Mapping of polar fox renal cortex proteins using two-dimensional gel electrophoresis and mass spectrometry – a preliminary study

• Autorzy: Ciechanowicz A.K. , Ozgo M. , Stanski L. R. , Herosimczyk A. , Piotrowska A. , Szymeczko R. , Laszczynska M. , Skrzypczak W. F.
• Języki publikacji: EN

Abstrakty

EN

The aim of the present study was to establish protein map of polar fox (Alopex lagopus) renal cortex. Kidney cortex proteins of isoelectric point ranging from 3 to 10 were analysed using two-dimensional electrophoresis and MALDI-TOF mass spectrometry. Sixteen protein spots corresponding to thirteen different gene products were identified. These proteins were divided into following groups: lipid and fatty acid metabolism, amino acid metabolism, energetic pathways, regulatory proteins, transport proteins and structural proteins. This is the first attempt to create reproducible 2-D map, of renal cortex proteins characteristic for polar foxes, used as animal model for carnivores. It is worth emphasizing that the results of this study may broaden currently available protein databases.

• Wydawca: -
• Czasopismo: Polish Journal of Veterinary Sciences
• Rocznik: 2014
• Tom: 17
• Numer: 2
• Opis fizyczny: p.231-237,fig.,ref.

Twórcy

autor

Ciechanowicz A.K.

• Department of Physiology, Cytobiology and Proteomics, Faculty of Biotechnology and Animal Husbandry, West Pomeranian University of Technology, Szczecin, Dr Judyma 6, 71-466 Szczecin, Poland

autor

Ozgo M.

• Department of Physiology, Cytobiology and Proteomics, Faculty of Biotechnology and Animal Husbandry, West Pomeranian University of Technology, Szczecin, Dr Judyma 6, 71-466 Szczecin, Poland

autor

Stanski L. R.

• Department of Physiology, Cytobiology and Proteomics, Faculty of Biotechnology and Animal Husbandry, West Pomeranian University of Technology, Szczecin, Dr Judyma 6, 71-466 Szczecin, Poland

autor

Herosimczyk A.

• Department of Physiology, Cytobiology and Proteomics, Faculty of Biotechnology and Animal Husbandry, West Pomeranian University of Technology, Szczecin, Dr Judyma 6, 71-466 Szczecin, Poland

autor

Piotrowska A.

• Department of Animal Physiology, Faculty of Animal Breeding and Biology, University of Technology and Life Sciences, Mazowiecka 28, 85-084 Bydgoszcz, Poland

autor

Szymeczko R.

• Department of Animal Physiology, Faculty of Animal Breeding and Biology, University of Technology and Life Sciences, Mazowiecka 28, 85-084 Bydgoszcz, Poland

autor

Laszczynska M.

• Laboratory of Histology and Developmental Biology, Pomeranian Medical University, Zolnierska 48, 71-210 Szczecin, Poland

autor

Skrzypczak W. F.

• Department of Physiology, Cytobiology and Proteomics, Faculty of Biotechnology and Animal Husbandry, West Pomeranian University of Technology, Szczecin, Dr Judyma 6, 71-466 Szczecin, Poland

Bibliografia

• Akerlöf E, Jörnvall H, Slotte H, Pousette A (1991) Identification of apolipoprotein A1 and immunoglobulin as components of a serum complex that mediates activation of human sperm motility. Biochemistry 30: 8986-8990.
• Arthur JM, Thongboonkerd V, Scherzer JA, Cai J, Pierce WM, Klein JB (2002) Differential expression of proteins in renal cortex and medulla: a proteomic approach. Kidney Int 62: 1314-1321.
• Ciechanowicz AK, Ozgo M, Herosimczyk A, Kurpińska A, Klonowska A, Lepczyński A, Stański LR (2011) Urinary proteomic strategies in biomarkers discovery of renal diseases. J Pre-Clinical Clin Res 5: 1-6.
• Das N, Levine RL, Orr WC, Sohal RS (2001) Selectivity of protein oxidative damage during aging in Drosophila melanogaster. Biochem J 360: 209-216.
• Deferrari G, Garibotto G, Robaudo C, Saffioti S, Russo R, Sala MR, Bruzzone M, Tizianello A (1994) Renal ammoniagenesis and interorgan flow of glutamine in chronic metabolic acidosis. Contrib Nephrol 110: 144-149.
• Hadziselimović H, Cus M (1975) Blood vessels and excretory apparatus of the kidney in some wild animals. Acta Anat (Basel) 91: 71-82.
• He C, Braunitzer G (1991) Carnivora: the primary structure of the hemoglobin from the silver fox (Vulpes vulpes var., Canidae). Biol Chem Hoppe Seyler 372: 43-48.
• Herosimczyk A, Dejeans N, Sayd T, Ozgo M, Skrzypczak WF, Mazur A (2006) Plasma proteome analysis: 2D gels and chips. J Physiol Pharmacol 57: 81-93.
• Jankowski M (2003) Usefulness of biopsy performed under control of USG in diagnosing nephropathy in dogs. Med Weter 59: 137-140.
• Jaskowski JM, Kempisty B, Wozna M, Walczak R, Szczepanska P, Dziuban J, Antosik P (2010) Selected methods of assessing the developmental competence of bovine oocytes and embryos. Med Weter 66: 740-744.
• Kempisty B, Zawierucha P, Nowicki M (2011) Technology based on expression microarrays, proteomic microarrays and tissue microarrays in mammalian oncogenesis research. Med Weter 67: 720-724.
• Lu J, Stewart AJ, Sadler PJ, Pinheiro TJ, Blindauer CA (2008) Albumin as a zinc carrier: properties of its high-affinity zinc-binding site. Biochem Soc Trans 36: 1317-1321.
• Nakata K, Kobayashi K, Yanagi H, Shimakura Y, Tsuchiya S, Arinami T, Hamaguchi H (1993) Autosomal dominant hypoalphalipoproteinemia due to a completely defective apolipoprotein A-I gene. Biochem Biophys Res Commun 196: 950-955.
• Ng DS, Leiter LA, Vezina C, Connelly PW, Hegele RA (1994) Apolipoprotein A-I Q[-2]X causing isolated apolipoprotein A-I deficiency in a family with analphalipoproteinemia. J Clin Invest 93: 223-229.
• Nichols WC, Dwulet FE, Liepnieks J, Benson MD (1988) Variant apolipoprotein AI as a major constituent of a human hereditary amyloid. Biochem Biophys Res Commun 156: 762-768.
• Nichols WC, Gregg RE, Brewer HB Jr, Benson MD (1990) A mutation in apolipoprotein A-I in the Iowa type of familial amyloidotic polyneuropathy. Genomics 8: 318-323.
• Nowicki M, Depta A, Rychlik A, Nieradka R, Kander M (2005) Comparative examinations of different renal biopsy techniques in dogs. Med Weter 61: 405-407.
• Committee on Animal Nutrition, National Research Council (1982) Nutrient requirements of mink and foxes, 2nd ed., National Academy Press, Washington DC.
• Ozgo M, Skrzypczak WF, Herosimczyk A, Mazur A (2007) Proteomics in relation to renal physiology and pathophysiology. Med Weter 63: 1146-1150.
• Soutar AK, Hawkins PN, Vigushin DM, Tennent GA, Booth SE, Hutton T, Nguyen O, Totty NF, Feest TG, Hsuan JJ, Pepys MB (1992) Apolipoprotein AI mutation Arg-60 causes autosomal dominant amyloidosis. Proc Natl Acad Sci U S A 89: 7389-7393.
• Treberg JR, Clow KA, Greene KA, Brosnan ME, Brosnan JT (2010) Systemic activation of glutamate dehydrogenase increases renal ammoniagenesis: implications for the hyperinsulinism/hyperammonemia syndrome. Am J Physiol Endocrinol Metab 298: E1219-E1225.
• Velic A, Macek B, Wagner CA (2010) Toward quantitative proteomics of organ substructures: implications for renal physiology. Semin Nephrol 30: 487-499.
• Xing Y, Ding J, Fan Q, Guan N (2006) Diversities of podocyte molecular changes induced by different antiproteinuria drugs. Exp Biol Med (Maywood) 231: 585-593.
• Yan LJ, Levine RL, Sohal RS (1997) Oxidative damage during aging targets mitochondrial aconitase. Proc Natl Acad Sci U S A 94: 11168- 11172.
• Yarian CS, Rebrin I, Sohal RS (2005) Aconitase and ATP synthase are targets of malondialdehyde modification and undergo an age-related decrease in activity in mouse heart mitochondria. Biochem Biophys Res Commun 330: 151-156.
• Yarian CS, Toroser D, Sohal RS (2006) Aconitase is the main functional target of aging in the citric acid cycle of kidney mitochondria from mice. Mech Ageing Dev 127: 79-84.
• Yoo KH, Kim YN, Lee MJ, Seong JK, Park JH (2009) Identification of apolipoprotein A1 reduction in the polycystic kidney by proteomics analysis of the Mxi1-deficient mouse. Proteomics 9: 3824-3832.
• Yoshida Y, Miyazaki K, Kamiie J, Sato M, Okuizumi S, Kenmochi A, Kamijo K, Nabetani T, Tsugita A, Xu B, Zhang Y, Yaoita E, Osawa T, Yamamoto T (2005) Two-dimensional electrophoretic profiling of normal human kidney glomerulus proteome and construction of an extensible markup language (XML)-based database. Proteomics 5: 1083-1096.
• Zhan YM, Yasuda J, Too K (1991) Reference data on the anatomy and serum biochemistry of the silver fox. Jpn J Vet Res 39: 39-50.

Identyfikatory

DOI

10.2478/pjvs-2014-003