An update on medium- and low-abundant blood plasma proteome of horse
A. Lepczyński,
M. Ożgo,
A. Dratwa-Chałupnik,
P. Robak,
A. Pyć,
D. Zaborski,
A. Herosimczyk
Affiliations
A. Lepczyński
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
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
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
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
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
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
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
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.