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Selenium Deficiency Mainly Influences the Gene Expressions of Antioxidative Selenoproteins in Chicken Muscles

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Abstract

Dietary selenium (Se) deficiency induces muscular dystrophy in chicken, but the molecular mechanism remains unclear. The aim of the present study was to investigate the effect of dietary Se deficiency on the expressions of 25 selenoproteins. One-day-old broiler chickens were fed either an Se deficiency diet (0.033 mg Se/kg; produced in the Se-deficient area of Heilongjiang, China) or a diet supplemented with Se (as sodium selenite) at 0.2 mg/kg for 55 days. Then, the mRNA levels of 25 selenoproteins in chicken muscles were examined, and the principal component was further analyzed. The results showed that antioxidative selenoproteins especially Gpxs and Sepw1 were highly and extensively expressed than other types of selenoproteins in chicken muscles. In 25 selenoproteins, Gpxs, Txnrd2, Txnrd 3, Dio1, Dio 3, Selk, Sels, Sepw1, Selh, Sep15, Selu, Selpb, Sepp1, Selo, Sepx1, and SPS2 were downregulated (P < 0.05), and other selenoproteins were not influenced (P > 0.05). Se deficiency decreased the expressions of 19 selenoproteins (P < 0.05), 11 of which were antioxidative selenoproteins. And, principal component analysis (PCA) further indicated that antioxidative selenoproteins, especially Gpx3, Gpx4, and Sepw1, may play crucial roles in chicken muscles. However, compared with these antioxidative selenoproteins, some other lower expressed selenoproteins (Dio1, Selu, Selpb, Sepp1) were excessively decreased (more than 60 %, P < 0.05) by Se deficiency. Thus, it may save the limited Se levels and be beneficial to remain the level of some crucial selenoproteins. These results suggested that Se deficiency mainly influenced the expressions of antioxidative selenoproteins in chicken muscles. And, antioxidative selenoproteins especially Gpxs and Sepw1 may play a crucial role in chicken muscles. Thus, it helps us focus on some specific selenoproteins when studying the role of Se in chicken muscles.

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References

  1. Rederstorff M, Krol A, Lescure A (2006) Understanding the importance of selenium and selenoproteins in muscle function. Cell Mol Life Sci 63:52–59

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  2. Yao HD, Wu Q, Zhang ZW et al (2013) Gene expression of endoplasmic reticulum resident selenoproteins correlates with apoptosis in various muscles of se-deficient chicks. J Nutr 143:613–619

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  3. Huang JQ, Li DL, Zhao H et al (2011) The selenium deficiency disease exudative diathesis in chicks is associated with downregulation of seven common selenoprotein genes in liver and muscle. J Nutr 141:1605–1610

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  4. Xu S-W, Yao H-D, Zhang J et al (2012) The oxidative damage and disbalance of calcium homeostasis in brain of chicken induced by selenium deficiency. Biol Trace Elem Res 151:225–233

    Article  PubMed  Google Scholar 

  5. Wu Q, Yao HD, Tan SR, et al. (2014) Possible Correlation of Selenoprotein W with Inflammation Factors in Chicken Skeletal Muscles. Biol Trace Elem Res. doi:10.1007/s12011-014-0092-7

  6. Ghazi Harsini S, Habibiyan M, Moeini MM, Abdolmohammadi AR (2012) Effects of dietary selenium, vitamin E, and their combination on growth, serum metabolites, and antioxidant defense system in skeletal muscle of broilers under heat stress. Biol Trace Elem Res 148:322–330

    Article  CAS  PubMed  Google Scholar 

  7. Kieliszek M, Blazejak S (2013) Selenium: significance, and outlook for supplementation. Nutrition 29:713–718

    Article  CAS  PubMed  Google Scholar 

  8. Mariotti M, Ridge PG, Zhang Y et al (2012) Composition and evolution of the vertebrate and mammalian selenoproteomes. PLoS One 7:e33066

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  9. Bellinger FP, Raman AV, Reeves MA, Berry MJ (2009) Regulation and function of selenoproteins in human disease. Biochem J 422:11–22

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  10. Dikiy A, Novoselov SV, Fomenko DE et al (2007) SelT, SelW, SelH, and Rdx12 genomics and molecular insights into the functions. Biochemistry 46:6871–6882

    Article  CAS  PubMed  Google Scholar 

  11. Pappas AC, Zoidis E, Surai PF, Zervas G (2008) Selenoproteins and maternal nutrition. Comp Biochem Physiol B Biochem Mol Biol 151:361–372

    Article  CAS  PubMed  Google Scholar 

  12. Sunde RA, Raines AM, Barnes KM, Evenson JK (2009) Selenium status highly regulates selenoprotein mRNA levels for only a subset of the selenoproteins in the selenoproteome. Biosci Rep 29:329–338

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  13. Lescure A, Rederstorff M, Krol A, Guicheney P, Allamand V (2009) Selenoprotein function and muscle disease. Biochim Biophys Acta 1790:1569–1574

    Article  CAS  PubMed  Google Scholar 

  14. Hawkes WC, Alkan Z (2011) Delayed cell cycle progression from SEPW1 depletion is p53- and p21-dependent in MCF-7 breast cancer cells. Biochem Biophys Res Commun 413:36–40

    Article  CAS  PubMed  Google Scholar 

  15. Hawkes WC, Alkan Z (2012) Delayed cell cycle progression in selenoprotein W-depleted cells is regulated by a mitogen-activated protein kinase kinase 4-p38/c-Jun NH2-terminal kinase-p53 pathway. J Biol Chem 287:27371–27379

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  16. Hawkes WC, Printsev I, Alkan Z (2012) Selenoprotein W depletion induces a p53- and p21-dependent delay in cell cycle progression in RWPE-1 prostate epithelial cells. J Cell Biochem 113:61–69

    Article  CAS  PubMed  Google Scholar 

  17. Martinez A, Santiago JL, Varade J et al (2008) Polymorphisms in the selenoprotein S gene: lack of association with autoimmune inflammatory diseases. BMC Genomics 9:329

    Article  PubMed Central  PubMed  Google Scholar 

  18. Du S, Zhou J, Jia Y, Huang K (2010) SelK is a novel ER stress-regulated protein and protects HepG2 cells from ER stress agent-induced apoptosis. Arch Biochem Biophys 502:137–143

    Article  CAS  PubMed  Google Scholar 

  19. Du S, Liu H, Huang K (2010) Influence of SelS gene silence on beta-mercaptoethanol-mediated endoplasmic reticulum stress and cell apoptosis in HepG2 cells. Biochim Biophys Acta 1800:511–517

    Article  CAS  PubMed  Google Scholar 

  20. Verma S, Hoffmann FW, Kumar M et al (2011) Selenoprotein K knockout mice exhibit deficient calcium flux in immune cells and impaired immune responses. J Immunol 186:2127–2137

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  21. Holben DH, Smith AM (1999) The diverse role of selenium within selenoproteins. J Am Diet Assoc 99:836–843

    Article  CAS  PubMed  Google Scholar 

  22. Liu Y, Zhao H, Zhang Q et al (2012) Prolonged dietary selenium deficiency or excess does not globally affect selenoprotein gene expression and/or protein production in various tissues of pigs. J Nutr 142:1410–1416

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  23. Ruan H, Zhang Z, Wu Q et al (2012) Selenium regulates gene expression of selenoprotein W in chicken skeletal muscle system. Biol Trace Elem Res 145:59–65

    Article  CAS  PubMed  Google Scholar 

  24. Peirson SN, Butler JN, Foster RG (2003) Experimental validation of novel and conventional approaches to quantitative real-time PCR data analysis. Nucleic Acids Res 31:e73

    Article  PubMed Central  PubMed  Google Scholar 

  25. Livak KJ, Schmittgen TD (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25:402–408

    Article  CAS  PubMed  Google Scholar 

  26. Messaoudi I, Banni M, Said L, Said K, Kerkeni A (2010) Involvement of selenoprotein P and GPx4 gene expression in cadmium-induced testicular pathophysiology in rat. Chem Biol Interact 188:94–101

    Article  CAS  PubMed  Google Scholar 

  27. Zhang J, Li J, Zhang Z et al (2012) Ubiquitous expression of selenoprotein N transcripts in chicken tissues and early developmental expression pattern in skeletal muscles. Biol Trace Elem Res 146:187–191

    Article  CAS  PubMed  Google Scholar 

  28. Gao X, Xing H, Li S et al (2012) Selenium regulates gene expression of selenoprotein W in chicken gastrointestinal tract. Biol Trace Elem Res 145:181–188

    Article  CAS  PubMed  Google Scholar 

  29. Sun B, Wang R, Li J, Jiang Z, Xu S (2011) Dietary selenium affects selenoprotein W gene expression in the liver of chicken. Biol Trace Elem Res 143:1516–1523

    Article  CAS  PubMed  Google Scholar 

  30. Wang R, Sun B, Zhang Z, Li S, Xu S (2011) Dietary selenium influences pancreatic tissue levels of selenoprotein W in chickens. J Inorg Biochem 105:1156–1160

    Article  CAS  PubMed  Google Scholar 

  31. Yu D, Li JL, Zhang JL, Gao XJ, Xu S (2011) Effects of dietary selenium on selenoprotein W gene expression in the chicken immune organs. Biol Trace Elem Res 144:678–687

    Article  CAS  PubMed  Google Scholar 

  32. Li JL, Li HX, Li S et al (2012) Effects of Selenoprotein W gene expression by selenium involves regulation of mRNA stability in chicken embryos neurons. Biometals 25:459–468

    Article  CAS  PubMed  Google Scholar 

  33. Liu CP, Fu J, Lin SL, Wang XS, Li S (2014) Effects of dietary selenium deficiency on mRNA levels of twenty-one selenoprotein genes in the liver of layer chicken. Biol Trace Elem Res 159:192–198

    Article  CAS  PubMed  Google Scholar 

  34. Lin SL, Wang CW, Tan SR, et al. (2014) Selenium Deficiency Inhibits the Conversion of Thyroidal Thyroxine (T) to Triiodothyronine (T ) in Chicken Thyroids. Biol Trace Elem Res. doi:10.1007/s12011-014-0083-8

  35. Liang Y, Lin SL, Wang CW et al (2014) Effect of selenium on selenoprotein expression in the adipose tissue of chickens. Biol Trace Elem Res 160:41–48

    Article  CAS  PubMed  Google Scholar 

  36. Reeves MA, Bellinger FP, Berry MJ (2010) The Neuroprotective Functions of Selenoprotein M and its Role in Cytosolic Calcium Regulation. Antioxidants & redox signaling 12(7):809–818

  37. Wang X-L, Yang C-P, Xu K, Qin O-J (2010) Selenoprotein W depletion in vitro might indicate that its main function is not as an antioxidative enzyme. Biochem Mosc 75:201–207

    Article  CAS  Google Scholar 

  38. Yao HD, Wu Q, Zhang ZW et al (2013) Selenoprotein W serves as an antioxidant in chicken myoblasts. Biochim Biophys Acta 1830:3112–3120

    Article  CAS  PubMed  Google Scholar 

  39. Nishida H, Ichikawa H, Konishi T (2007) Shengmai-san enhances antioxidant potential in C2C12 myoblasts through the induction of intracellular glutathione peroxidase. J Pharmacol Sci 105:342–352

    Article  CAS  PubMed  Google Scholar 

  40. Franco AA, Odom RS, Rando TA (1999) Regulation of antioxidant enzyme gene expression in response to oxidative stress and during differentiation of mouse skeletal muscle. Free Radic Biol Med 27:1122–1132

    Article  CAS  PubMed  Google Scholar 

  41. McClung JP, Roneker CA, Mu W et al (2004) Development of insulin resistance and obesity in mice overexpressing cellular glutathione peroxidase. Proc Natl Acad Sci U S A 101:8852–8857

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  42. Wang XD, Vatamaniuk MZ, Wang SK et al (2008) Molecular mechanisms for hyperinsulinaemia induced by overproduction of selenium-dependent glutathione peroxidase-1 in mice. Diabetologia 51:1515–1524

    Article  CAS  PubMed  Google Scholar 

  43. Hawkes WC, Alkan Z (2010) Regulation of redox signaling by selenoproteins. Biol Trace Elem Res 134:235–251

    Article  CAS  PubMed Central  PubMed  Google Scholar 

Download references

Acknowledgments

This study was supported by the National Natural Science Foundation of China (31272626); the International (Regional) Cooperation and Exchange Projects of the National Natural Science Foundation of China (31320103920); the Study Abroad Foundation of Heilongjiang Province (LC201031); and the Doctoral Fund of the Ministry of Education of China (20122325110018). We are thankful for the support of the Key Laboratory of Myocardial Ischemia, Harbin Medical University. The authors thank Elsevier English Language Editing System to correct grammatical, spelling, and other common errors.

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The authors declare that there are no conflicts of interest

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Authors and Affiliations

  1. College of Veterinary Medicine, Northeast Agricultural University, Harbin, 150030, People’s Republic of China

    Haidong Yao, Wenchao Zhao, Xia Zhao, Ruifeng Fan, Pervez Ahmed Khoso, Ziwei Zhang, Wei Liu & Shiwen Xu

  2. The Key Laboratory of Myocardial Ischemia, Harbin Medical University, Ministry of Education, Harbin, Heilongjiang Province, China

    Wei Liu

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  1. Haidong Yao
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  2. Wenchao Zhao
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  3. Xia Zhao
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Correspondence to Wei Liu or Shiwen Xu.

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Yao, H., Zhao, W., Zhao, X. et al. Selenium Deficiency Mainly Influences the Gene Expressions of Antioxidative Selenoproteins in Chicken Muscles. Biol Trace Elem Res 161, 318–327 (2014). https://doi.org/10.1007/s12011-014-0125-2

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