The interaction of selenoprotein F (SELENOF) with retinol dehydrogenase 11 (RDH11) implied a role of SELENOF in vitamin A metabolism
- Nutr Metab (Lond). 2018 Jan 22;15:7. doi: 10.1186/s12986-017-0235-x.
- 1. 1College of Life Sciences and Oceanography, Shenzhen Key Laboratory of Marine Bioresources and Eco-environmental Science, Shenzhen University, Shenzhen, 518060 China.
- 2. 2College of Life Sciences and Oceanography, Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen, 518060 China.
- 3. 3College of Life Sciences and Oceanography, Shenzhen Engineering Laboratory for Marine Algal Biotechnology, Shenzhen University, Shenzhen, 518060 China.
- 4. 4Department of Neurology, Shenzhen University 1st Affiliated Hospital, Shenzhen Second People's Hospital, Sungang West Road, Shenzhen, China.
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.