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An update on medium- and low-abundant blood plasma proteome of horse

Published online by Cambridge University Press:  10 July 2017

A. Lepczyński ,
M. Ożgo ,
A. Dratwa-Chałupnik ,
P. Robak ,
A. Pyć ,
D. Zaborski  and
A. Herosimczyk
A. Lepczyński*
Affiliation:
Department of Physiology, Cytobiology and Proteomics, Faculty of Biotechnology and Animal Husbandry, West Pomeranian University of Technology Szczecin, Doktora Judyma 6, 71-466 Szczecin, Poland
M. Ożgo
Affiliation:
Department of Physiology, Cytobiology and Proteomics, Faculty of Biotechnology and Animal Husbandry, West Pomeranian University of Technology Szczecin, Doktora Judyma 6, 71-466 Szczecin, Poland
A. Dratwa-Chałupnik
Affiliation:
Department of Physiology, Cytobiology and Proteomics, Faculty of Biotechnology and Animal Husbandry, West Pomeranian University of Technology Szczecin, Doktora Judyma 6, 71-466 Szczecin, Poland
P. Robak
Affiliation:
Department of Physiology, Cytobiology and Proteomics, Faculty of Biotechnology and Animal Husbandry, West Pomeranian University of Technology Szczecin, Doktora Judyma 6, 71-466 Szczecin, Poland
A. Pyć
Affiliation:
Department of Physiology, Cytobiology and Proteomics, Faculty of Biotechnology and Animal Husbandry, West Pomeranian University of Technology Szczecin, Doktora Judyma 6, 71-466 Szczecin, Poland
D. Zaborski
Affiliation:
Laboratory of Biostatistics, Department of Ruminants Science, Faculty of Biotechnology and Animal Husbandry, West Pomeranian University of Technology Szczecin, Doktora Judyma 10, 71-466 Szczecin, Poland
A. Herosimczyk
Affiliation:
Department of Physiology, Cytobiology and Proteomics, Faculty of Biotechnology and Animal Husbandry, West Pomeranian University of Technology Szczecin, Doktora Judyma 6, 71-466 Szczecin, Poland
*
†E-mail: [email protected]
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Abstract

The main objectives of the study were to: (1) deeply analyse the serum protein composition of Equus caballus, (2) assess the effectiveness of the high-abundant protein depletion and improve the concentration of medium- and low-abundant proteins. The analysis were performed on the blood plasma of three healthy part-Arabian mares. The implementation of two-dimensional electrophoresis and matrix-assisted laser desorption/ionisation – time of flight mass spectrometry allowed us to establish a horse plasma proteome map. Serum proteins were resolved at pH 4 to 7, followed by 12% SDS-PAGE. As a result 136 spots were successfully identified, representing the products of 46 unique genes. Of these, 22 gene products have not been previously identified in horse serum/plasma samples using proteomic tools. Gene ontology analysis showed that almost 30% of all identified gene products belong to the coagulation and complement cascades. These results can undoubtedly serve as a useful and prospective prerequisite for the future analysis of horse plasma proteome changes in different physiological and pathophysiological conditions. The use of the medium- and low-abundant protein enrichment tool increased their abundance and allowed us to identify a higher number of protein gene products. The highest depletion efficiency was observed for the most abundant plasma proteins, that is albumin, IgG heavy chains and serotransferrin.

Keywords

two-dimensional electrophoresisMALDI-TOFproteomelow-abundant proteinblood
Type
Research Article
Information
animal , Volume 12 , Issue 1 , January 2018 , pp. 76 - 87
Copyright
© The Animal Consortium 2017 

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References

Amara, U, Flierl, MA, Rittirsch, D, Klos, A, Chen, H, Acker, B, Brückner, UB, Nilsson, B, Gebhard, F, Lambris, JD and Huber-Lang, M 2010. Molecular intercommunication between the complement and coagulation systems. Journal of Immunology 185, 5628–5636.Google Scholar
Anderson, NL and Anderson, NG 2002. The human plasma proteome: history, character, and diagnostic prospects. Molecular & Cellular Proteomics 1, 845–867.CrossRefGoogle ScholarPubMed
Argraves, WS, Greene, LM, Cooley, MA and Gallagher, WM 2003. Fibulins: physiological and disease perspectives. EMBO Reports 4, 1127–1131.Google Scholar
Arlaud, GJ, Gaboriaud, C, Thielens, NM, Rossi, V, Bersch, B, Hernandez, JF and Fontecilla-Camps, JC 2001. Structural biology of C1: dissection of a complex molecular machinery. Immunological Reviews 180, 136–145.Google Scholar
Beck, HC, Overgaard, M and Rasmussen, ML 2015. Plasma proteomics to identify biomarkers – application to cardiovascular diseases. Translational Proteomics 7, 40–48.Google Scholar
Bendixen, E, Danielsen, M, Hollung, K, Gianazza, E and Miller, I 2011. Farm animal proteomics-a review. Journal of Proteomics 74, 282–293.CrossRefGoogle ScholarPubMed
Bierl, C, Voetsch, B, Jin, RC, Handy, DE and Loscalzo, J 2004. Determinants of human plasma glutathione peroxidase (GPx-3) expression. The Journal of Biological Chemistry 279, 26839–26845.Google Scholar
Bouley, J, Chambon, C and Picard, B 2004. Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry. Proteomics 4, 1811–1824.Google Scholar
Chiaradia, E, Pepe, M, Tartaglia, M, Scoppetta, F, D’Ambrosio, C, Renzone, G, Avellini, L, Moriconi, F, Gaiti, A, Bertuglia, A, Beccati, F and Scaloni, A 2012. Gambling on putative biomarkers of osteoarthris and osteochondrisis by equine synovial fluid proteomics. Journal of Proteomics 75, 4478–4493.CrossRefGoogle Scholar
Citi, S, Pulimeno, P and Paschoud, S 2012. Cingulin, paracingulin, and PLEKHA7: signaling and cytoskeletal adaptors at the apical junctional complex. Annals of the New York Academy of Sciences 1257, 125–132.Google Scholar
Cooper, ST and Attie, AD 1992. Pig apolipoprotein R: a new member of the short consensus repeat family of proteins. Biochemistry 31, 12328–12336.Google Scholar
Deeg, MA, Bierman, EL and Cheung, MC 2001. GPI-specific phospholipase D associates with an apoA-I- and apoA-IV-containing complex. The Journal of Lipid Research 42, 442–451.Google Scholar
Di Girolamo, F, D’Amato, A, Lante, I, Signore, F, Muraca, M and Putignani, L 2014. Farm animal serum proteomics and impact on human health. International Journal of Molecular Sciences 15, 15396–15411.Google Scholar
Dominguez, R and Holmes, KC 2011. Actin structure and function. Annual Review of Biophysics 40, 169–186.Google Scholar
Ermert, D and Blom, AM 2016. C4b-binding protein: the good, the bad and the deadly. Novel functions of an old friend. Immunology Letters 169, 82–92.Google Scholar
Gianazza, E, Miller, I, Palazzolo, L, Parravicini, C and Eberini, I 2016. With or without you – proteomics with or without major plasma/serum proteins. Journal of Proteomics 140, 62–80.Google Scholar
Guerrier, L, Righetti, PG and Boschetti, E 2008. Reduction of dynamic protein concentration range of biological extracts for the discovery of low abundance proteins by means of hexapeptide ligand library. Nature Protocols 3, 883–890.CrossRefGoogle ScholarPubMed
Gunning, PW, Hardeman, EC, Lappalainen, P and Mulvihill, DP 2015. Tropomyosin – master regulator of actin filament function in the cytoskeleton. Journal of Cell Science 15, 2965–2974.Google Scholar
Hammond, JW, Cai, D and Verhey, KJ 2008. Tubulin modifications and their cellular functions. Current Opinion in Cell Biology 20, 71–76.Google Scholar
Hatters, DM, Peters-Libeu, CA and Weisgraber, KH 2006. Apolipoprotein E structure: insights into function. Trends in Biochemical Sciences 31, 445–454.Google Scholar
Henning, AK, Albrecht, D, Riedel, K, Mettenleiter, TC and Karger, A 2015. An alternative method for serum protein depletion/enrichment by precipitation at mildly acidic pH values and low ionic strength. Proteomics 15, 1935–1940.Google Scholar
Hierholzer, C and Billiar, TR 2001. Molecular mechanisms in the early phase of hemorrhagic shock. Langenbeck’s Archives of Surgery 386, 302–308.Google Scholar
Holmes, RS, Cox, LA and VandeBerg, JL 2009. Horse carboxylesterases: evidence for six CES1 and four families of CES genes on chromosome 3. Comparative Biochemistry and Physiology Part D, Genomics & Proteomics 4, 54–65.Google Scholar
Kanehisa, M, Sato, Y, Kawashima, M, Furumichi, M and Tanabe, M 2016. KEGG as a reference resource for gene and protein annotation. Nucleic Acids Research 44, D457–D462.Google Scholar
Koc, EC, Burkhart, W, Blackburn, K, Moyer, MB, Schlatzer, DM, Moseley, A and Spremulli, LL 2001. The large subunit of the mammalian mitochondrial ribosome. Analysis of the complement of ribosomal proteins present. Journal of Biological Chemistry 23, 43958–43969.Google Scholar
Kulka, M 2016. A review of paraoxonase 1 properties and diagnostic applications. Polish Journal of Veterinary Sciences 19, 225–232.Google Scholar
Lepczyński, A, Dratwa-Chałupnik, A, Herosimczyk, A, Staszak, K, Majewska, A and Ożgo, M 2014. Impact of the depletion of high-abundance proteins in blood plasma/serum on the proteome of these media in growing farm animals. Turkish Journal of Veterinary and Animal Sciences 38, 490–495.CrossRefGoogle Scholar
Marco-Ramell, A and Bassols, A 2010. Enrichment of low-abundance proteins from bovine and porcine serum samples for proteomic studies. Research in Veterinary Science 89, 340–343.CrossRefGoogle ScholarPubMed
Miller, I, Friendlein, A, Tsangaris, G, Maris, A, Fountoulakis, M and Gemeiner, M 2004. The serum proteome of Equus caballus . Proteomics 4, 3227–3234.CrossRefGoogle ScholarPubMed
Mosesson, MW 2005. Fibrinogen and fibrin structure and functions. Journal of Thrombosis and Haemostasis 3, 1894–1904.CrossRefGoogle ScholarPubMed
Munthe-Fog, L, Hummelshoj, T, Honoré, C, Moller, ME, Skjoedt, MO, Palsgaard, I, Borregaard, N, Madsen, HO and Garred, P 2012. Variation in FCN1 affects biosynthesis of ficolin-1 and is associated with outcome of systemic inflammation. Genes and Immunity 13, 515–522.CrossRefGoogle ScholarPubMed
Muszbek, L, Bereczky, Z, Bagoly, Z, Komáromi, I and Katona, É 2011. Factor XIII: a coagulation factor with multiple plasmatic and cellular functions. Physiological Reviews 91, 931–972.Google Scholar
Nanjappa, V, Thomas, JK, Marimuthu, A, Muthusamy, B, Radhakrishnan, A, Sharma, R, Ahmad Khan, A, Balakrishnan, L, Sahasrabuddhe, NA, Kumar, S, Jhaveri, BN, Sheth, KV, Kumar Khatana, R, Shaw, PG, Srikanth, SM, Mathur, PP, Shankar, S, Nagaraja, D, Christopher, R, Mathivanan, S, Raju, R, Sirdeshmukh, R, Chatterjee, A, Simpson, RJ, Harsha, HC, Pandey, A and Prasad, TS 2014. Plasma proteome database as a resource for proteomics research. Nucleic Acids Research 42, D959–D965.Google Scholar
Olver, CS, Webb, TL, Long, LJ, Scherman, H and Prenni, JE 2010. Comparison of methods for depletion of albumin and IgG from equine serum. Veterinary Clinical Pathology 39, 337–345.Google Scholar
Ozgo, M, Lepczyński, A and Herosimczyk, A 2015. Two-dimensional gel-based serum protein profile of growing piglets. Turkish Journal of Biology 39, 320–327.Google Scholar
Pink, M, Verma, N, Rettenmeier, AW and Schmitz-Spanke, S 2010. CBB staining protocol with higher sensitivity and mass spectrometric compatibility. Electrophoresis 31, 593–598.Google Scholar
Rasaputra, KS, Liyanage, R, Lay, JO Jr., Erf, GF, Okimato, R and Rash, NC 2012. Changes in serum protein profiles of chickens with tibial dyschondroplasia. Open Proteomics Journal 5, 1–7.Google Scholar
Rogowska-Wrzesinska, A, Bihan, MC, Thaysen-Andersen, M and Roepstorffm, P 2013. 2D gels still have a niche in proteomics. Journal of Proteomics 88, 4–13.Google Scholar
Sanjurjo, L, Aran, G, Roher, N, Valledor, AF and Sarrias, MR 2015. AIM/CD5L: a key protein in the control of immune homeostasis and inflammatory disease. Journal of Leukocyte Biology 98, 173–184.Google Scholar
Scoppetta, F, Tartagila, M, Renzone, G, Avellini, L, Gaiti, A, Scaloni, A and Chiaradia, E 2012. Plasma protein changes in horse after prolonged physical exercise: a proteomic study. Journal of Proteomics 75, 4494–4504.Google Scholar
Skrzypczak, WF, Ożgo, M, Lepczyński, A and Herosimczyk, A 2011. Defining the blood plasma protein repertoire of seven day old dairy calves – a preliminary study. Journal of Physiology and Pharmacology 62, 313–319.Google Scholar
Stastna, M and Van Eyk, JE 2012. Secreted proteins as a fundamental source for biomarker discovery. Proteomics 12, 722–735.Google Scholar
Stavenuiter, F, Bouwens, EAM and Mosnier, LO 2013. Down-regulation of the clotting cascade by the protein C pathway. Hematology Education 7, 365–374.Google Scholar
Steelman, SM and Chowdhary, BP 2012. Plasma proteomics showsan elevation of the anti-inflammatory protein APOA-IV in chronic equine laminitis. BMC Veterinary Research 8, 179.Google Scholar
Szklarczyk, D, Franceschini, A, Wyder, S, Forslund, K, Heller, D, Huerta-Cepas, J, Simonovic, M, Roth, A, Santos, A, Tsafou, KP, Kuhn, M, Bork, P, Jensen, LJ and von Mering, C 2015. STRING v10: protein-protein interaction networks, integrated over the tree of life. Nucleic Acids Research 43, D447–D452.Google Scholar
Tirumalai, RS, Chan, KC, Prieto, DA, Issaq, HJ, Conrads, TP and Veenstra, TD 2003. Characterization of the low molecular weight human serum proteome. Molecular & Cellular Proteomics 2, 1096–1103.Google Scholar
Tollefsen, DM 2007. Heparin cofactor II modulates the response to vascular injury. Arteriosclerosis, Thrombosis, and Vascular Biology 27, 454–460.Google Scholar
Wang, M, Weiss, M, Simonovic, M, Haertinger, G, Schrimpf, SP, Hengartner, MO and von Mering, C 2012. PaxDb, a database of protein abundance averages across all three domains of life. Molecular & Cellular Proteomics 11, 492–500.Google Scholar
Zipplies, JK, Hauck, SM, Schoeffmann, S, Amann, B, Stangassinger, M, Ueffing, M and Deeg, C 2009. Serum PEDF levels are decreased in a spontaneous animal model for human autoimmune uveitis. Journal of Proteome Research 8, 992–998.Google Scholar
Zipplies, JK, Hauck, SM, Schoeffmann, S, Amann, B, van der Meijden, CH, Stangassinger, M, Ueffing, M and Deeg, CA 2010. Kininogen in autoimmune uveitis: decrease in peripheral blood stream versus increase in target tissue. Investigative Ophthalmology & Visual Science Journal 51, 375–382.Google Scholar
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