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The interaction of selenoprotein F (SELENOF) with retinol dehydrogenase 11 (RDH11) implied a role of SELENOF in vitamin A metabolismстатья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Дата последнего поиска статьи во внешних источниках: 10 августа 2018 г.
- Авторы: Tian Jing, Liu Jiapan, Jieqiong Li, Zheng Jingxin, Chen Lifang, Wang Yujuan, Liu Qiong, Jiazuan Ni
- Журнал: Nutrition & metabolism
- Том: 15
- Номер: 7
- Год издания: 2018
- Издательство: BioMed Central
- Местоположение издательства: London
- Первая страница: 1
- Последняя страница: 9
- DOI: 10.1186/s12986-017-0235-x
- Аннотация: Background Selenoprotein F (SELENOF, was named as 15-kDa selenoprotein) has been reported to play important roles in oxidative stress, endoplasmic reticulum (ER) stress and carcinogenesis. However, the biological function of SELENOF is still unclear. Methods A yeast two-hybrid system was used to screen the interactive protein of SELENOF in a human fetal brain cDNA library. The interaction between SELENOF and interactive protein was validated by fluorescence resonance energy transfer (FRET), co-immunoprecipitation (co-IP) and pull-down assays. The production of retinol was detected by high performance liquid chromatograph (HPLC). Results Retinol dehydrogenase 11 (RDH11) was found to interact with SELENOF. RDH11 is an enzyme for the reduction of all-trans-retinaldehyde to all-trans-retinol (vitamin A). The production of retinol was decreased by SELENOF overexpression, resulting in more retinaldehyde. Conclusions SELENOF interacts with RDH11 and blocks its enzyme activity to reduce all-trans-retinaldehyde.
- Добавил в систему: Гладышев Вадим Николаевич