Diet affects the redox system in developing Atlantic cod (Gadus morhua) larvae

Redox Biology

Volumn 5, Issue , 2015, Pages 308-318

  Penglase, Samuel ^a   Edvardsen, Rolf B ^a   Furmanek, Tomasz ^a   Rønnestad, Ivar ^b   Karlsen, Ørjan ^a   van der Meeren, Terje ^a   Hamre, Kristin ^a  

^a INSTITUTE OF MARINE RESEARCH   (Norway)

^b UNIVERSITY OF BERGEN   (Norway)

Author keywords

Development; Fish; Glutathione; Nrf2; Nutrition; Redox

Indexed keywords

GLUTATHIONE; MESSENGER RNA; TRANSCRIPTION FACTOR NRF2; RNA;

ANIMAL CELL; ANIMAL TISSUE; ANTIOXIDANT ACTIVITY; ARTEMIA; ARTICLE; ATLANTIC COD; CONTROLLED STUDY; DIETARY INTAKE; GENE; LARVAL DEVELOPMENT; NONHUMAN; NRF2 GENE; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION REACTION; OXIDATION REDUCTION STATE; OXIDATIVE STRESS; PRIORITY JOURNAL; REDOX STRESS; RNA GENE; ROTIFERA; SPECIES COMPARISON; TRANSCRIPTION REGULATION; UPREGULATION; ANIMAL; CHEMISTRY; DIET; GENE EXPRESSION REGULATION; GENETICS; GROWTH, DEVELOPMENT AND AGING; HIGH THROUGHPUT SEQUENCING; METABOLISM; SEQUENCE ANALYSIS;

ARTEMIA; COPEPODA; GADUS MORHUA; ROTIFERA;

ANIMALS; DIET; GADUS MORHUA; GENE EXPRESSION REGULATION; GLUTATHIONE; HIGH-THROUGHPUT NUCLEOTIDE SEQUENCING; NF-E2-RELATED FACTOR 2; OXIDATION-REDUCTION; OXIDATIVE STRESS; RNA; SEQUENCE ANALYSIS, RNA;

EID: 84934897423     PISSN: 22132317     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.redox.2015.06.003     Document Type: Article

References (49)

1. Busch K.E.T., Falk-Petersen I.B., Peruzzi S., Rist N.A., Hamre K. Natural zooplankton as larval feed in intensive rearing systems for juvenile production of Atlantic cod (Gadus morhua L.). Aquac. Res. 2010, 41(12):1727-1740. 10.1111/j.1365-2109.2009.02450.x.
2. Busch K.E.T., Peruzzi S., Tonning F., Falk-Petersen I.B. Effect of prey type and size on the growth, survival and pigmentation of cod (Gadus morhua L.) larvae. Aquac. Nutr. 2011, 17(2):e595-e603. 10.1111/j.1365-2095.2010.00800.x.
3. Karlsen Ø, van der Meeren T., Rønnestad I., Mangor-Jensen A., Galloway T.F., Kjørsvik E., Hamre K. Copepods enhance nutritional status, growth and development in Atlantic cod (Gadus morhua L.) larvae - can we identify the underlying factors?. PeerJ 2015, 3:e902. http://www.ncbi.nlm.nih.gov/pubmed/26038712, 10.7717/peerj.902.
4. Hamre K., Opstad I., Espe M., Solbakken J., Hemre G.-I., Pittman K. Nutrient composition and metamorphosis success of Atlantic halibut (Hippoglossus hippoglossus, L.) larvae fed natural zooplankton or artemia. Aquac. Nutr. 2002, 8(2):139-148. 10.1046/j.1365-2095.2002.00201.x.
5. Penglase S., Hamre K., Olsvik P.A., Grøtan E., Nordgreen A. Rotifers enriched with iodine, copper and manganese had no effect on larval cod (Gadus morhua) growth, mineral status or redox system gene mRNA levels. Aquac. Res. 2013.
6. Hawkyard M., Laurel B., Langdon C. Rotifers enriched with taurine by microparticulate and dissolved enrichment methods influence the growth and metamorphic development of northern rock sole (Lepidopsetta polyxystra) larvae. Aquaculture 2014, 424-425:151-157. 10.1016/j.aquaculture.2013.12.035.
7. Hamre K., Srivastava A., Rønnestad I., Mangor-Jensen A., Stoss J. Several micronutrients in the rotifer Brachionus sp. may not fulfil the nutritional requirements of marine fish larvae. Aquac. Nutr. 2008, 14(1):51-60. 10.1111/j.1365-2095.2007.00504.x.
8. van der Meeren T., Olsen R.E., Hamre K., Fyhn H.J. Biochemical composition of copepods for evaluation of feed quality in production of juvenile marine fish. Aquaculture 2008, 274(2-4):375-397. 10.1016/j.aquaculture.2007.11.041.
9. Hamre K., Yúfera M., Rønnestad I., Boglione C., Conceição L.E.C., Izquierdo M. Fish larval nutrition and feed formulation: knowledge gaps and bottlenecks for advances in larval rearing. Rev. Aquac. 2013, 5:S26-S58. 10.1111/j.1753-5131.2012.01086.x.
10. Conceição L., Aragão C., Rønnestad I. Proteins. Larval Fish Nutrition 2011, 83-116. Wiley Blackwell, Malaysia. G.J. Holt (Ed.).
11. Moren M., Waagbø R., Hamre K. Micronutrients. Larval Fish Nutrition 2011, 117-149. Wiley Blackwell, Malaysia. G.J. Holt (Ed.).
12. Ufer C., Wang C.C. The roles of glutathione peroxidases during embryo development. Front. Mol. Neurosci. 2011, 4:12. http://www.ncbi.nlm.nih.gov/pubmed/21847368, 10.3389/fnmol.2011.00012.
13. Meier P., Finch A., Evan G. Apoptosis in development. Nature 2000, 407(6805):796-801. http://www.ncbi.nlm.nih.gov/pubmed/11048731, 10.1038/35037734.
14. Cole L.K., Ross L.S. Apoptosis in the developing zebrafish embryo. Dev. Biol. 2001, 240(1):123-142. http://www.ncbi.nlm.nih.gov/pubmed/11784051, 10.1006/dbio.2001.0432.
15. Pedersen T., Falk-Petersen I.B. Morphological changes during metamorphosis in cod (Gadus morhua L.), with particular reference to the development of the stomach and pyloric caeca. J. Fish Biol. 1992, 41(3):449-461. 10.1111/j.1095-8649.1992.tb02673.x.
16. Schafer F.Q., Buettner G.R. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic. Biol. Med. 2001, 30(11):1191-1212. http://www.ncbi.nlm.nih.gov/pubmed/11368918, 10.1016/S0891-5849(01)00480-4.
17. Kirlin W.G., Cai J., Thompson S.A., Diaz D., Kavanagh T.J., Jones D.P. Glutathione redox potential in response to differentiation and enzyme inducers. Free Radic. Biol. Med. 1999, 27(11-12):1208-1218. http://www.ncbi.nlm.nih.gov/pubmed/10641713, 10.1016/S0891-5849(99)00145-8.
18. Go Y.M., Jones D.P. The redox proteome. J. Biol. Chem. 2013, 288(37):26512-26520. http://www.ncbi.nlm.nih.gov/pubmed/23861437, 10.1074/jbc.R113.464131.
19. Ma Q. Role of Nrf2 in oxidative stress and toxicity. Annu. Rev. Pharmacol. Toxicol. 2013, 53:401-426. http://www.ncbi.nlm.nih.gov/pubmed/23294312, 10.1146/annurev-pharmtox-011112-140320.
20. Huseby N.E., Sundkvist E., Svineng G. Glutathione and sulfur containing amino acids: antioxidant and conjugation activities. Glutathione and Sulfur Containing Amino Acids in Human Health and Disease 2009, Wiley, Hoboken, NJ. R. Masella, G. Mazza (Eds.).
21. Hamre K., Penglase S.J., Rasinger J.D., Skjærven K.H., Olsvik P.A. Ontogeny of redox regulation in Atlantic cod (Gadus morhua) larvae. Free Radic. Biol. Med. 2014, 73:337-348. http://www.ncbi.nlm.nih.gov/pubmed/24873722, 10.1016/j.freeradbiomed.2014.05.017.
22. Timme-Laragy A.R., Goldstone J.V., Imhoff B.R., Stegeman J.J., Hahn M.E., Hansen J.M. Glutathione redox dynamics and expression of glutathione-related genes in the developing embryo. Free Radic. Biol. Med. 2013, 65:89-101. http://www.ncbi.nlm.nih.gov/pubmed/23770340, 10.1016/j.freeradbiomed.2013.06.011.
23. Skjærven K.H., Penglase S., Olsvik P.A., Hamre K. Redox regulation in Atlantic cod (Gadus morhua) embryos developing under normal and heat-stressed conditions. Free Radic. Biol. Med. 2013, 57:29-38. http://www.ncbi.nlm.nih.gov/pubmed/23246569, 10.1016/j.freeradbiomed.2012.11.022.
24. van der Meeren T., Karlsen Ø., Liebig P.L., Mangor-Jensen A. Copepod production in a saltwater pond system: a reliable method for achievement of natural prey in start-feeding of marine fish larvae. Aquac. Eng. 2014, 62:17-27. 10.1016/j.aquaeng.2014.07.003.
25. Steneck R.S. Apex predators and trophic cascades in large marine ecosystems: learning from serendipity. Proc. Natl. Acad. Sci. U. S. A. 2012, 109(21):7953-7954. http://www.ncbi.nlm.nih.gov/pubmed/22586126, 10.1073/pnas.1205591109.
26. FAO The State of the Worlds Fisheries and Aquaculture 2010, Food and Agriculture Organization of the United Nations, Rome.
27. van der Meeren T., Lønøy T. Use of mesocosms in larval rearing of saithe [Pollachius virens (L.)], goldsinny [Ctenolabrus rupestris (L.)], and corkwing [Crenilabrus melops (L.)]. Aquac. Eng. 1998, 17(4):253-260. 10.1016/S0144-8609(98)00020-X.
28. Star B., Nederbragt A.J., Jentoft S., Grimholt U., Malmstrøm M., Gregers T.F., Rounge T.B., Paulsen J., Solbakken M.H., Sharma A., Wetten O.F., Lanzén A., Winer R., Knight J., Vogel J.-H.H., Aken B., Andersen O., Lagesen K., Tooming-Klunderud A., Edvardsen R.B., Tina K.G., Espelund M., Nepal C., Previti C., Karlsen B.O., Moum T., Skage M., Berg P.R., Gjøen T., Kuhl H., Thorsen J., Malde K., Reinhardt R., Du L., Johansen S.D., Searle S., Lien S., Nilsen F., Jonassen I., Omholt S.W. The genome sequence of Atlantic cod reveals a unique immune system. Nature 2011, 477(7363):207-210. http://www.ncbi.nlm.nih.gov/pubmed/21832995, 10.1038/nature10342.
29. Li H., Durbin R. Fast and accurate short read alignment with Burrows-Wheeler transform. Bioinformatics 2009, 25(14):1754-1760. http://www.ncbi.nlm.nih.gov/pubmed/19451168, 10.1093/bioinformatics/btp324.
30. Morgan B., Ezeriņa D., Amoako T.N., Riemer J., Seedorf M., Dick T.P. Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis. Nat. Chem. Biol. 2013, 9(2):119-125. http://www.ncbi.nlm.nih.gov/pubmed/23242256, 10.1038/nchembio.1142.
31. Kemp M., Go Y.-M.M., Jones D.P. Nonequilibrium thermodynamics of thiol/disulfide redox systems: a perspective on redox systems biology. Free Radic. Biol. Med. 2008, 44(6):921-937. http://www.ncbi.nlm.nih.gov/pubmed/18155672, 10.1016/j.freeradbiomed.2007.11.008.
32. Osborne J.W. Improving your data transformations: applying the Box-Cox transformation. Pract. Assess. Res. Eval. 2010, 15(12):9.
33. Thompson A.B., Harrop R.T. Feeding dynamics of fish larvae on copepoda in the western Irish Sea, with particular reference to cod Gadus morhua. Mar. Ecol. Prog. Ser. 1991, 68:213-223.
34. Lu S.C. Glutathione synthesis. Biochim. Biophys. Acta 2013, 1830(5):3143-3153. http://www.ncbi.nlm.nih.gov/pubmed/22995213, 10.1016/j.bbagen.2012.09.008.
35. Stanton R.C. Glucose-6-phosphate dehydrogenase, NADPH, and cell survival. I.U.B.M.B. Life 2012, 64(5):362-369. http://www.ncbi.nlm.nih.gov/pubmed/22431005.
36. Berndt C., Lillig C.H., Flohé L. Redox regulation by glutathione needs enzymes. Front. Pharmacol. 2014, 5:168. http://www.ncbi.nlm.nih.gov/pubmed/25100998, 10.3389/fphar.2014.00168.
37. Mailloux R.J., Willmore W.G. S-glutathionylation reactions in mitochondrial function and disease. Front. Cell. Dev. Biol. 2014, 2:68. http://www.ncbi.nlm.nih.gov/pubmed/25453035, 10.3389/fcell.2014.00068.
38. Hayes J.D., McMahon M. NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer. Trends Biochem. Sci. 2009, 34(4):176-188. http://www.ncbi.nlm.nih.gov/pubmed/19321346, 10.1016/j.tibs.2008.12.008.
39. Mukaigasa K., Nguyen L.T., Li L., Nakajima H., Yamamoto M., Kobayashi M. Genetic evidence of an evolutionarily conserved role for Nrf2 in the protection against oxidative stress. Mol. Cell. Biol. 2012, 32(21):4455-4461. http://www.ncbi.nlm.nih.gov/pubmed/22949501, 10.1128/MCB.00481-12.
40. Michiels C., Raes M., Toussaint O., Remacle J. Importance of SE-glutathione peroxidase, catalase, and CU/ZN-SOD for cell survival against oxidative stress. Free Radic. Biol. Med. 1994, 17(3):235-248. http://www.ncbi.nlm.nih.gov/pubmed/7982629, 10.1016/0891-5849(94)90079-5.
41. Karplus P.A. A primer on peroxiredoxin biochemistry. Free Radic. Biol. Med. 2015, 80:183-190. 10.1016/j.freeradbiomed.2014.10.009.
42. Du Y., Zhang H., Zhang X., Lu J., Holmgren A. Thioredoxin 1 is inactivated due to oxidation induced by peroxiredoxin under oxidative stress and reactivated by the glutaredoxin system. J. Biol. Chem. 2013, 288(45):32241-32247. http://www.ncbi.nlm.nih.gov/pubmed/24062305, 10.1074/jbc.M113.495150.
43. Takeuchi T. Progress on larval and juvenile nutrition to improve the quality and health of seawater fish: a review. Fish. Sci. 2014, 80(3):389-403. 10.1007/s12562-014-0744-8.
44. Hansen S.H., Andersen M.L., Cornett C., Gradinaru R., Grunnet N. A role for taurine in mitochondrial function. J. Biomed. Sci. 2010, 17(Suppl. 1). 10.1186/1423-0127-17-S1-S23.
45. Jong C.J., Azuma J., Schaffer S. Mechanism underlying the antioxidant activity of taurine: prevention of mitochondrial oxidant production. Amino Acids 2012, 42(6):2223-2232. http://www.ncbi.nlm.nih.gov/pubmed/21691752, 10.1007/s00726-011-0962-7.
46. Mailloux R.J., McBride S.L., Harper M.-E.E. Unearthing the secrets of mitochondrial ROS and glutathione in bioenergetics. Trends Biochem. Sci. 2013, 38(12):592-602. http://www.ncbi.nlm.nih.gov/pubmed/24120033, 10.1016/j.tibs.2013.09.001.
47. Lee B.C., Dikiy A., Kim H.-Y., Gladyshev V.N. Functions and evolution of selenoprotein methionine sulfoxide reductases. Biochim. Biophys. Acta 2009, 1790(11):1471-1477. http://www.ncbi.nlm.nih.gov/pubmed/19406207, 10.1016/j.bbagen.2009.04.014.
48. 2 generation: redox signaling and oxidative stress. J. Biol. Chem. 2014, 289(13):8735-8741. http://www.ncbi.nlm.nih.gov/pubmed/24515117, 10.1074/jbc.R113.544635.
49. Cox A.G., Winterbourn C.C., Hampton M.B. Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling. Biochem. J. 2010, 425(2):313-325. http://www.ncbi.nlm.nih.gov/pubmed/20025614, 10.1042/BJ20091541.