and Redox Signaling
- Том: 20
- Номер: 7
- Год издания: 2014
- Издательство: Mary Ann Liebert Inc.
- Местоположение издательства: United States
- Первая страница: 1039
- Последняя страница: 1044
- DOI: 10.1089/ars.2013.5618
- Аннотация: Yeast D-amino acid oxidase (DAO) can serve as a genetically encoded producer of reactive oxygen species (ROS) in redox signaling studies. However, dynamics of hydrogen peroxide production and its sensitivity to externally added D-alanine (D-Ala) in cells have not been determined. Here we show that DAO, fused to a genetically encoded H 2 O 2 indicator HyPer, can be used for controlled production of ROS in living eukaryotic cells. We found a clear heterogeneity in ROS production dynamics between individual cells. Moreover, different cell lines demonstrated distinct sensitivity to added D-Ala. Finally, by comparing signals generated by the HyPer-DAO fusion protein versus coexpressed HyPer and DAO proteins, we show that the fusion system is more sensitive to hydrogen peroxide production. Our results show the utility of the HyPer-DAO genetically encoded system for redox signaling studies and suggest that H 2 O 2 produced by DAO in the cytoplasm acts locally in close proximity to the enzyme. Antioxid. Redox Signal. 20, 1039-1044. © Mary Ann Liebert, Inc.
- Добавил в систему: Ениколопов Григорий Николаевич