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Characterization and Expression of Chicken Selenoprotein U

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Abstract

Selenoprotein U (SelU) may regulate a myriad of biological processes through its redox function. In chicks, neither the nucleotide sequence nor the amino acid sequence is known. The main objectives of this study were to clone and characterize the chicken Selu gene and investigate Selu messenger RNA (mRNA) and protein expression in chicken tissues. The coding sequence (CDS) of Selu contained 387 bases with a typical mammalian selenocysteine insertion sequence (SECIS) located in the 3′-untranslated region. The deduced amino acid sequence of chicken SelU contains 224 amino acids with UAA as the stop codon. Like all SelU genes identified in different species, chicken SelU contains one well-conserved selenocysteine (Sec) at the 85th position encoded by the UGA codon. The SECIS element was with the conserved denosine (--AAA--) rather than the motif cytidine (--CC--) motif. Moreover, the expression pattern of Selu mRNA in muscle, liver, kidney, heart, spleen, lung, testis, and brain was analyzed with real-time quantitative PCR in young male chickens fed a Se-deficient corn-soybean meal basal diet supplemented with 0.0 and 0.3 mg Se/kg in the form of sodium selenite. We found that the abundance of Selu mRNA in muscle, liver, kidney, heart, spleen, and lung was downregulated (P < 0.05) by Se deficiency. However, it was not affected by dietary Se concentrations in testis and brain. Furthermore, protein abundance of SelU in these seven tissues was consistent with the mRNA abundance. Hence, we suggest that Selu might play an important role in the biochemical function of Se in birds.

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Abbreviations

BD:

Basal diet

EST:

Expressed sequence tag

PCR:

Polymerase chain reaction

Q-PCR:

Real-time quantitative PCR

Se:

Selenium

SECIS:

Selenocysteine insertion sequence

SelU:

Selenoprotein U

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Acknowledgments

This research was supported in part by Chinese Natural Science Foundation: the Major International (Regional) Joint Research Program of China (No. 31320103920) and the Project of Creating Excellent of the Capital (Beijing) Food Safety Technology (No. Z141100002614011).

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Authors and Affiliations

  1. Beijing Laboratory of Food Quality and Safety, and Key Laboratory of Functional Dairy, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, 100083, China

    Yun-Yun Jiang, Jia-Qiang Huang, Gao-Chao Lin, Hui-Yuan Guo, Fa-Zheng Ren & Hao Zhang

  2. Beijing Higher Institution Engineering Research Center of Animal Product, Beijing, 100083, China

    Yun-Yun Jiang, Jia-Qiang Huang, Gao-Chao Lin & Hao Zhang

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  1. Yun-Yun Jiang
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  2. Jia-Qiang Huang
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  3. Gao-Chao Lin
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  4. Hui-Yuan Guo
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  5. Fa-Zheng Ren
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  6. Hao Zhang
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Correspondence to Hao Zhang.

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Jiang, YY., Huang, JQ., Lin, GC. et al. Characterization and Expression of Chicken Selenoprotein U. Biol Trace Elem Res 166, 216–224 (2015). https://doi.org/10.1007/s12011-015-0257-z

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  • DOI: https://doi.org/10.1007/s12011-015-0257-z

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