Ceusters 2013 Mitochondrion
|Ceusters Justine D, Mouithys-Mickalad AA, Franck TJ, Derochette S, Vanderplasschen A, Deby-Dupont GP, Serteyn DA (2013) Effect of myeloperoxidase and anoxia/reoxygenation on mitochondrial respiratory function of cultured primary equine skeletal myoblasts. Mitochondrion 13:410-16.|
Abstract: Horses are particularly sensitive to excessive inflammatory reaction where myeloperoxidase, a marker of inflammation, may contribute to mitochondrial dysfunctions. This study investigated the interaction between myeloperoxidase and cultured primary equine skeletal myoblasts, particularly its effect on mitochondrial respiration combined or not with anoxia followed by reoxygenation (AR). We showed that active myeloperoxidase entered into the cells, interacted with mitochondria and decreased routine and maximal respirations. When combined with AR, myeloperoxidase caused a further decrease of these respiratory parameters while the leak increased. Our results indicate that myeloperoxidase amplifies the mitochondrial damages initiated by AR phenomenon and alters the mitochondrial function.
• Keywords: Anoxia/reoxygenation, CCCP, Creatine kinase, FCCP, High-resolution oxymetry, Mitochondria, Myeloperoxidase, neutrophil, Oxydative phosphorylation, Primary equine skeletal myoblasts, Reactive oxygen and nitrogen species
• O2k-Network Lab: BE Liege Votion DM
Labels: MiParea: Respiration
Stress:Ischemia-reperfusion, Oxidative stress;RONS Organism: Horse Tissue;cell: Skeletal muscle Preparation: Permeabilized cells
Coupling state: LEAK, ROUTINE, OXPHOS, ET