title: Mitochondrial proteomes of porcine kidney cortex and medulla: foundation for translational proteomics.
abstract: BACKGROUND
  Emerging evidence has linked mitochondrial dysfunction to the pathogenesis of many renal disorders, including acute kidney injury, sepsis and even chronic kidney disease. Proteomics is a powerful tool in elucidating the role of mitochondria in renal pathologies. Since the pig is increasingly recognized as a major mammalian model for translational research, the lack of physiological proteome data of large mammals prompted us to examine renal mitochondrial proteome in porcine kidney cortex and medulla
  
  
  METHODS
  Kidneys were obtained from six healthy pigs. Mitochondria from cortex and medulla were isolated using differential centrifugation and proteome maps of cortical and medullar mitochondria were constructed using two-dimensional gel electrophoresis (2DE). Protein spots with significant difference between mitochondrial fraction of renal cortex and medulla were identified by mass spectrometry.
  
  
  RESULTS
  Proteomic analysis identified 81 protein spots. Of these spots, 41 mitochondrial proteins were statistically different between renal cortex and medulla (p < 0.05). Protein spots containing enzymes of beta oxidation, amino acid metabolism, and gluconeogenesis were predominant in kidney cortex mitochondria. Spots containing tricarboxylic acid cycle enzymes and electron transport system proteins, proteins maintaining metabolite transport and mitochondrial translation were more abundant in medullar mitochondria.
  
  
  CONCLUSIONS
  This study provides the first proteomic profile of porcine kidney cortex and medullar mitochondrial proteome. Different protein expression pattern reflects divergent functional metabolic role of mitochondria in various kidney compartments. Our study could serve as a useful reference for further porcine experiments investigating renal mitochondrial physiology under various pathological states.
authors.affiliation: Faculty of Medicine in Plzen, Biomedical Center, Charles University in Prague, alej Svobody, 1655/76, Plzen, Czech Republic. zdenek.tuma@lfp.cuni.cz.
authors.forename: Zdenek
authors.identifier: http://orcid.org/0000-0002-2375-4169
authors.initials: Z
authors.lastname: Tuma
authors.affiliation: Faculty of Medicine in Plzen, Biomedical Center, Charles University in Prague, alej Svobody, 1655/76, Plzen, Czech Republic.|Department of Physiology, Charles University Medical School, Plzen, Czech Republic.
authors.forename: Jitka
authors.initials: J
authors.lastname: Kuncova
authors.affiliation: Faculty of Medicine in Plzen, Biomedical Center, Charles University in Prague, alej Svobody, 1655/76, Plzen, Czech Republic.|Department of Internal Medicine I, Charles University Medical School and Teaching Hospital, Plzen, Czech Republic.
authors.forename: Jan
authors.initials: J
authors.lastname: Mares
authors.affiliation: Faculty of Medicine in Plzen, Biomedical Center, Charles University in Prague, alej Svobody, 1655/76, Plzen, Czech Republic.|Department of Internal Medicine I, Charles University Medical School and Teaching Hospital, Plzen, Czech Republic.
authors.forename: Martin
authors.initials: M
authors.lastname: Matejovic
mesh_terms: D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional; D005260:Female; D007672:Kidney Cortex / Q000737:chemistry*; D007679:Kidney Medulla / Q000737:chemistry*; D008297:Male; D008928:Mitochondria / Q000737:chemistry*; D024101:Mitochondrial Proteins / Q000032:analysis*; D023421:Models, Animal; D040901:Proteomics / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D034421:Sus scrofa; D053719:Tandem Mass Spectrometry; D057170:Translational Research, Biomedical / Q000379:methods*
chemical_list: D024101:Mitochondrial Proteins
keywords: Mitochondria; Pig kidney; Proteomics; Two-dimensional electrophoresis