Difference between revisions of "Ceusters 2013 Mitochondrion"
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{{Publication | {{Publication | ||
|title=Ceusters JD, 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 | |title=Ceusters JD, 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: 410-416. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/23268199 PMID:23268199] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/23268199 PMID:23268199] | ||
|authors=Ceusters JD, Mouithys-Mickalad AA, Franck TJ, Derochette S, Vanderplasschen A, Deby-Dupont GP, Serteyn DA | |authors=Ceusters JD, Mouithys-Mickalad AA, Franck TJ, Derochette S, Vanderplasschen A, Deby-Dupont GP, Serteyn DA | ||
|year=2013 | |year=2013 | ||
|journal=Mitochondrion | |journal=Mitochondrion | ||
|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. | |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 | |||
}} | }} | ||
{{Labeling | {{Labeling | ||
|area=Respiration | |area=Respiration | ||
|organism=Horse | |||
|tissues=Skeletal muscle | |||
|preparations=Permeabilized cells | |||
|injuries=Ischemia-Reperfusion; Preservation, RONS; Oxidative Stress | |||
|couplingstates=LEAK, ROUTINE, OXPHOS, ETS | |||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
|additional=Labels | |additional=Labels | ||
}} | }} | ||
Revision as of 13:32, 7 October 2013
| Ceusters JD, 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: 410-416. |
Ceusters JD, Mouithys-Mickalad AA, Franck TJ, Derochette S, Vanderplasschen A, Deby-Dupont GP, Serteyn DA (2013) Mitochondrion
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
Labels: MiParea: Respiration
Stress:Ischemia-Reperfusion; Preservation"Ischemia-Reperfusion; Preservation" is not in the list (Cell death, Cryopreservation, Ischemia-reperfusion, Permeability transition, Oxidative stress;RONS, Temperature, Hypoxia, Mitochondrial disease) of allowed values for the "Stress" property., RONS; Oxidative Stress"RONS; Oxidative Stress" is not in the list (Cell death, Cryopreservation, Ischemia-reperfusion, Permeability transition, Oxidative stress;RONS, Temperature, Hypoxia, Mitochondrial disease) of allowed values for the "Stress" property. Organism: Horse Tissue;cell: Skeletal muscle Preparation: Permeabilized cells
Coupling state: LEAK, ROUTINE, OXPHOS, ETS"ETS" is not in the list (LEAK, ROUTINE, OXPHOS, ET) of allowed values for the "Coupling states" property.
HRR: Oxygraph-2k
Labels
