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Molecular & Cellular Proteomics 5:979-986, 2006.
© 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Warm Ischemia-induced Alterations in Oxidative and Inflammatory Proteins in Hepatic Kupffer Cells in Rats^*

From the ^d Mass Spectrometry Facility, Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94143-0446, the ^f Department of Surgery, Chonnam National University Medical School, Gwangju 501-757, Korea, the ⁱ Department of Urology, Kwangju Christian Hospital, Gwangju 503-822, Korea, the ^g Department of Surgery, Division of Transplantation, University of California, San Francisco, California 94143-0780, the ^j Rice Liver Center Laboratory, University of California, San Francisco, California 94143, the ^a Anesthesia and Perioperative Care University of California, San Francisco, California 94143-0648, the ^b Cardiovascular Research Institute, University of California, San Francisco, California 94143-0130, the ^e Departments of Pediatrics, University of Colorado Health Science Center, Aurora, Colorado 80262, and the ^h Department of Medicine, University of California, San Francisco, California 94143-0624

The aim of the study was to investigate the impact of ischemia/reperfusion injury on the proteome of Kupffer cells. Lean Zucker rats (n = 6 each group) were randomized to 75 min of warm ischemia or sham operation. After reperfusion for 8 h, Kupffer cells were isolated by enzymatic perfusion and density gradient centrifugation. Proteins were tryptically digested into peptides and differentially labeled with iTRAQ (isobaric tags for relative and absolute quantitation) reagent. After fractionation by cation exchange chromatography, peptides were identified by mass spectrometry (ESI-LC-MS/MS). Spectra were interrogated against the Swiss-Prot database and quantified using ProteinProspector®. The results for heat shock protein 70 and myeloperoxidase were validated by ELISA. Quantitative information for more than 1559 proteins was obtained. In the ischemia group proteins involved in inflammation were significantly up-regulated. The ratio for calgranulin B in the ischemia/sham group was 1.81 ± 0.97 (p < 0.0001), for complement C3 the ratio was 1.81 ± 0.49 (p < 0.0001), and for myeloperoxidase the ratio was 1.30 ± 0.32. Myeloperoxidase was only recently documented in Kupffer cells. The antioxidative proteins Cu,Zn-superoxide dismutase (1.34 ± 0.19; p < 0.001) and catalase (1.23 ± 0.43; p < 0.001) were also elevated. In conclusion, ischemia/reperfusion injury induces alterations in the Kupffer cell proteome. Isotope ratio mass spectrometry is a powerful tool to investigate these reactions. The ability to simultaneously monitor several pathways involved in reperfusion stress may result in important mechanistic insight and possibly new treatment options.

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