Effects of acclimation salinity on the expression of selenoproteins in the tilapia, Oreochromis mossambicus.

Lucia A Seale, Christy L Gilman, Benjamin P Moorman, Marla J Berry, E Gordon Grau, Andre P Seale
Author Information
  1. Lucia A Seale: Department of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii at Manoa, Honolulu, HI 96813, USA. Electronic address: lseale@hawaii.edu.
  2. Christy L Gilman: Department of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii at Manoa, Honolulu, HI 96813, USA.
  3. Benjamin P Moorman: Hawaii Institute of Marine Biology, University of Hawaii, Kaneohe, HI 96744, USA.
  4. Marla J Berry: Department of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii at Manoa, Honolulu, HI 96813, USA.
  5. E Gordon Grau: Hawaii Institute of Marine Biology, University of Hawaii, Kaneohe, HI 96744, USA.
  6. Andre P Seale: Hawaii Institute of Marine Biology, University of Hawaii, Kaneohe, HI 96744, USA.

Abstract

Selenoproteins are ubiquitously expressed, act on a variety of physiological redox-related processes, and are mostly regulated by selenium levels in animals. To date, the expression of most selenoproteins has not been verified in euryhaline fish models. The Mozambique tilapia, Oreochromis mossambicus, a euryhaline cichlid fish, has a high tolerance for changes in salinity and survives in fresh water (FW) and seawater (SW) environments which differ greatly in selenium availability. In the present study, we searched EST databases for cichlid selenoprotein mRNAs and screened for their differential expression in FW and SW-acclimated tilapia. The expression of mRNAs encoding iodothyronine deiodinases 1, 2 and 3 (Dio1, Dio2, Dio3), Fep15, glutathione peroxidase 2, selenoproteins J, K, L, M, P, S, and W, was measured in the brain, eye, gill, kidney, liver, pituitary, muscle, and intraperitoneal white adipose tissue. Gene expression of selenophosphate synthetase 1, Secp43, and selenocysteine lyase, factors involved in selenoprotein synthesis or in selenium metabolism, were also measured. The highest variation in selenoprotein and synthesis factor mRNA expression between FW- and SW-acclimated fish was found in gill and kidney. While the branchial expression of Dio3 was increased upon transferring tilapia from SW to FW, the inverse effect was observed when fish were transferred from FW to SW. Protein content of Dio3 was higher in fish acclimated to FW than in those acclimated to SW. Together, these results outline tissue distribution of selenoproteins in FW and SW-acclimated tilapia, and indicate that at least Dio3 expression is regulated by environmental salinity.

Keywords

References

  1. Bioinformatics. 2007 Nov 1;23(21):2947-8 [PMID: 17846036]
  2. Endocrinology. 1997 May;138(5):1787-93 [PMID: 9112369]
  3. Gen Comp Endocrinol. 2012 May 1;176(3):354-60 [PMID: 22036842]
  4. J Biol Chem. 2007 Aug 17;282(33):23759-65 [PMID: 17526492]
  5. FEBS Lett. 1999 Jul 2;454(1-2):16-20 [PMID: 10413087]
  6. Comp Biochem Physiol C Toxicol Pharmacol. 2012 May;155(4):560-5 [PMID: 22261037]
  7. Biochim Biophys Acta. 2009 Nov;1790(11):1441-7 [PMID: 19345254]
  8. Curr Opin Pediatr. 2011 Aug;23(4):429-35 [PMID: 21670677]
  9. Proc Natl Acad Sci U S A. 2007 Aug 28;104(35):13919-24 [PMID: 17715293]
  10. Genes Cells. 2000 Nov;5(11):897-903 [PMID: 11122377]
  11. Comp Biochem Physiol A Mol Integr Physiol. 2002 Feb;131(2):387-95 [PMID: 11818227]
  12. Nucleic Acids Res. 2007;35(12):3963-73 [PMID: 17553827]
  13. J Nutr. 1984 Mar;114(3):627-33 [PMID: 6699743]
  14. Endocrinology. 1997 Feb;138(2):642-8 [PMID: 9002998]
  15. IUBMB Life. 2008 Apr;60(4):232-5 [PMID: 18344183]
  16. Cell Mol Life Sci. 2009 Aug;66(15):2457-78 [PMID: 19399585]
  17. J Endocrinol. 2012 Apr;213(1):89-98 [PMID: 22266961]
  18. J Nutr. 1980 Dec;110(12):2527-35 [PMID: 7441379]
  19. Methods Mol Biol. 2000;132:365-86 [PMID: 10547847]
  20. Comp Biochem Physiol A Mol Integr Physiol. 2010 Mar;155(3):294-300 [PMID: 19879953]
  21. J Lipid Res. 2007 Mar;48(3):503-8 [PMID: 17132865]
  22. Genome Biol. 2008;9(3):R62 [PMID: 18377657]
  23. Endocrinology. 1999 Aug;140(8):3666-73 [PMID: 10433225]
  24. J Endocrinol Invest. 2011 May;34(5):395-407 [PMID: 21427525]
  25. Proc Natl Acad Sci U S A. 2005 Nov 8;102(45):16188-93 [PMID: 16260744]
  26. J Biol Chem. 1995 Sep 15;270(37):21659-64 [PMID: 7665581]
  27. Aquat Toxicol. 2013 Apr 15;130-131:97-111 [PMID: 23384997]
  28. J Inorg Biochem. 2006 Oct;100(10):1679-84 [PMID: 16876868]
  29. Genes Cells. 2000 Dec;5(12):1049-60 [PMID: 11168591]
  30. Aquat Toxicol. 2012 Jun 15;114-115:134-41 [PMID: 22446825]
  31. Biochem Biophys Res Commun. 2011 Jun 17;409(4):814-9 [PMID: 21624347]
  32. J Leukoc Biol. 2013 May;93(5):771-80 [PMID: 23444136]
  33. J Biol Chem. 2000 Mar 3;275(9):6195-200 [PMID: 10692412]
  34. Environ Pollut. 2009 Oct;157(10):2790-7 [PMID: 19467747]
  35. Gen Comp Endocrinol. 2013 Oct 1;192:191-203 [PMID: 23722201]
  36. J Biol Chem. 2003 Apr 18;278(16):13640-6 [PMID: 12574155]
  37. Antioxid Redox Signal. 2010 Apr 1;12(7):809-18 [PMID: 19769485]
  38. Mol Cell Biol. 2006 Mar;26(6):2337-46 [PMID: 16508009]
  39. Biosci Rep. 2009 Jun 25;29(5):329-38 [PMID: 19076066]
  40. J Exp Biol. 2002 Dec;205(Pt 23):3699-706 [PMID: 12409496]
  41. Thyroid. 2005 Aug;15(8):799-813 [PMID: 16131323]
  42. Mol Cell Biol. 2006 Dec;26(24):9177-84 [PMID: 17000762]
  43. Comp Biochem Physiol A Mol Integr Physiol. 2007 Nov;148(3):479-97 [PMID: 17689996]
  44. Am J Physiol Regul Integr Comp Physiol. 2007 Aug;293(2):R877-83 [PMID: 17522123]
  45. Biochem J. 2006 Mar 15;394(Pt 3):575-9 [PMID: 16236027]
  46. Comp Biochem Physiol B. 1979;63(1):39-44 [PMID: 400960]
  47. Genome Biol. 2007;8(9):R198 [PMID: 17880704]
  48. Comp Biochem Physiol A Mol Integr Physiol. 2010 Dec;157(4):310-8 [PMID: 20659579]
  49. J Exp Biol. 1989 Jul;144:507-20 [PMID: 2549165]
  50. Gen Comp Endocrinol. 2000 Nov;120(2):157-67 [PMID: 11078627]
  51. Fish Physiol Biochem. 1989 Jun;7(1-6):11-9 [PMID: 24221750]
  52. Physiol Rev. 2005 Jan;85(1):97-177 [PMID: 15618479]
  53. PLoS One. 2012;7(3):e33066 [PMID: 22479358]
  54. FEBS Lett. 2004 Apr 9;563(1-3):185-90 [PMID: 15063746]
  55. Lancet. 2012 Mar 31;379(9822):1256-68 [PMID: 22381456]
  56. Comp Biochem Physiol B Biochem Mol Biol. 2012 Apr;161(4):392-7 [PMID: 22285500]
  57. J Biol Chem. 1982 Apr 25;257(8):4386-91 [PMID: 6461656]
  58. Antioxid Redox Signal. 2010 Apr 1;12(7):839-49 [PMID: 19747065]

Grants

  1. G12 MD007601/NIMHD NIH HHS
  2. G12 RR003061/NCRR NIH HHS
  3. R01 DK047320/NIDDK NIH HHS
  4. G12RR003061-27/NCRR NIH HHS

MeSH Term

Animals
Phosphotransferases
Selenium
Selenoproteins
Tilapia

Chemicals

Selenoproteins
Phosphotransferases
Selenium

Word Cloud

Created with Highcharts 10.0.0expressionFWfishtilapiaselenoproteinssalinitySWDio3seleniumselenoproteinSW-acclimatedregulatedeuryhalineOreochromismossambicuscichlidmRNAs12measuredgillkidneytissuesynthesisacclimatedSelenoproteinsubiquitouslyexpressedactvarietyphysiologicalredox-relatedprocessesmostlylevelsanimalsdateverifiedmodelsMozambiquehightolerancechangessurvivesfreshwaterseawaterenvironmentsdiffergreatlyavailabilitypresentstudysearchedESTdatabasesscreeneddifferentialencodingiodothyroninedeiodinases3Dio1Dio2Fep15glutathioneperoxidaseJKLMPSWbraineyeliverpituitarymuscleintraperitonealwhiteadiposeGeneselenophosphatesynthetaseSecp43selenocysteinelyasefactorsinvolvedmetabolismalsohighestvariationfactormRNAFW-foundbranchialincreasedupontransferringinverseeffectobservedtransferredProteincontenthigherTogetherresultsoutlinedistributionindicateleastenvironmentalEffectsacclimationAcclimationEuryhalineFishSeleniumSelenoproteinTilapia

Similar Articles

Cited By