Effect of myeloperoxidase and anoxia/reoxygenation on mitochondrial respiratory function of cultured primary equine skeletal myoblasts.
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.
Copyright © 2012 Elsevier B.V. All rights reserved.
Publication Date: 2012-12-22 PubMed ID: 23268199DOI: 10.1016/j.mito.2012.12.004Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This study explores how myeloperoxidase, a marker of inflammation, affects mitochondrial function in horse cells under normal and oxygen-deprived conditions.
Research Objective
- The primary purpose of this research was to assess the impact of myeloperoxidase (MPO) – a protein associated with inflammation – on the mitochondrial respiratory function of cultured primary equine skeletal myoblasts (horse muscle cells), particularly under anoxia (lack of oxygen) and reoxygenation (restore of oxygen) conditions.
Methods Used
- The researchers used a cell culture model, exposing equine skeletal myoblasts to active myeloperoxidase and observing its behavior in both normal and anoxiareoxygenation conditions.
Findings
- The study revealed a noteworthy interaction between active myeloperoxidase and horse muscle cells, where MPO entered the cells and interacted with the mitochondria. The presence of myeloperoxidase resulted in a decrease in routine and maximal mitochondrial respiration, indicating disrupted cell metabolism.
- Further, when myeloperoxidase-exposed cells underwent an anoxia-reoxygenation cycle, MPO was found to further take down the respiratory parameters, while simultaneously causing an increase in mitochondrial leak – a sign of cell stress and possible damage to mitochondrial structure and function.
- These findings suggest that myeloperoxidase amplifies the mitochondrial damages initiated by the anoxia-reoxygenation phenomenon and notably alters the mitochondrial function.
Implications
- The results of this study hold significant implications in understanding the role of inflammation, particularly the role of myeloperoxidase, in causing cellular damages in horses. As horses are known to be especially susceptible to excessive inflammation, understanding the negative effects of MPO on cell metabolism and integrity could help in developing potential therapeutic targets to combat inflammatory responses in these animals.
Cite This Article
APA
Ceusters JD, Mouithys-Mickalad AA, Franck TJ, Derochette S, Vanderplasschen A, Deby-Dupont GP, Serteyn DA.
(2012).
Effect of myeloperoxidase and anoxia/reoxygenation on mitochondrial respiratory function of cultured primary equine skeletal myoblasts.
Mitochondrion, 13(5), 410-416.
https://doi.org/10.1016/j.mito.2012.12.004 Publication
Researcher Affiliations
- Center for Oxygen Research and Development, Institute of Chemistry B6a, University of Liège, Sart Tilman, 4000 Liège, Belgium. j.ceusters@ulg.ac.be
MeSH Terms
- Animals
- Cell Respiration
- Cells, Cultured
- Horses
- Hypoxia
- Mitochondria / drug effects
- Mitochondria / metabolism
- Myoblasts, Skeletal / physiology
- Oxygen / metabolism
- Peroxidase / metabolism
Citations
This article has been cited 2 times.- Parrilla Hernández S, Franck T, Munaut C, Feyereisen É, Piret J, Farnir F, Reigner F, Barrière P, Deleuze S. Characterization of Myeloperoxidase in the Healthy Equine Endometrium. Animals (Basel) 2023 Jan 21;13(3).
- Hendrick E, Peixoto P, Blomme A, Polese C, Matheus N, Cimino J, Frère A, Mouithys-Mickalad A, Serteyn D, Bettendorff L, Elmoualij B, De Tullio P, Eppe G, Dequiedt F, Castronovo V, Mottet D. Metabolic inhibitors accentuate the anti-tumoral effect of HDAC5 inhibition. Oncogene 2017 Aug 24;36(34):4859-4874.
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