1 Fritvold, C. & Jensen, B. B. Cardiomyopathy syndrome (CMS). 52-55 (Norwegian Veterinary Institute, Norway, 2019).
2 Fritvold, C. Cardiomyopathy syndrome (CMS). 30-31 (The Norwegian Veterinary Institute, Norway, 2016).
3 Garseth, A. H., Fritsvold, C., Svendsen, J. C., Bang Jensen, B. & Mikalsen, A. B. Cardiomyopathy syndrome in Atlantic salmon Salmo salar L.: A review of the current state of knowledge. J Fish Dis41, 11-26, doi:10.1111/jfd.12735 (2018).
4 Ferguson, H. W., Poppe, T. & Speare, D. J. Cardiomyopathy in farmed Norwegian salmon. Dis Aquat Organ8, 225-231 (1990).
5 Brun, E., Poppe, T., A., S. & Jarp, J. Cardiomyopathy syndrome in farmed Atlantic salmon Salmo salar: occurrence and direct financial losses for Norwegian aquaculture Dis Aquat Organ56, 214-247 (2003).
6 Amin, A. B. & Trasti, J. Endomyocarditis in atlantic salmon in Norwegian seafarms. A case report. Bull. Eur. Assoc. Fish Pathol.8, 70-71 (1988).
7 Poppe, T. T. & Seierstad, S. L. First description of cardiomyopathy syndrome (CMS)-related lesions in wild Atlantic salmon Salmo salar in Norway. Dis Aquat Organ56, 87-88 (2003).
8 Rodger, H. D., McCleary, S. J. & Ruane, N. M. Clinical cardiomyopathy syndrome in Atlantic salmon, Salmo salar L. J Fish Dis37, 935-939, doi:10.1111/jfd.12186 (2014).
9 Bruno, D. W. & Noguera, P. A. Comparative experimental transmission of cardiomyopathy syndrome (CMS) in Atlantic salmon Salmo salar. Dis Aquat Organ87, 235-242, doi:10.3354/dao02129 (2009).
10 Fritsvold, C. et al. Experimental transmission of cardiomyopathy syndrome (CMS) in Atlantic salmon Salmo salar. Dis Aquat Organ87, 225-234, doi:10.3354/dao02123 (2009).
11 Løvoll, M. et al. A novel totivirus and piscine reovirus (PRV) in Atlantic salmon (Salmo salar) with cardiomyopathy syndrome (CMS). Virol J7, 309, doi:10.1186/1743-422X-7-309 (2010).
12 Haugland, O. et al. Cardiomyopathy syndrome of atlantic salmon (Salmo salar L.) is caused by a double-stranded RNA virus of the Totiviridae family. J Virol85, 5275-5286, doi:10.1128/JVI.02154-10 (2011).
13 Mayeux, R. Biomarkers potential uses and limitations. NeuroRx1, 182-188, doi:10.1602/neurorx.1.2.182 (2004).
14 Rodger, H. D., Murphy, T. M., Drinan, E. M. & Rice, D. A. Acute skeletal myopathy in farmed Atlantic salmon Salmo salar. Dis Aquat Organ12, 17-23 (1991).
15 Yousaf, M. N. & Powell, M. D. The effects of heart and skeletal muscle inflammation and cardiomyopathy syndrome on creatine kinase and lactate dehydrogenase levels in Atlantic salmon (Salmo salar L.). Scientific World Journal2012, 741302, doi:10.1100/2012/741302 (2012).
16 Rojas, V. et al. Detection of muscle-specific creatine kinase expression as physiological indicator for Atlantic salmon (Salmo salar L.) skeletal muscle damage. Aquaculture496, 66-72, doi:10.1016/j.aquaculture.2018.07.006 (2018).
17 Barbosa, E. B. et al. Proteomics: methodologies and applications to the study of human diseases. Rev Assoc Med Bras58, 366-375, doi:10.1016/s2255-4823(12)70209-6 (2012).
18 Byrnes, S. A. & Weigl, B. H. Selecting analytical biomarkers for diagnostic applications: a first principles approach. Expert Rev Mol Diagn18, 19-26, doi:10.1080/14737159.2018.1412258 (2018).
19 Ahrens, C. H., Brunner, E., Qeli, E., Basler, K. & Aebersold, R. Generating and navigating proteome maps using mass spectrometry. Nat Rev Mol Cell Biol11, 789-801, doi:10.1038/nrm2973 (2010).
20 Geyer, P. E., Holdt, L. M., Teupser, D. & Mann, M. Revisiting biomarker discovery by plasma proteomics. Mol Syst Biol13, 942, doi:10.15252/msb.20156297 (2017).
21 Banerjee, S. et al. Identification of potential biomarkers of hepatotoxicity by plasma proteome analysis of arsenic-exposed carp Labeo rohita. J Hazard Mater336, 71-80, doi:10.1016/j.jhazmat.2017.04.054 (2017).
22 Alderman, S. L., Dindia, L. A., Kennedy, C. J., Farrell, A. P. & Gillis, T. E. Proteomic analysis of sockeye salmon serum as a tool for biomarker discovery and new insight into the sublethal toxicity of diluted bitumen. Comp Biochem Physiol Part D Genomics Proteomics22, 157-166, doi:10.1016/j.cbd.2017.04.003 (2017).
23 Smith, J. G. & Gerszten, R. E. Emerging Affinity-Based Proteomic Technologies for Large-Scale Plasma Profiling in Cardiovascular Disease. Circulation135, 1651-1664, doi:10.1161/CIRCULATIONAHA.116.025446 (2017).
24 Group, B. D. W. Biomarkers and surrogate endpoints: preferred definitions and conceptual framework. Clin Pharmacol Ther69, 89-95, doi:10.1067/mcp.2001.113989 (2001).
25 Zhou, B. et al. Plasma proteomics-based identification of novel biomarkers in early gastric cancer. Clin Biochem76, 5-10, doi:10.1016/j.clinbiochem.2019.11.001 (2020).
26 Kemp, M., Donovan, J., Higham, H. & Hooper, J. Biochemical markers of myocardial injury. Br J Anaesth93, 63-73, doi:10.1093/bja/aeh148 (2004).
27 Lippi, G., Mattiuzzi, C., Comelli, I. & Cervellin, G. Glycogen phosphorylase isoenzyme BB in the diagnosis of acute myocardial infarction: a meta-analysis. Biochem Med (Zagreb)23, 78-82, doi:10.11613/bm.2013.010 (2013).
28 Bodor, G. S. Biochemical markers of myocardial damage. EJIFCC27, 95-112 (2016).
29 Cabaniss, C. D. in Clinical methods: The history, physical, and laboratory examinations (eds H.K. Walker, W.D. Hall, & J.W. Hurst) Ch. 32, (Butterworths, 1990).
30 Braceland, M. et al. The serum proteome of Atlantic salmon, Salmo salar, during pancreas disease (PD) following infection with salmonid alphavirus subtype 3 (SAV3). J Proteomics94, 423-436, doi:10.1016/j.jprot.2013.10.016 (2013).
31 Khan, A. A., Allemailem, K. S., Alhumaydhi, F. A., Gowder, S. J. T. & Rahmani, A. H. The biochemical and clinical perspectives of lactate dehydrogenase: an enzyme of active metabolism. Endocr Metab Immune Disord Drug Targets20, 855-868, doi:10.2174/1871530320666191230141110 (2020).
32 Klein, R., Nagy, O., Tóthová, C. & Chovanová, F. Clinical and Diagnostic Significance of Lactate Dehydrogenase and Its Isoenzymes in Animals. Vet. Med. Int.2020, 5346483, doi:10.1155/2020/5346483 (2020).
33 Oliveira, R. et al. Effects of oxytetracycline and amoxicillin on development and biomarkers activities of zebrafish (Danio rerio). Environ. Toxicol. Pharmacol.36, 903-912, doi:https://doi.org/10.1016/j.etap.2013.07.019 (2013).
34 Ajima, M. N. O., Ogo, O. A., Audu, B. S. & Ugwoegbu, K. C. Chronic diclofenac (DCF) exposure alters both enzymatic and haematological profile of African catfish, Clarias gariepinus. Drug Chem. Toxicol.38, 383-390, doi:10.3109/01480545.2014.974108 (2015).
35 Elia, A. C. et al. Oxidative stress and related biomarkers in cupric and cuprous chloride-treated rainbow trout. Environ Sci Pollut Res Int24, 10205-10219, doi:10.1007/s11356-017-8651-z (2017).
36 Kumar, S. et al. Effects on haematological and serum biochemical parameters of Pangasianodon hypophthalmus to an experimental infection of Thaparocleidus sp. (Monogenea: dactylogyridae). Experimental Parasitology188, 1-7, doi:https://doi.org/10.1016/j.exppara.2018.02.007 (2018).
37 David, E. S. & Crerar, M. M. Quantitation of muscle glycogen phosphorylase mRNA and enzyme amounts in adult rat tissues. Biochim Biophys Acta Gen Subj880, 78-90, doi:https://doi.org/10.1016/0304-4165(86)90122-4 (1986).
38 Zhu, Y. & Gius, D. Glycogen Phosphorylase: A Novel Biomarker in Doxorubicin-Induced Cardiac Injury. Clin Cancer Res24, 1516-1517, doi:10.1158/1078-0432.CCR-17-3276 (2018).
39 Sundby, A., Hemre, G.-I., Borrebaek, B., Christophersen, B. & Blom, A. K. Insulin and glucagon family peptides in relation to activities of hepatic hexokinase and other enzymes in fed and starved Atlantic salmon (Salmo salar) and cod (Gadus morhua). Comp Biochem Physiol Part B: Comp Biochem100, 467-470, doi:https://doi.org/10.1016/0305-0491(91)90205-R (1991).
40 Begum, G. Enzymes as biomarkers of cypermethrin toxicity: response of Clarias batrachus tissues ATPase and glycogen phosphorylase as a function of exposure and recovery at sublethal level. Toxicol. Mech. Methods19, 29-39, doi:10.1080/15376510802205650 (2009).
41 Lindskog, S. Structure and mechanism of carbonic anhydrase. Pharmacol. Ther.74, 1-20, doi:https://doi.org/10.1016/S0163-7258(96)00198-2 (1997).
42 Zamanova, S., Shabana, A. M., Mondal, U. K. & Ilies, M. A. Carbonic anhydrases as disease markers. Expert Opin. Ther. Pat.29, 509-533, doi:10.1080/13543776.2019.1629419 (2019).
43 Vuotikka, P. et al. Serum Myoglobin/Carbonic Anhydrase III Ratio in the Diagnosis of Perioperative Myocardial Infarction During Coronary Bypass Surgery. Scand. Cardiovasc. J.37, 23-29, doi:10.1080/14017430310006992 (2003).
44 Alderman, S. L. et al. Evidence for a plasma-accessible carbonic anhydrase in the lumen of salmon heart that may enhance oxygen delivery to the myocardium. J Exp Biol219, 719-724, doi:10.1242/jeb.130443 (2016).
45 Latimer, K. S. Duncan and Prasse's veterinary laboratory medicine: clinical pathology. 5 edn, 178-179 (Wiley-Blackwell 2011).
46 Kumar, V., Abbas, A. K. & Aster, J. C. Robbins & Cotran pathologic basis of disease. 88-89 (Elsevier 2014).
47 Andersen, C. B. et al. Structure of the haptoglobin-haemoglobin complex. Nature489, 456-459, doi:10.1038/nature11369 (2012).
48 Nirala, N. R., Harel, Y., Lellouche, J.-P. & Shtenberg, G. Ultrasensitive haptoglobin biomarker detection based on amplified chemiluminescence of magnetite nanoparticles. J. Nanobiotechnology18, 6, doi:10.1186/s12951-019-0569-9 (2020).
49 Holme, I., Aastveit, A. H., Hammar, N., Jungner, I. & Walldius, G. Haptoglobin and risk of myocardial infarction, stroke, and congestive heart failure in 342,125 men and women in the Apolipoprotein MOrtality RISk study (AMORIS). Ann. Med.41, 522-532, doi:10.1080/07853890903089453 (2009).
50 Haas, B. et al. Proteomic analysis of plasma samples from patients with acute myocardial infarction identifies haptoglobin as a potential prognostic biomarker. J. Proteom.75, 229-236, doi:https://doi.org/10.1016/j.jprot.2011.06.028 (2011).
51 Cordero, H., Li, C. H., Chaves-Pozo, E., Esteban, M. Á. & Cuesta, A. Molecular identification and characterization of haptoglobin in teleosts revealed an important role on fish viral infections. Dev Comp Immunol76, 189-199, doi:https://doi.org/10.1016/j.dci.2017.06.006 (2017).
52 Valenzuela-Muñoz, V., Boltaña, S. & Gallardo-Escárate, C. Uncovering iron regulation with species-specific transcriptome patterns in Atlantic and coho salmon during a Caligus rogercresseyi infestation. J. Fish Dis.40, 1169-1184, doi:10.1111/jfd.12592 (2017).
53 Jain, S., Gautam, V. & Naseem, S. Acute-phase proteins: As diagnostic tool. J. Pharm. Bioallied Sci.3, 118-127, doi:10.4103/0975-7406.76489 (2011).
54 Weisel, J. W. et al. The shape of high molecular weight kininogen. Organization into structural domains, changes with activation, and interactions with prekallikrein, as determined by electron microscopy. J Biol Chem269, 10100-10106 (1994).
55 Wong, M. K. S. in Handbook of Hormones (eds Yoshio Takei, Hironori Ando, & Kazuyoshi Tsutsui) 268-e230A-263 (Academic Press, 2016).
56 Wu, Q., Kuo, H. C. & Deng, G. G. Serine proteases and cardiac function. Biochim Biophys Acta1751, 82-94, doi:10.1016/j.bbapap.2004.09.005 (2005).
57 Patel, S. A critical review on serine protease: Key immune manipulator and pathology mediator. Allergol Immunopathol (Madr)45, 579-591, doi:10.1016/j.aller.2016.10.011 (2017).
58 de Boer, J. P. et al. Alpha-2-macroglobulin functions as an inhibitor of fibrinolytic, clotting, and neutrophilic proteinases in sepsis: studies using a baboon model. Infect Immun61, 5035-5043, doi:10.1128/IAI.61.12.5035-5043.1993 (1993).
59 Ramasamy, S. et al. Cardiac isoform of alpha 2 macroglobulin, an early diagnostic marker for cardiac manifestations in AIDS patients. AIDS20 (2006).
60 Yoshino, S. et al. Molecular form and concentration of serum α2-macroglobulin in diabetes. Sci. Rep.9, 12927, doi:10.1038/s41598-019-49144-7 (2019).
61 Soman, S., Manju, C. S., Rauf, A. A., Indira, M. & Rajamanickam, C. Role of cardiac isoform of alpha-2 macroglobulin in diabetic myocardium. Mol Cell Biochem350, 229-235, doi:10.1007/s11010-010-0702-4 (2011).
62 Salte, R., Norberg, K., Ødegaard, O. R., Arnesen, J. A. & Olli, J. J. Exotoxin-induced consumptive coagulopathy in Atlantic salmon, Salmo salar L.: inhibitory effects of exogenous antithrombin and α2-macroglobulin on Aeromonas salmonicida serine protease. J. Fish Dis.16, 425-435, doi:10.1111/j.1365-2761.1993.tb00876.x (1993).
63 Hellman, N. E. & Gitlin, J. D. Ceruloplasmin metabolism and function. Annu Rev Nutr22, 439-458, doi:10.1146/annurev.nutr.22.012502.114457 (2002).
64 Reunanen, A., Knekt, P. & Aaran, R. K. Serum ceruloplasmin level and the risk of myocardial infarction and stroke. Am J Epidemiol136, 1082-1090, doi:10.1093/oxfordjournals.aje.a116573 (1992).
65 Mänttäri, M. et al. Serum ferritin and ceruloplasmin as coronary risk factors. Eur Heart J15, 1599-1603, doi:10.1093/oxfordjournals.eurheartj.a060440 (1994).
66 Ziakas, A. et al. Ceruloplasmin is a better predictor of the long-term prognosis compared with fibrinogen, CRP, and IL-6 in patients with severe unstable angina. Angiology60, 50-59, doi:10.1177/0003319708314249 (2009).
67 Dadu, R. T. et al. Ceruloplasmin and heart failure in the Atherosclerosis Risk in Communities study. Circ Heart Fail6, 936-943, doi:10.1161/CIRCHEARTFAILURE.113.000270 (2013).
68 Xu, Y., Lin, H., Zhou, Y., Cheng, G. & Xu, G. Ceruloplasmin and the extent of heart failure in ischemic and nonischemic cardiomyopathy patients. Mediators Inflamm2013, 348145, doi:10.1155/2013/348145 (2013).
69 Andreasova, T. et al. Evaluation of ceruloplasmin - a potential biomarker in chronic heart failure. J. Clin. Exp. Cardiol.09, doi:10.4172/2155-9880.1000601 (2018).
70 Sahoo, P. K. et al. Characterization of the ceruloplasmin gene and its potential role as an indirect marker for selection to Aeromonas hydrophila resistance in rohu, Labeo rohita. Fish Shellfish Immunol34, 1325-1334, doi:10.1016/j.fsi.2013.02.020 (2013).
71 Hourcade, D. E., Mitchell, L. M. & Oglesby, T. J. A conserved element in the serine protease domain of complement factor B. J Biol Chem273, 25996-26000, doi:10.1074/jbc.273.40.25996 (1998).
72 Kulkarni, P. A. & Afshar-Kharghan, V. Anticomplement therapy. Biologics2, 671-685, doi:10.2147/btt.s2753 (2008).
73 Ricklin, D., Hajishengallis, G., Yang, K. & Lambris, J. D. Complement: a key system for immune surveillance and homeostasis. Nat Immunol11, 785-797, doi:10.1038/ni.1923 (2010).
74 Pankov, R. & Yamada, K. M. Fibronectin at a glance. J. Cell Sci.115, 3861-3863, doi:10.1242/jcs.00059 (2002).
75 Wang, J., Karra, R., Dickson, A. L. & Poss, K. D. Fibronectin is deposited by injury-activated epicardial cells and is necessary for zebrafish heart regeneration. Dev. Biol.382, 427-435, doi:https://doi.org/10.1016/j.ydbio.2013.08.012 (2013).
76 Liu, X. & Collodi, P. Novel form of fibronectin from zebrafish mediates infectious hematopoietic necrosis virus infection. J. Virol.76, 492-498, doi:10.1128/jvi.76.2.492-498.2002 (2002).
77 Liu, X., Zhao, Q. & Collodi, P. A truncated form of fibronectin is expressed in fish and mammals. Matrix Biol22, 393-396, doi:10.1016/s0945-053x(03)00071-4 (2003).
78 Bearzotti, M. et al. Fish Rhabdovirus Cell Entry Is Mediated by Fibronectin. J. Virol.73, 7703-7709, doi:10.1128/jvi.73.9.7703-7709.1999 (1999).
79 Chakravarti, S. et al. Lumican regulates collagen fibril assembly: skin fragility and corneal opacity in the absence of lumican. J Cell Biol141, 1277-1286, doi:10.1083/jcb.141.5.1277 (1998).
80 Engebretsen, K. V. T. et al. Lumican is increased in experimental and clinical heart failure, and its production by cardiac fibroblasts is induced by mechanical and proinflammatory stimuli. The FEBS Journal280, 2382-2398, doi:10.1111/febs.12235 (2013).
81 Mohammadzadeh, N. et al. The extracellular matrix proteoglycan lumican improves survival and counteracts cardiac dilatation and failure in mice subjected to pressure overload. Sci. Rep.9, 9206, doi:10.1038/s41598-019-45651-9 (2019).
82 Saleh, M. et al. Quantitative shotgun proteomics distinguishes wound-healing biomarker signatures in common carp skin mucus in response to Ichthyophthirius multifiliis. Vet Res49, 37, doi:10.1186/s13567-018-0535-9 (2018).
83 Kikuchi, K. et al. Retinoic acid production by endocardium and epicardium is an injury response essential for zebrafish heart regeneration. Dev Cell20, 397-404, doi:10.1016/j.devcel.2011.01.010 (2011).
84 Flower, D. R. The lipocalin protein family: structure and function. Biochem J318 ( Pt 1), 1-14, doi:10.1042/bj3180001 (1996).
85 Yndestad, A. et al. Increased systemic and myocardial expression of neutrophil gelatinase-associated lipocalin in clinical and experimental heart failure. Eur. Heart J.30, 1229-1236, doi:10.1093/eurheartj/ehp088 (2009).
86 Shevchenko, A., Wilm, M., Vorm, O. & Mann, M. Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels. Anal. Chem.68, 850-858, doi:10.1021/ac950914h (1996).
87 Batycka, M. et al. Ultra-fast tandem mass spectrometry scanning combined with monolithic column liquid chromatography increases throughput in proteomic analysis. Rapid Commun. Mass Spectrom.20, 2074-2080, doi:10.1002/rcm.2563 (2006).
88 Taylor, G. K. & Goodlett, D. R. Rules governing protein identification by mass spectrometry. Rapid Commun. Mass Spectrom.19, 3420-3420, doi:10.1002/rcm.2225 (2005).