title: Hyperoxia-Induced Protein Alterations in Renal Rat Tissue: A Quantitative Proteomic Approach to Identify Hyperoxia-Induced Effects in Cellular Signaling Pathways.
abstract: BACKGROUND
  In renal tissue as well as in other organs, supranormal oxygen pressure may lead to deleterious consequences on a cellular level. Additionally, hyperoxia-induced effect in cells and related free radicals may potentially contribute to renal failure. The aim of this study was to analyze time-dependent alterations of rat kidney protein expression after short-term normobaric hyperoxia using proteomics and bioinformatic approaches.
  
  
  METHODS
  N = 36 Wistar rats were randomized into six different groups: three groups with normobaric hyperoxia (exposure to 100% oxygen for 3 h) and three groups with normobaric normoxia (NN; room air). After hyperoxia exposure, kidneys were removed immediately, after 3 days and after 7 days. Kidney lysates were analyzed by two-dimensional gel electrophoresis followed by peptide mass fingerprinting using tandem mass spectrometry. Statistical analysis was performed with DeCyder 2D software (p < 0.01). Biological functions of differential regulated proteins were studied using functional network analysis (Ingenuity Pathways Analysis and PathwayStudio).
  
  
  RESULTS
  Expression of 14 proteins was significantly altered (p < 0.01): eight proteins (MEP1A_RAT, RSSA_RAT, F16P1_RAT, STML2_RAT, BPNT1_RAT, LGMN_RAT, ATPA_RAT, and VDAC1_RAT) were downregulated and six proteins (MTUS1_RAT, F16P1_RAT, ACTG_RAT, ACTB_RAT, 2ABA_RAT, and RAB1A_RAT) were upregulated. Bioinformatic analyses revealed an association of regulated proteins with inflammation.
  
  
  CONCLUSIONS
  Significant alterations in renal protein expression could be demonstrated for up to 7 days even after short-term hyperoxia. The identified proteins indicate an association with inflammation signaling cascades. MEP1A and VDAC1 could be promising candidates to identify hyperoxic injury in kidney cells.
authors.affiliation: Department for Anaesthesiology and Intensive Care Medicine, University Hospital of Cologne, 50937 Cologne, Germany.
authors.forename: Jochen
authors.initials: J
authors.lastname: Hinkelbein
authors.affiliation: Department for Anaesthesiology and Intensive Care Medicine, University Hospital of Cologne, 50937 Cologne, Germany.
authors.forename: Lennert
authors.initials: L
authors.lastname: Böhm
authors.affiliation: Department for Anaesthesiology and Intensive Care Medicine, University Hospital of Cologne, 50937 Cologne, Germany.
authors.forename: Oliver
authors.initials: O
authors.lastname: Spelten
authors.affiliation: Department for Anaesthesiology and Intensive Care Medicine, University Hospital of Cologne, 50937 Cologne, Germany.
authors.forename: David
authors.initials: D
authors.lastname: Sander
authors.affiliation: Department for Anaesthesia, Dormagen Hospital, 41540 Dormagen, Germany.
authors.forename: Stefan
authors.initials: S
authors.lastname: Soltész
authors.affiliation: Department for Anaesthesiology and Intensive Care Medicine, University Hospital of Cologne, 50937 Cologne, Germany.
authors.forename: Stefan
authors.initials: S
authors.lastname: Braunecker
mesh_terms: D000818:Animals; D005786:Gene Expression Regulation; D018496:Hyperoxia / Q000378:metabolism*; D007668:Kidney / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D051381:Rats; D017208:Rats, Wistar; D015398:Signal Transduction; D053719:Tandem Mass Spectrometry