The interaction of selenoprotein F (SELENOF) with retinol dehydrogenase 11 (RDH11) implied a role of SELENOF in vitamin A metabolism

Jing Tian,Qiong Liu,Jingxin Zheng,Lifang Chen,Jieqiong Li,Jiapan Liu,Jiazuan Ni,Yujuan Wang

doi:10.1186/s12986-017-0235-x

Jing Tian, Qiong Liu + Show 6 more

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https://doi.org/10.1186/s12986-017-0235-x

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Abstract

BackgroundSelenoprotein 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.MethodsA 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).ResultsRetinol 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.ConclusionsSELENOF interacts with RDH11 and blocks its enzyme activity to reduce all-trans-retinaldehyde.

Highlights

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
Retinol dehydrogenase 11 (RDH11) is involved in the retinal pigment epithelium (RPE) during the retinoid visual cycle, it is found in different tissues such as brain, testis and prostate [25]
The production of retinol converted from retinaldehyde was inhibited by selenoprotein F (SELENOF) implied its role, WHICH revealed the possible role of SELENOF in the vitamin A metabolism

Summary

Introduction

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. Selenium (Se) is a necessary trace element for human health. It primarily exerts its function through selenoproteins in which Se is present in the form of selenocysteine (Sec), which is encoded by UGA, traditionally read as a stop codon in the coding region. SELENOF, initially named as 15-kDa selenoprotein (Sep15) is one of the 25 genes in humans encoding for selenoproteins [1]. It is conserved from worms to human beings, whereas the genes in C. elegans, B. malayiand Drosophila encode homologous proteins that contain cysteine in place of selenocysteine [2]. The NMR structure of fruit fly SELENOF shows that the protein contains a thioredoxin-like motif. Tunicamycin (an N-linked glycosylation inhibitor and is commonly used to induce ER stress experimentally) upregulates the SELENOF protein level, whereas dithiothreitol

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