Abstract
The demand for animal protein for human consumption is currently on the rise fueled mainly by an exponential increase of the world population. The higher demand of fishery products and capture restrictions as a result of wild fish stock exploitation made aquaculture an extremely important source of protein (mainly fish, shellfish, and algae) available in human diet. Production statistics database from FAO states a value of about 97.2 million tonnes, of which around 70.0 million tonnes of the total food fish and 27.0 million tonnes of aquatic plants. The awareness that nowadays competitiveness is extremely dependent on scientific knowledge and new technologies made the number of manuscripts published in this area to rise almost exponentially. Aquaculture faces many challenges in order to continuously deliver a high-quality farmed fish through a sustainable production system. In order to achieve this goal, new management strategies need to be addressed, and state-of-the-art technologies like proteomics have been applied to study many factors like welfare, safety, nutrition, and diseases, which are directly responsible for the end-product quality.
References
Adams A, Thompson KD (2006) Biotechnology offers revolution to fish health management. Trends Biotechnol 24(5):201–205. https://doi.org/10.1016/j.tibtech.2006.03.004
Addis MF, Cappuccinelli R, Tedde V, Pagnozzi D, Porcu MC, Bonaglini E, Roggio T, Uzzau S (2010) Proteomic analysis of muscle tissue from gilthead sea bream (Sparus aurata, L.) farmed in offshore floating cages. Aquaculture 309(1–4):245–252. https://doi.org/10.1016/j.aquaculture.2010.08.022
Ahsan N, Rao RSP, Gruppuso PA, Ramratnam B, Salomon AR (2016) Targeted proteomics: current status and future perspectives for quantification of food allergens. J Proteome 143:15–23. https://doi.org/10.1016/j.jprot.2016.04.018
Almeida AM, Bassols A, Bendixen E, Bhide M, Ceciliani F, Cristobal S, Eckersall PD, Hollung K, Lisacek F, Mazzucchelli G, McLaughlin M, Miller I, Nally JE, Plowman J, Renaut J, Rodrigues P, Roncada P, Staric J, Turk R (2015) Animal board invited review: advances in proteomics for animal and food sciences. Animal 9(1):1–17. https://doi.org/10.1017/S1751731114002602
Alves RN, Cordeiro O, Silva TS, Richard N, de Vareilles M, Marino G, Di Marco P, Rodrigues PM, Conceição LEC (2010) Metabolic molecular indicators of chronic stress in gilthead seabream (Sparus aurata) using comparative proteomics. Aquaculture 299(1–4):57–66. https://doi.org/10.1016/j.aquaculture.2009.11.014
Ardura A, Planes S, Garcia-Vazquez E (2011) Beyond biodiversity: fish metagenomes. PLoS One 6(8):e22592. https://doi.org/10.1371/journal.pone.0022592
Ashley PJ (2007) Fish welfare: current issues in aquaculture. Appl Anim Behav Sci 104(3–4):199–235. https://doi.org/10.1016/j.applanim.2006.09.001
Ballmer-Weber BK, Fernandez-Rivas M, Beyer K, Defernez M, Sperrin M, Mackie AR, Salt LJ, Hourihane JOB, Asero R, Belohlavkova S, Kowalski M, de Blay F, Papadopoulos NG, Clausen M, Knulst AC, Roberts G, Popov T, Sprikkelman AB, Dubakiene R, Vieths S, van Ree R, Crevel R, Mills ENC (2015) How much is too much? Threshold dose distributions for 5 food allergens. J Allergy Clin Immunol 135(4):964–971. https://doi.org/10.1016/j.jaci.2014.10.047
Barbosa EB, Vidotto A, Polachini GM, Henrique T, de Marqui ABT, Tajara EH (2012) Proteomics: methodologies and applications to the study of human diseases. Rev Assoc Med Bras 58(3):366–375
Baumgarner BL, Bharadwaj AS, Inerowicz D, Goodman AS, Brown PB (2013) Proteomic analysis of rainbow trout (Oncorhynchus mykiss) intestinal epithelia: physiological acclimation to short-term starvation. Comp Biochem Physiol Part D Genomics Proteomics 8(1):58–64. https://doi.org/10.1016/j.cbd.2012.11.001
Berrill IK, Cooper T, MacIntyre CM, Ellis T, Knowles TG, Jones EKM, Turnbull JF (2012) Achieving consensus on current and future priorities for farmed fish welfare: a case study from the UK. Fish Physiol Biochem 38(1):219–229. https://doi.org/10.1007/s10695-010-9399-2
Berrini A, Tepedino V, Borromeo V, Secchi C (2006) Identification of freshwater fish commercially labelled “perch” by isoelectric focusing and two-dimensional electrophoresis. Food Chem 96(1):163–168. https://doi.org/10.1016/j.foodchem.2005.04.007
Berthelot C, Brunet F, Chalopin D, Juanchich A, Bernard M, Noël B, Bento P, Da Silva C, Labadie K, Alberti A, Aury J-M, Louis A, Dehais P, Bardou P, Montfort J, Klopp C, Cabau C, Gaspin C, Thorgaard GH, Boussaha M, Quillet E, Guyomard R, Galiana D, Bobe J, Volff J-N, Genêt C, Wincker P, Jaillon O, Crollius HR, Guiguen Y (2014) The rainbow trout genome provides novel insights into evolution after whole-genome duplication in vertebrates. Nat Commun 5:3657. https://doi.org/10.1038/ncomms4657
Boltaña S, Rey S, Roher N, Vargas R, Huerta M, Huntingford FA, Goetz FW, Moore J, Garcia-Valtanen P, Estepa A, MacKenzie S (2013) Behavioural fever is a synergic signal amplifying the innate immune response. Proc R Soc B Biol Sci 280(1766). https://doi.org/10.1098/rspb.2013.1381
Booth NJ, Bilodeau-Bourgeois AL (2009) Proteomic analysis of head kidney tissue from high and low susceptibility families of channel catfish following challenge with Edwardsiella ictaluri. Fish Shellfish Immunol 26(1):193–196. https://doi.org/10.1016/j.fsi.2008.03.003
Braceland M, Bickerdike R, Tinsley J, Cockerill D, McLoughlin MF, Graham DA, Burchmore RJ, Weir W, Wallace C, Eckersall PD (2013) The serum proteome of Atlantic salmon, Salmo salar, during pancreas disease (PD) following infection with salmonid alphavirus subtype 3 (SAV3). J Proteome 94:423–436. https://doi.org/10.1016/j.jprot.2013.10.016
Braceland M, McLoughlin MF, Tinsley J, Wallace C, Cockerill D, McLaughlin M, Eckersall PD (2015) Serum enolase: a non-destructive biomarker of white skeletal myopathy during pancreas disease (PD) in Atlantic salmon Salmo salar L. J Fish Dis 38(9):821–831. https://doi.org/10.1111/jfd.12296
Brownridge P, de Mello LV, Peters M, McLean L, Claydon A, Cossins AR, Whitfield PD, Young IS (2009) Regional variation in parvalbumin isoform expression correlates with muscle performance in common carp (Cyprinus carpio). J Exp Biol 212(2):184–193. https://doi.org/10.1242/Jeb.021857
Buján N, Hernández-Haro C, Monteoliva L, Gil C, Magariños B (2015) Comparative proteomic study of Edwardsiella tarda strains with different degrees of virulence. J Proteome 127(Part B):310–320. https://doi.org/10.1016/j.jprot.2015.05.008
Burge CA, Friedman CS, Getchell R, House M, Lafferty KD, Mydlarz LD, Prager KC, Sutherland KP, Renault T, Kiryu I, Vega-Thurber R (2016) Complementary approaches to diagnosing marine diseases: a union of the modern and the classic. Philos Trans R Soc B 371(1689). https://doi.org/10.1098/rstb.2015.0207
Carrera M, Canas B, Pineiro C, Vazquez J, Gallardo JM (2006) Identification of commercial hake and grenadier species by proteomic analysis of the parvalbumin fraction. Proteomics 6(19):5278–5287. https://doi.org/10.1002/pmic.200500899
Carrera M, Canas B, Lopez-Ferrer D, Pineiro C, Vazquez J, Gallardo JM (2011) Fast monitoring of species-specific peptide biomarkers using high-intensity-focused-ultrasound-assisted tryptic digestion and selected MS/MS ion monitoring. Anal Chem 83(14):5688–5695. https://doi.org/10.1021/ac200890w
Carrera M, Canas B, Gallardo JM (2012) Rapid direct detection of the major fish allergen, parvalbumin, by selected MS/MS ion monitoring mass spectrometry. J Proteome 75(11):3211–3220. https://doi.org/10.1016/j.jprot.2012.03.030
Carrera M, Cañas B, Gallardo JM (2013) Proteomics for the assessment of quality and safety of fishery products. Food Res Int 54(1):972–979. https://doi.org/10.1016/j.foodres.2012.10.027
Castillo J, Teles M, Mackenzie S, Tort L (2009) Stress-related hormones modulate cytokine expression in the head kidney of gilthead seabream (Sparus aurata). Fish Shellfish Immunol 27(3):493–499. https://doi.org/10.1016/j.fsi.2009.06.021
Chatterjee A, Eccles MR (2015) DNA methylation and epigenomics: new technologies and emerging concepts. Genome Biol 16(1):103. https://doi.org/10.1186/s13059-015-0674-5
Chen Z, Peng B, Wang S, Peng X (2004) Rapid screening of highly efficient vaccine candidates by immunoproteomics. Proteomics 4(10):3203–3213. https://doi.org/10.1002/pmic.200300844
Chicano-Gálvez E, Asensio E, Cañavate JP, Alhama J, López-Barea J (2015) Proteomic analysis through larval development of Solea senegalensis flatfish. Proteomics 15(23–24):4105–4119. https://doi.org/10.1002/pmic.201500176
Coates CJ, Decker H (2016) Immunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin. Cell Mol Life Sci 1–25. https://doi.org/10.1007/s00018-016-2326-7
Cordeiro O, Silva T, Alves R, Costas B, Wulff T, Richard N, de Vareilles M, Conceição LC, Rodrigues P (2012) Changes in liver proteome expression of Senegalese Sole (Solea senegalensis) in response to repeated handling stress. Mar Biotechnol 14(6):714–729. https://doi.org/10.1007/s10126-012-9437-4
de Vareilles M, Conceição LEC, Gómez-Requeni P, Kousoulaki K, Richard N, Rodrigues PM, Fladmark KE, Rønnestad I (2012) Dietary lysine imbalance affects muscle proteome in zebrafish (Danio rerio): a comparative 2D-DIGE study. Mar Biotechnol 14(5):643–654. https://doi.org/10.1007/s10126-012-9462-3
Di Girolamo F, Muraca M, Mazzina O, Lante I, Dahdah L (2015) Proteomic applications in food allergy: food allergenomics. Curr Opin Allergy Clin Immunol 15(3):259–266. https://doi.org/10.1097/aci.0000000000000160
Drivenes Ø, Taranger GL, Edvardsen RB (2012) Gene expression profiling of Atlantic cod (Gadus morhua) embryogenesis using microarray. Mar Biotechnol 14(2):167–176. https://doi.org/10.1007/s10126-011-9399-y
Dumpala PR, Gülsoy N, Lawrence ML, Karsi A (2010) Proteomic analysis of the fish pathogen Flavobacterium columnare. Proteome Sci 8(1):26. https://doi.org/10.1186/1477-5956-8-26
Ellis T, Yildiz HY, López-Olmeda J, Spedicato MT, Tort L, Øverli Ø, Martins CIM (2012) Cortisol and finfish welfare. Fish Physiol Biochem 38(1):163–188. https://doi.org/10.1007/s10695-011-9568-y
Encinas P, Rodriguez-Milla MA, Novoa B, Estepa A, Figueras A, Coll J (2010) Zebrafish fin immune responses during high mortality infections with viral haemorrhagic septicemia rhabdovirus. A proteomic and transcriptomic approach. BMC Genomics 11(1):518. https://doi.org/10.1186/1471-2164-11-518
Enyu YL, Shu-Chien AC (2011) Proteomics analysis of mitochondrial extract from liver of female zebrafish undergoing starvation and refeeding: proteomics analysis of mitochondrial extract of female zebrafish. Aquac Nutr 17(2):e413–e423. https://doi.org/10.1111/j.1365-2095.2010.00776.x
European P (2005) Commission regulation (EC) No 2073/2005 of 15 November 2005 on microbiological criteria for foodstuffs. Off J Eur Union L338:1–26
European P (2013) Council regulation (EU) No 1379/2013 of 11 December 2013 on the common organisation of the markets in fishery and aquaculture products. Off J Eur Union L354:1–21
FAO (2012) Code of practice for fish and fishery products. Quality and safety of fish and fish products. Fisheries and Aquaculture department. http://www.fao.org/fishery/quality_safety/en#container. Accessed 25 Oct 2016
Fernández-Álvarez C, Gijón D, Álvarez M, Santos Y (2016) First isolation of Aeromonas salmonicida subspecies salmonicida from diseased sea bass, Dicentrarchus labrax (L.), cultured in Spain. Aquaculture Rep 4:36–41. https://doi.org/10.1016/j.aqrep.2016.05.006
Forné I, Abián J, Cerdà J (2010) Fish proteome analysis: model organisms and non-sequenced species. Proteomics 10(4):858–872. https://doi.org/10.1002/pmic.200900609
Galland C, Dupuy C, Loizeau V, Danion M, Auffret M, Quiniou L, Laroche J, Pichereau V (2015) Proteomic analysis of the European flounder Platichthys flesus response to experimental PAH–PCB contamination. Mar Pollut Bull 95(2):646–657. https://doi.org/10.1016/j.marpolbul.2015.04.038
Gebriel M, Prabhudesai S, Uleberg K-E, Larssen E, Piston D, Bjørnstad AH, Møller SG (2014) Zebrafish brain proteomics reveals central proteins involved in neurodegeneration. J Neurosci Res 92(1):104–115. https://doi.org/10.1002/jnr.23297
Ghaedi G, Keyvanshokooh S, Azarm HM, Akhlaghi M (2016) Proteomic analysis of muscle tissue from rainbow trout (Oncorhynchus mykiss) fed dietary β-glucan. Iran J Vet Res 17(3):184
Ghisaura S, Anedda R, Pagnozzi D, Biosa G, Spada S, Bonaglini E, Cappuccinelli R, Roggio T, Uzzau S, Addis MF (2014) Impact of three commercial feed formulations on farmed gilthead sea bream (Sparus aurata, L.) metabolism as inferred from liver and blood serum proteomics. Proteome Sci 12(1):1. https://doi.org/10.1186/s12953-014-0044-3
Gómez-Requeni P, de Vareilles M, Kousoulaki K, Jordal A-EO, Conceição LEC, Rønnestad I (2011) Whole body proteome response to a dietary lysine imbalance in zebrafish Danio rerio. Comp Biochem Physiol Part D Genomics Proteomics 6(2):178–186. https://doi.org/10.1016/j.cbd.2011.02.002
Hamza N, Silvestre F, Mhetli M, Khemis IB, Dieu M, Raes M, Cahu C, Kestemont P (2010) Differential protein expression profile in the liver of pikeperch (Sander lucioperca) larvae fed with increasing levels of phospholipids. Comp Biochem Physiol Part D Genomics Proteomics 5(2):130–137. https://doi.org/10.1016/j.cbd.2010.03.005
Hill BJ (2005) The need for effective disease control in international aquaculture. Dev Biol (Basel) 121:3–12
Hogstrand C, Balesaria S, Glover CN (2002) Application of genomics and proteomics for study of the integrated response to zinc exposure in a non-model fish species, the rainbow trout. Comp Biochem Physiol B Biochem Mol Biol 133(4):523–535. https://doi.org/10.1016/S1096-4959(02)00125-2
Hosseini M, Kolangi Miandare H, Hoseinifar SH, Yarahmadi P (2016) Dietary Lactobacillus acidophilus modulated skin mucus protein profile, immune and appetite genes expression in gold fish (Carassius auratus gibelio). Fish Shellfish Immunol 59:149–154. https://doi.org/10.1016/j.fsi.2016.10.026
Huntingford F, Kadri S (2014) Defining, assessing and promoting the welfare of farmed fish. Rev Sci Tech (Int Off Epizootics) 33(1):233–244
Ibarz A, Costa R, Harrison AP, Power DM (2010a) Dietary keto-acid feed-back on pituitary activity in gilthead sea bream: effects of oral doses of AKG. A proteomic approach. Gen Comp Endocrinol 169(3):284–292. https://doi.org/10.1016/j.ygcen.2010.09.010
Ibarz A, Martin-Perez M, Blasco J, Bellido D, de Oliveira E, Fernandez-Borras J (2010b) Gilthead sea bream liver proteome altered at low temperatures by oxidative stress. Proteomics 10(5):963–975. https://doi.org/10.1002/pmic.200900528
Jensen LB (2015) Nutritional and environmental impacts on skin and mucus condition in Atlantic salmon (Salmo salar L.). Doctoral Thesis. University of Bergen, Norway
Jensen LB, Provan F, Larssen E, Bron JE, Obach A (2015) Reducing sea lice (Lepeophtheirus salmonis) infestation of farmed Atlantic salmon (Salmo salar L.) through functional feeds. Aquac Nutr 21(6):983–993. https://doi.org/10.1111/anu.12222
Jessen F, Wulff T, Mikkelsen JB, Hyldig G, Nielsen H (2012) Vegetable based fish feed changes protein expression in muscle of rainbow trout (Oncorhynchus mykiss). In: Rodrigues P, Eckersall D, de Almeida A (eds) Farm animal proteomics. Wageningen Academic, Wageningen, pp 134–137. https://doi.org/10.3920/978-90-8686-751-6_31
Johnson SL, Villarroel M, Rosengrave P, Carne A, Kleffmann T, Lokman PM, Gemmell NJ (2014) Proteomic analysis of chinook salmon (Oncorhynchus tshawytscha) ovarian fluid. PLoS One 9(8):e104155
Johnston I, Dunn J (1987) Temperature acclimation and metabolism in ectotherms with particular reference to teleost fish. In: Symposia of the society for experimental biology. Cambridge University Press, Cambridge, pp 67–93
Jury DR (2005) Proteomic analysis of the effects of diet in zebrafish liver. University of Akron, Akron
Jury DR, Kaveti S, Duan Z-H, Willard B, Kinter M, Londraville R (2008) Effects of calorie restriction on the zebrafish liver proteome. Comp Biochem Physiol Part D Genomics Proteomics 3(4):275–282. https://doi.org/10.1016/j.cbd.2008.07.003
Kao DY, Cheng YC, Kuo TY, Lin SB, Lin CC, Chow LP, Chen WJ (2009) Salt-responsive outer membrane proteins of Vibrio anguillarum serotype O1 as revealed by comparative proteome analysis. J Appl Microbiol 106(6):2079–2085. https://doi.org/10.1111/j.1365-2672.2009.04178.x
Karim M, Puiseux-Dao S, Edery M (2011) Toxins and stress in fish: proteomic analyses and response network. Toxicon 57(7–8):959–969. https://doi.org/10.1016/j.toxicon.2011.03.018
Keyvanshokooh S, Tahmasebi-Kohyani A (2012) Proteome modifications of fingerling rainbow trout (Oncorhynchus mykiss) muscle as an effect of dietary nucleotides. Aquaculture 324–325:79–84. https://doi.org/10.1016/j.aquaculture.2011.10.013
Kobayashi A, Kobayashi Y, Shiomi K (2016a) Fish allergy in patients with parvalbumin-specific immunoglobulin E depends on parvalbumin content rather than molecular differences in the protein among fish species. Biosci Biotechnol Biochem 80(10):2018–2021. https://doi.org/10.1080/09168451.2016.1189318
Kobayashi Y, Yang T, Yu C-T, Ume C, Kubota H, Shimakura K, Shiomi K, Hamada-Sato N (2016b) Quantification of major allergen parvalbumin in 22 species of fish by SDS–PAGE. Food Chem 194:345–353. https://doi.org/10.1016/j.foodchem.2015.08.037
Kochzius M, Seidel C, Antoniou A, Botla SK, Campo D, Cariani A, Vazquez EG, Hauschild J, Hervet C, Hjorleifsdottir S, Hreggvidsson G, Kappel K, Landi M, Magoulas A, Marteinsson V, Nolte M, Planes S, Tinti F, Turan C, Venugopal MN, Weber H, Blohm D (2010) Identifying fishes through DNA barcodes and microarrays. PLoS One 5(9):e12620. https://doi.org/10.1371/journal.pone.0012620
Kolder ICRM, van der Plas-Duivesteijn SJ, Tan G, Wiegertjes GF, Forlenza M, Guler AT, Travin DY, Nakao M, Moritomo T, Irnazarow I, den Dunnen JT, Anvar SY, Jansen HJ, Dirks RP, Palmblad M, Lenhard B, Henkel CV, Spaink HP (2016) A full-body transcriptome and proteome resource for the European common carp. BMC Genomics 17(1):701. https://doi.org/10.1186/s12864-016-3038-y
Kolditz C, Lefèvre F, Borthaire M, Médale F (2007) Transcriptome and proteome analysis of changes induced in trout liver by suppression of dietary fish oil. FASEB J 21(6):A1402–A1403
Kolditz CI, Paboeuf G, Borthaire M, Esquerre D, SanCristobal M, Lefevre F, Medale F (2008) Changes induced by dietary energy intake and divergent selection for muscle fat content in rainbow trout (Oncorhynchus mykiss), assessed by transcriptome and proteome analysis of the liver. BMC Genomics 9(1):506. https://doi.org/10.1186/1471-2164-9-506
Krogdahl Å, Gajardo K, Kortner TM, Penn M, Gu M, Berge GM, Bakke AM (2015) Soya saponins induce enteritis in Atlantic salmon (Salmo salar L.) J Agric Food Chem 63(15):3887–3902. https://doi.org/10.1021/jf506242t
Król E, Douglas A, Tocher DR, Crampton VO, Speakman JR, Secombes CJ, Martin SAM (2016) Differential responses of the gut transcriptome to plant protein diets in farmed Atlantic salmon. BMC Genomics 17(1):156. https://doi.org/10.1186/s12864-016-2473-0
Kuehn A, Swoboda I, Arumugam K, Hilger C, Hentges F (2014) Fish allergens at a glance: variable allergenicity of parvalbumins, the major fish allergens. Front Immunol 5:179. https://doi.org/10.3389/fimmu.2014.00179
Kumar G, Hummel K, Ahrens M, Menanteau-Ledouble S, Welch TJ, Eisenacher M, Razzazi-Fazeli E, El-Matbouli M (2016) Shotgun proteomic analysis of Yersinia ruckeri strains under normal and iron-limited conditions. Vet Res 47(1):100. https://doi.org/10.1186/s13567-016-0384-3
Kwasek KA (2012) The nutritional and genetic effects on body growth, reproduction and molecular mechanisms responsible for muscle growth in yellow perch Perca flavescens. The Ohio State University, Columbus
Lee KH (2001) Proteomics: a technology-driven and technology-limited discovery science. Trends Biotechnol 19(6):217–222. https://doi.org/10.1016/S0167-7799(01)01639-0
Lerebours A, Bignell JP, Stentiford GD, Feist SW, Lyons BP, Rotchell JM (2013) Advanced diagnostics applied to fish liver tumours: relating pathology to underlying molecular aetiology. Mar Pollut Bull 72(1):94–98. https://doi.org/10.1016/j.marpolbul.2013.04.016
Lien S, Koop BF, Sandve SR, Miller JR, Kent MP, Nome T, Hvidsten TR, Leong JS, Minkley DR, Zimin A, Grammes F, Grove H, Gjuvsland A, Walenz B, Hermansen RA, von Schalburg K, Rondeau EB, Di Genova A, Samy JKA, Olav Vik J, Vigeland MD, Caler L, Grimholt U, Jentoft S, Inge Våge D, de Jong P, Moen T, Baranski M, Palti Y, Smith DR, Yorke JA, Nederbragt AJ, Tooming-Klunderud A, Jakobsen KS, Jiang X, Fan D, Hu Y, Liberles DA, Vidal R, Iturra P, Jones SJM, Jonassen I, Maass A, Omholt SW, Davidson WS (2016) The Atlantic salmon genome provides insights into rediploidization. Nature 533(7602):200–205. https://doi.org/10.1038/nature17164
Liu GY, Nie P, Zhang J, Li N (2008) Proteomic analysis of the sarcosine-insoluble outer membrane fraction of Flavobacterium columnare. J Fish Dis 31(4):269–276. https://doi.org/10.1111/j.1365-2761.2007.00898.x
Liu S, Zhang Y, Zhou Z, Waldbieser G, Sun F, Lu J, Zhang J, Jiang Y, Zhang H, Wang X, Rajendran K, Khoo L, Kucuktas H, Peatman E, Liu Z (2012) Efficient assembly and annotation of the transcriptome of catfish by RNA-Seq analysis of a doubled haploid homozygote. BMC Genomics 13(1):595. https://doi.org/10.1186/1471-2164-13-595
Liu L, Li Q, Lin L, Wang M, Lu Y, Wang W, Yuan J, Li L, Liu X (2013) Proteomic analysis of epithelioma papulosum cyprini cells infected with spring viremia of carp virus. Fish Shellfish Immunol 35(1):26–35. https://doi.org/10.1016/j.fsi.2013.03.367
Lorgen M, Casadei E, Król E, Douglas A, Birnie Mike J, Ebbesson Lars OE, Nilsen Tom O, Jordan William C, Jørgensen EH, Dardente H, Hazlerigg David G, Martin Samuel AM (2015) Functional divergence of type 2 deiodinase paralogs in the Atlantic salmon. Curr Biol 25(7):936–941. https://doi.org/10.1016/j.cub.2015.01.074
Madeira D, Araújo JE, Vitorino R, Capelo JL, Vinagre C, Diniz MS (2016) Ocean warming alters cellular metabolism and induces mortality in fish early life stages: a proteomic approach. Environ Res 148:164–176. https://doi.org/10.1016/j.envres.2016.03.030
Mahanty A, Purohit GK, Banerjee S, Karunakaran D, Mohanty S, Mohanty BP (2016) Proteomic changes in the liver of Channa striatus in response to high temperature stress. Electrophoresis 37(12):1704–1717. https://doi.org/10.1002/elps.201500393
Mäkinen H, Papakostas S, Vøllestad LA, Leder EH, Primmer CR (2015) Plastic and evolutionary gene expression responses are correlated in European grayling (Thymallus thymallus) subpopulations adapted to different thermal environments. J Hered. https://doi.org/10.1093/jhered/esv069
Marco-Ramell A, de Almeida AM, Cristobal S, Rodrigues P, Roncada P, Bassols A (2016) Proteomics and the search for welfare and stress biomarkers in animal production in the one-health context. Mol BioSyst 12:2024–2035. https://doi.org/10.1039/c5mb00788g
Martin SAM, Cash P, Blaney S, Houlihan DF (2001) Proteome analysis of rainbow trout (Oncorhynchus mykiss) liver proteins during short term starvation. Fish Physiol Biochem 24(3):259–270. https://doi.org/10.1023/A:1014015530045
Martin SAM, Vilhelmsson O, Medale F, Watt P, Kaushik S, Houlihan DF (2003) Proteomic sensitivity to dietary manipulations in rainbow trout. Biochim Biophys Acta 1651(1–2):17–29. https://doi.org/10.1016/S1570-9639(03)00231-0
Martinez I, Jakobsen Friis T (2004) Application of proteome analysis to seafood authentication. Proteomics 4(2):347–354. https://doi.org/10.1002/pmic.200300569
Martinez I, Slizyte R, Dauksas E (2007) High resolution two-dimensional electrophoresis as a tool to differentiate wild from farmed cod (Gadus morhua) and to assess the protein composition of klipfish. Food Chem 102(2):504–510. https://doi.org/10.1016/j.foodchem.2006.03.037
Matos E, Silva TS, Wulff T, Valente LMP, Sousa V, Sampaio E, Goncalves A, Silva JMG, de Pinho PG, Dinis MT, Rodrigues PM, Dias J (2013) Influence of supplemental maslinic acid (olive-derived triterpene) on the post-mortem muscle properties and quality traits of gilthead seabream. Aquaculture 396:146–155. https://doi.org/10.1016/j.aquaculture.2013.02.044
Matsumoto T, Feroudj H, Kikuchi R, Kawana Y, Kondo H, Hirono I, Mochizuki T, Nagashima Y, Kaneko G, Ushio H, Kodama M, Watabe S (2014) DNA microarray analysis on the genes differentially expressed in the liver of the pufferfish, Takifugu rubripes, following an intramuscular administration of Tetrodotoxin. Microarrays (Basel) 3(4):226–244. https://doi.org/10.3390/microarrays3040226
Mazzeo MF, Siciliano RA (2016) Proteomics for the authentication of fish species. J Proteome 147:119–124. https://doi.org/10.1016/j.jprot.2016.03.007
Mazzeo MF, De Giulio B, Guerriero G, Ciarcia G, Malorni A, Russo GL, Siciliano RA (2008) Fish authentication by MALDI-TOF mass spectrometry. J Agric Food Chem 56(23):11071–11076. https://doi.org/10.1021/jf8021783
Mente E, Pierce GJ, Antonopoulou E, Stead D, Martin SAM (2017) Postprandial hepatic protein expression in trout Oncorhynchus mykiss a proteomics examination. Biochem Biophys Rep 9:79–85. https://doi.org/10.1016/j.bbrep.2016.10.012
Micallef G, Cash P, Fernandes JM, Rajan B, Tinsley JW, Bickerdike R, Martin SA, Bowman AS (2017) Dietary yeast cell wall extract alters the proteome of the skin mucous barrier in Atlantic salmon (Salmo salar): increased abundance and expression of a calreticulin-like protein. PLoS One 12(1):e0169075. https://doi.org/10.1371/journal.pone.0169075
Moghadam H, Morkore T, Robinson N (2015) Epigenetics—potential for programming fish for aquaculture. J Mar Sci Eng 3:175–192. https://doi.org/10.3390/jmse3020175
Nakamura R, Satoh R, Nakajima Y, Kawasaki N, Yamaguchi T, Sawada J, Nagoya H, Teshima R (2009) Comparative study of GH-transgenic and non-transgenic amago salmon (Oncorhynchus masou ishikawae) allergenicity and proteomic analysis of amago salmon allergens. Regul Toxicol Pharmacol 55(3):300–308. https://doi.org/10.1016/j.yrtph.2009.08.002
Nuez-Ortín WG, Carter CG, Wilson R, Cooke I, Nichols PD (2016) Preliminary validation of a high Docosahexaenoic acid (DHA) and -Linolenic acid (ALA) dietary oil blend: tissue fatty acid composition and liver proteome response in Atlantic salmon (Salmo salar) Smolts. PLoS One 11(8):e0161513. https://doi.org/10.1371/journal.pone.0161513
Oskoueian E, Eckersall PD, Bencurova E, Dandekar T (2016) Application of proteomic biomarkers in livestock disease management. In: Salekdeh GH (ed) Agricultural proteomics, Environmental stresses, vol 2. Springer, Cham, pp 299–310. https://doi.org/10.1007/978-3-319-43278-6_14
Panhuis TM, Broitman-Maduro G, Uhrig J, Maduro M, Reznick DN (2011) Analysis of expressed sequence tags from the placenta of the live-bearing fish Poeciliopsis (Poeciliidae). J Hered. https://doi.org/10.1093/jhered/esr002
Park SB, Aoki T, Jung TS (2012) Pathogenesis of and strategies for preventing Edwardsiella tarda infection in fish. Vet Res 43(1):67. https://doi.org/10.1186/1297-9716-43-67
Parrington J, Coward K (2002) Use of emerging genomic and proteomic technologies in fish physiology. Aquat Living Resour 15(3):193–196
Peatman E, Baoprasertkul P, Terhune J, Xu P, Nandi S, Kucuktas H, Li P, Wang S, Somridhivej B, Dunham R, Liu Z (2007) Expression analysis of the acute phase response in channel catfish (Ictalurus punctatus) after infection with a Gram-negative bacterium. Dev Comp Immunol 31(11):1183–1196. https://doi.org/10.1016/j.dci.2007.03.003
Peng X-X (2013) Proteomics and its applications to aquaculture in China: infection, immunity, and interaction of aquaculture hosts with pathogens. Dev Comp Immunol 39(1–2):63–71. https://doi.org/10.1016/j.dci.2012.03.017
Picotti P, Bodenmiller B, Mueller LN, Domon B, Aebersold R (2009) Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics. Cell 138(4):795–806. https://doi.org/10.1016/j.cell.2009.05.051
Pineiro C, Vazquez J, Marina AI, Barros-Velazquez J, Gallardo JM (2001) Characterization and partial sequencing of species-specific sarcoplasmic polypeptides from commercial hake species by mass spectrometry following two-dimensional electrophoresis. Electrophoresis 22(8):1545–1552. https://doi.org/10.1002/1522-2683(200105)22:8<1545::Aid-Elps1545>3.0.Co;2-5
Piovesana S, Capriotti AL, Caruso G, Cavaliere C, La Barbera G, Zenezini Chiozzi R, Lagana A (2016) Labeling and label free shotgun proteomics approaches to characterize muscle tissue from farmed and wild gilthead sea bream (Sparus aurata). J Chromatogr A 1428:193–201. https://doi.org/10.1016/j.chroma.2015.07.049
Ponnerassery SS, Benjamin RL, Douglas RC, William FS, Scott EL, Gregory DW, Kenneth DC (2007) Identification of potential vaccine target antigens by immunoproteomic analysis of a virulent and a non-virulent strain of the fish pathogen Flavobacterium psychrophilum. Dis Aquat Org 74(1):37–47
Provan F, Jensen LB, Uleberg KE, Larssen E, Rajalahti T, Mullins J, Obach A (2013) Proteomic analysis of epidermal mucus from sea lice–infected Atlantic salmon, Salmo salar L. J Fish Dis 36(3):311–321. https://doi.org/10.1111/jfd.12064
Prunet P, Øverli Ø, Douxfils J, Bernardini G, Kestemont P, Baron D (2012) Fish welfare and genomics. Fish Physiol Biochem 38(1):43–60. https://doi.org/10.1007/s10695-011-9522-z
Purushothaman S, Saxena S, Meghah V, Meena Lakshmi MG, Singh SK, Brahmendra Swamy CV, Idris MM (2015) Proteomic and gene expression analysis of zebrafish brain undergoing continuous light/dark stress. J Sleep Res 24(4):458–465. https://doi.org/10.1111/jsr.12287
Qian X, Ba Y, Zhuang Q, Zhong G (2014) RNA-Seq technology and its application in fish transcriptomics. Omics: J Integr Biol 18(2):98–110. https://doi.org/10.1089/omi.2013.0110
Quinn NL, Gutierrez AP, Koop BF, Davidson WS (2012) Genomics and genome sequencing: benefits for finfish aquaculture. INTECH Open Access Publisher
Rasmussen RS, Morrissey MT (2008) DNA-Based methods for the identification of commercial fish and seafood species. Compr Rev Food Sci Food Saf 7(3):280–295. https://doi.org/10.1111/j.1541-4337.2008.00046.x
Richard N, Fernández I, Wulff T, Hamre K, Cancela L, Conceição LEC, Gavaia PJ (2014) Dietary supplementation with vitamin K affects transcriptome and proteome of Senegalese Sole, improving larval performance and quality. Mar Biotechnol 16(5):522–537. https://doi.org/10.1007/s10126-014-9571-2
Richard N, Silva TS, Wulff T, Schrama D, Dias JP, Rodrigues PML, Conceição LEC (2016) Nutritional mitigation of winter thermal stress in gilthead seabream: associated metabolic pathways and potential indicators of nutritional state. J Proteome 142:1–14. https://doi.org/10.1016/j.jprot.2016.04.037
Rodrigues PM, Silva TS, Dias J, Jessen F (2012) Proteomics in aquaculture: applications and trends. J Proteome 75(14):4325–4345. https://doi.org/10.1016/j.jprot.2012.03.042
Rodrigues PM, Schrama D, Campos A, Osório H, Freitas M (2016) Applications of proteomics in aquaculture. In: Salekdeh GH (ed) Agricultural proteomics, Crops, horticulture, farm animals, food, insect and microorganisms, vol 1. Springer, Cham, pp 165–199. https://doi.org/10.1007/978-3-319-43275-5_10
Rossi F, Chini V, Cattaneo AG, Bernardini G, Terova G, Saroglia M, Gornati R (2007) EST-based identification of genes expressed in perch (Perca fluviatilis, L.) Gene Expr 14(2):117–127. https://doi.org/10.3727/105221607783417600
Rufino-Palomares E, Reyes-Zurita FJ, Fuentes-Almagro CA, de la Higuera M, Lupianez JA, Peragon J (2011) Proteomics in the liver of gilthead sea bream (Sparus aurata) to elucidate the cellular response induced by the intake of maslinic acid. Proteomics 11(16):3312–3325. https://doi.org/10.1002/pmic.201000271
Russell S, Hayes MA, Simko E, Lumsden JS (2006) Plasma proteomic analysis of the acute phase response of rainbow trout (Oncorhynchus mykiss) to intraperitoneal inflammation and LPS injection. Dev Comp Immunol 30(4):393–406. https://doi.org/10.1016/j.dci.2005.06.002
Salas-Leiton E, Cánovas-Conesa B, Zerolo R, López-Barea J, Cañavate JP, Alhama J (2009) Proteomics of Juvenile Senegal Sole (Solea senegalensis) affected by gas bubble disease in hyperoxygenated ponds. Mar Biotechnol 11(4):473–487. https://doi.org/10.1007/s10126-008-9168-8
Salem M, Paneru B, Al-Tobasei R, Abdouni F, Thorgaard GH, Rexroad CE, Yao J (2015) Transcriptome assembly, gene annotation and tissue gene expression atlas of the rainbow trout. PLoS One 10(3):e0121778. https://doi.org/10.1371/journal.pone.0121778
Santos GA, Schrama JW, Mamauag REP, Rombout JHWM, Verreth JAJ (2010) Chronic stress impairs performance, energy metabolism and welfare indicators in European seabass (Dicentrarchus labrax): the combined effects of fish crowding and water quality deterioration. Aquaculture 299(1–4):73–80. https://doi.org/10.1016/j.aquaculture.2009.11.018
Saptarshi SR, Sharp MF, Kamath SD, Lopata AL (2014) Antibody reactivity to the major fish allergen parvalbumin is determined by isoforms and impact of thermal processing. Food Chem 148:321–328. https://doi.org/10.1016/j.foodchem.2013.10.035
Satoh TP, Miya M, Mabuchi K, Nishida M (2016) Structure and variation of the mitochondrial genome of fishes. BMC Genomics 17(1):719. https://doi.org/10.1186/s12864-016-3054-y
Schrama D, Richard N, Silva TS, Figueiredo FA, Conceição LEC, Burchmore R, Eckersall D, Rodrigues PML (2016) Enhanced dietary formulation to mitigate winter thermal stress in gilthead sea bream (Sparus aurata): a 2D-DIGE plasma proteome study. Fish Physiol Biochem. https://doi.org/10.1007/s10695-016-0315-2
Shinn AP, Pratoomyot J, Bron JE, Paladini G, Brooker EE, Brooker AJ (2015) Economic costs of protistan and metazoan parasites to global mariculture. Parasitology 142(Special Issue 01):196–270. https://doi.org/10.1017/S0031182014001437
Siciliano RA, d’Esposito D, Mazzeo MF (2016) Food authentication by MALDI MS: MALDI-TOF MS analysis of fish species. In: Cramer R (ed) Advances in MALDI and laser-induced soft ionization mass spectrometry. Springer, Cham, pp 263–277. https://doi.org/10.1007/978-3-319-04819-2_14
Silva TS, Cordeiro O, Richard N, Conceicao LE, Rodrigues PM (2011) Changes in the soluble bone proteome of reared white seabream (Diplodus sargus) with skeletal deformities. Comp Biochem Physiol Part D Genomics Proteomics 6(1):82–91. https://doi.org/10.1016/j.cbd.2010.03.008
Silva TS, Matos E, Cordeiro OD, Colen R, Wulff T, Sampaio E, Sousa V, Valente LMP, Gonçalves A, Silva JMG, Bandarra N, Nunes ML, Dinis MT, Dias J, Jessen F, Rodrigues PM (2012) Dietary tools to modulate glycogen storage in gilthead seabream muscle: glycerol supplementation. J Agric Food Chem 60(42):10613–10624. https://doi.org/10.1021/jf3023244
Silva TS, da Costa AM, Conceicao LE, Dias JP, Rodrigues PM, Richard N (2014a) Metabolic fingerprinting of gilthead seabream (Sparus aurata) liver to track interactions between dietary factors and seasonal temperature variations. PeerJ 2:e527. https://doi.org/10.7717/peerj.527
Silva TS, Richard N, Dias JP, Rodrigues PM (2014b) Data visualization and feature selection methods in gel-based proteomics. Curr Protein Pept Sci 15(1):4–22. https://doi.org/10.2174/1389203715666140221112334
Silvestre F, Linares-Casenave J, Doroshov SI, Kültz D (2010) A proteomic analysis of green and white sturgeon larvae exposed to heat stress and selenium. Sci Total Environ 408(16):3176–3188. https://doi.org/10.1016/j.scitotenv.2010.04.005
Sissener NH (2009) Genetically modified plants as fish feed ingredients. Roundup Ready® soy, MON810 maize, Atlantic salmon, zebrafish
Sissener NH, Martin SAM, Cash P, Hevrøy EM, Sanden M, Hemre G-I (2010) Proteomic profiling of liver from Atlantic salmon (Salmo salar) fed genetically modified soy compared to the near-isogenic non-GM line. Mar Biotechnol 12(3):273–281. https://doi.org/10.1007/s10126-009-9214-1
Sletten G, Van Do T, Lindvik H, Egaas E, Florvaag E (2010) Effects of industrial processing on the immunogenicity of commonly ingested fish species. Int Arch Allergy Immunol 151(3):223–236
Smith RW, Cash P, Ellefsen S, Nilsson GE (2009) Proteomic changes in the crucian carp brain during exposure to anoxia. Proteomics 9(8):2217–2229. https://doi.org/10.1002/pmic.200800662
Smith RW, Wang J, Mothersill CE, Lee LEJ, Seymour CB (2015) Proteomic responses in the gills of fathead minnows (Pimephales promelas, Rafinesque, 1820) after 6 months and 2 years of continuous exposure to environmentally relevant dietary 226Ra. Int J Radiat Biol 91(3):248–256. https://doi.org/10.3109/09553002.2014.988894
Spaink HP, Jansen HJ, Dirks RP (2014) Advances in genomics of bony fish. Brief Funct Genomics 13(2):144–156. https://doi.org/10.1093/bfgp/elt046
Srinivasa Rao PS, Yamada Y, Tan YP, Leung KY (2004) Use of proteomics to identify novel virulence determinants that are required for Edwardsiella tarda pathogenesis. Mol Microbiol 53(2):573–586. https://doi.org/10.1111/j.1365-2958.2004.04123.x
Stentiford GD, Viant MR, Ward DG, Johnson PJ, Martin A, Wenbin W, Cooper HJ, Lyons BP, Feist SW (2005) Liver tumors in wild Flatfish: a histopathological, proteomic, and metabolomic study. OMICS 9(3):281–299. https://doi.org/10.1089/omi.2005.9.281
Sun F, Liu S, Gao X, Jiang Y, Perera D, Wang X, Li C, Sun L, Zhang J, Kaltenboeck L, Dunham R, Liu Z (2013) Male-biased genes in catfish as revealed by RNA-Seq analysis of the testis transcriptome. PLoS One 8(7):e68452. https://doi.org/10.1371/journal.pone.0068452
Sveinsdóttir H, Steinarsson A, Gudmundsdóttir Á (2009) Differential protein expression in early Atlantic cod larvae (Gadus morhua) in response to treatment with probiotic bacteria. Comp Biochem Physiol Part D Genomics Proteomics 4(4):249–254. https://doi.org/10.1016/j.cbd.2009.06.001
Swoboda I, Bugajska-Schretter A, Verdino P, Keller W, Sperr WR, Valent P, Valenta R, Spitzauer S (2002) Recombinant carp parvalbumin, the major cross-reactive fish allergen: a tool for diagnosis and therapy of fish allergy. J Immunol 168(9):4576–4584
Tedesco S, Mullen W, Cristobal S (2014) High-throughput proteomics: a new tool for quality and safety in fishery products. Curr Protein Pept Sci 15(2):118–133
Teklemariam AD, Tessema F, Abayneh T (2015) Review on evaluation of safety of fish and fish products. Int J Fish Aquat Stud 3(2):111–117
Tomm JM, van Do T, Jende C, Simon JC, Treudler R, von Bergen M, Averbeck M (2013) Identification of new potential allergens from nile perch (Lates niloticus) and cod (Gadus morhua). J Investig Allergol Clin Immunol 23(3):159–167
Varó I, Rigos G, Navarro JC, del Ramo J, Calduch-Giner J, Hernández A, Pertusa J, Torreblanca A (2010) Effect of ivermectin on the liver of gilthead sea bream Sparus aurata: a proteomic approach. Chemosphere 80(5):570–577. https://doi.org/10.1016/j.chemosphere.2010.04.030
Vasanth G, Kiron V, Kulkarni A, Dahle D, Lokesh J, Kitani Y (2015) A microbial feed additive abates intestinal inflammation in Atlantic salmon. Front Immunol 6:409. https://doi.org/10.3389/fimmu.2015.00409
Veiseth-Kent E, Pedersen ME, Hollung K, Ytteborg E, Bæverfjord G, Takle H, Åsgård TE, Ørnsrud R, Lock E-J, Albrektsen S (2013) Changes in protein abundance in the vertebral column of Atlantic salmon (Salmo salar) fed variable dietary P levels. In: de Almeida A, Eckersall D, Bencurova E et al (eds) Farm animal proteomics 2013. Wageningen Academic, Wageningen, pp 188–191. https://doi.org/10.3920/978-90-8686-776-9_48
Vilhelmsson OT, Martin SAM, Medale F, Kaushik SJ, Houlihan DF (2004) Dietary plant-protein substitution affects hepatic metabolism in rainbow trout (Oncorhynchus mykiss). Br J Nutr 92(1):71–80. https://doi.org/10.1079/Bjn20041176
Wenne R, Boudry P, Hemmer-Hansen J, Lubieniecki KP, Was A, Kause A (2007) What role for genomics in fisheries management and aquaculture? Aquat Living Resour 20(3):241–255. https://doi.org/10.1051/alr:2007037
Williams TD, Mirbahai L, Chipman JK (2014) The toxicological application of transcriptomics and epigenomics in zebrafish and other teleosts. Brief Funct Genomics 13(2):157–171. https://doi.org/10.1093/bfgp/elt053
Wu Y, Wang S, Peng X (2004) Serum acute phase response (APR)-related proteome of loach to trauma. Fish Shellfish Immunol 16(3):381–389. https://doi.org/10.1016/j.fsi.2003.06.003
Wulff T, Jokumsen A, Hojrup P, Jessen F (2012) Time-dependent changes in protein expression in rainbow trout muscle following hypoxia. J Proteome 75(8):2342–2351. https://doi.org/10.1016/j.jprot.2012.02.010
Xing M, Hou Z, Yuan J, Liu Y, Qu Y, Liu B (2013) Taxonomic and functional metagenomic profiling of gastrointestinal tract microbiome of the farmed adult turbot (Scophthalmus maximus). FEMS Microbiol Ecol 86(3):432–443. https://doi.org/10.1111/1574-6941.12174
Xiong X-P, Dong C-F, Xu X, Weng S-P, Liu Z-Y, He J-G (2011) Proteomic analysis of zebrafish (Danio rerio) infected with infectious spleen and kidney necrosis virus. Dev Comp Immunol 35(4):431–440. https://doi.org/10.1016/j.dci.2010.11.006
Yadetie F, Bjørneklett S, Garberg HK, Oveland E, Berven F, Goksøyr A, Karlsen OA (2016) Quantitative analyses of the hepatic proteome of methylmercury-exposed Atlantic cod (Gadus morhua) suggest oxidative stress-mediated effects on cellular energy metabolism. BMC Genomics 17(1):554. https://doi.org/10.1186/s12864-016-2864-2
Ye C-X, Wan F, Sun Z-Z, Cheng C-H, Ling R-Z, Fan L-F, Wang A-L (2016) Effect of phosphorus supplementation on cell viability, anti-oxidative capacity and comparative proteomic profiles of puffer fish (Takifugu obscurus) under low temperature stress. Aquaculture 452:200–208. https://doi.org/10.1016/j.aquaculture.2015.10.039
Zhou S, Wan Q, Huang Y, Huang X, Cao J, Ye L, Lim T-K, Lin Q, Qin Q (2011) Proteomic analysis of Singapore grouper iridovirus envelope proteins and characterization of a novel envelope protein VP088. Proteomics 11(11):2236–2248. https://doi.org/10.1002/pmic.200900820
Zhou X, Ding Y, Wang Y (2012) Proteomics: present and future in fish, shellfish and seafood. Rev Aquac 4(1):11–20. https://doi.org/10.1111/j.1753-5131.2012.01058.x
Acknowledgments
Rodrigues’s lab was supported by project ALG-01-0247-FEDER-003520—ALISSA—Healthy and sustainable feeds for farmed fish, supported by Portugal and the European Union through FEDER, COMPETE 2020, and CRESC Algarve 2020, in the framework of Portugal 2020. Denise Schrama acknowledges scholarship on project ALG-01-0247-FEDER-003520—ALISSA—Healthy and sustainable feeds for farmed fish, supported by Portugal and the European Union through FEDER, COMPETE 2020, and CRESC Algarve 2020, in the framework of Portugal 2020. Márcio Moreira was financially supported by BONAQUA (0433_BONAQUA_5_E) and DIVERSIAQUA projects. Marcelo Sousa (MarceloArt84) for the artwork.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer International Publishing AG
About this chapter
Cite this chapter
Rodrigues, P.M. et al. (2018). Proteomics in Fish and Aquaculture Research. In: de Almeida, A., Eckersall, D., Miller, I. (eds) Proteomics in Domestic Animals: from Farm to Systems Biology. Springer, Cham. https://doi.org/10.1007/978-3-319-69682-9_16
Download citation
DOI: https://doi.org/10.1007/978-3-319-69682-9_16
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-69681-2
Online ISBN: 978-3-319-69682-9
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)