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Home / Equine Research Bank / Vet Immunol Immunopathol / Activation of equine neutrophils by phorbol myristate acetat...
Veterinary immunology and immunopathology2009; 130(3-4); 243-250; doi: 10.1016/j.vetimm.2009.02.015

Activation of equine neutrophils by phorbol myristate acetate or N-formyl-methionyl-leucyl-phenylalanine induces a different response in reactive oxygen species production and release of active myeloperoxidase.

Abstract: Neutrophil (PMN) contribution to the acute inflammatory processes may lead to an excessive generation of reactive oxygen metabolites species (ROS) and secretion of granule enzymes. We compared the effects of either phorbol myristate acetate (PMA) or N-formyl-methionyl-leucyl-phenylalanine (fMLP) in combination with a pre-treatment by cytochalasin B (CB) on the production of ROS and the release of total and active myeloperoxidase (MPO) by isolated equine PMNs. The ROS production was assessed by lucigenin dependent chemiluminescence (CL) and ethylene release by alpha-keto-gamma-methylthiobutyric acid (KMB) oxidation. In the supernatant of activated PMNs, total equine MPO was measured by ELISA and active MPO by the SIEFED (Specific Immunologic Extraction Followed by Enzymatic Detection) technique that allows for the study of the interaction of a compound directly with the enzyme. The stimulation of PMNs with CB-fMLP only modestly increased the release of MPO, but more than 70% of released MPO was active. PMA stimulation markedly increased the production of ROS and release of MPO, but more than 95% of released MPO was inactive. When PMNs were pre-incubated with superoxide dismutase (SOD) prior to PMA activation, the lucigenin enhanced CL, which is linked to the superoxide anion (O2-) production, was much more decreased than KMB oxidation, linked to the hydroxyl-like radical production. The addition of SOD prior to the activation of PMNs by PMA also limited the loss of the activity of released MPO. These results confirm the key role of O2- generation in the ROS cascade in PMN and reveal its critical role on MPO inactivation.
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Publication Date: 2009-03-04 PubMed ID: 19328559DOI: 10.1016/j.vetimm.2009.02.015Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research explores how the activation of equine neutrophils, a type of white blood cell, by two different chemicals results in varying reactions in the production of reactive oxygen species and the release of an enzyme called myeloperoxidase.

Experiment Setup

  • The researchers studied the behavior of isolated equine neutrophils when activated by either phorbol myristate acetate (PMA) or N-formyl-methionyl-leucyl-phenylalanine (fMLP).
  • These neutrophils were also pre-treated with cytochalasin B (CB) before the activation process.
  • The research focused on observing changes in the production of reactive oxygen metabolites species (ROS) and the release of total and active myeloperoxidase (MPO), an enzyme contained in neutrophils.

Observations

  • Following the activation of neutrophils with CB-fMLP, the release of MPO was slightly increased. However, over 70% of this released MPO remained active.
  • When the neutrophils were stimulated with PMA, the ROS production and MPO release greatly increased. But more than 95% of the released MPO became inactive.
  • The researchers used superoxide dismutase (SOD) to treat neutrophils before PMA activation. This treatment decreased the production of superoxide anion (a type of ROS) significantly but had a smaller impact on the production of hydroxyl-like radical (another type of ROS).
  • When SOD was added prior to PMA activation, it prevented the inactivation of the released MPO.

Conclusion

  • This study confirms the significant role that superoxide anion has in the ROS cascade inside neutrophils. It also emphasizes the impact it has on the inactivation of MPO.
  • The findings suggest that the manner and conditions under which equine neutrophils are activated can alter their response, especially in terms of reactive oxygen species production and enzyme release.

Cite This Article

APA
Franck T, Kohnen S, de la Rebière G, Deby-Dupont G, Deby C, Niesten A, Serteyn D. (2009). Activation of equine neutrophils by phorbol myristate acetate or N-formyl-methionyl-leucyl-phenylalanine induces a different response in reactive oxygen species production and release of active myeloperoxidase. Vet Immunol Immunopathol, 130(3-4), 243-250. https://doi.org/10.1016/j.vetimm.2009.02.015

Publication

Veterinary immunology and immunopathology
ISSN: 1873-2534
NlmUniqueID: 8002006
Country: Netherlands
Language: English
Volume: 130
Issue: 3-4
Pages: 243-250

Researcher Affiliations

Franck, T
  • Department of Clinical Sciences, Large Animal Surgery, B 41,University of Liège, Sart Tilman, Liège BE-4000, Belgium. t.franck@ulg.ac.be
Kohnen, S
    de la Rebière, G
      Deby-Dupont, G
        Deby, C
          Niesten, A
            Serteyn, D

              MeSH Terms

              • Animals
              • Biphenyl Compounds / pharmacology
              • Cell Degranulation / drug effects
              • Cytochalasin B / pharmacology
              • Ethylenes / metabolism
              • Horse Diseases / physiopathology
              • Horses / immunology
              • Horses / physiology
              • In Vitro Techniques
              • Inflammation / physiopathology
              • Inflammation / veterinary
              • Luminescent Measurements
              • N-Formylmethionine Leucyl-Phenylalanine / pharmacology
              • Neutrophils / drug effects
              • Neutrophils / immunology
              • Neutrophils / physiology
              • Onium Compounds / pharmacology
              • Peroxidase / metabolism
              • Reactive Oxygen Species / metabolism
              • Superoxide Dismutase / metabolism
              • Superoxide Dismutase / pharmacology
              • Tetradecanoylphorbol Acetate / pharmacology

              Citations

              This article has been cited 4 times.
              1. Franck T, Ceusters J, Graide H, Mouithys-Mickalad A, Serteyn D. Muscle Derived Mesenchymal Stem Cells Inhibit the Activity of the Free and the Neutrophil Extracellular Trap (NET)-Bond Myeloperoxidase. Cells 2021 Dec 10;10(12).
                doi: 10.3390/cells10123486pubmed: 34943996google scholar: lookup
              2. Tsuzuki N, Kanbayashi Y, Kusano K. Markers for oxidative stress in the synovial fluid of Thoroughbred horses with carpal bone fracture. J Equine Sci 2019 Mar;30(1):13-16.
                doi: 10.1294/jes.30.13pubmed: 30944542google scholar: lookup
              3. Khan AA, Alsahli MA, Rahmani AH. Myeloperoxidase as an Active Disease Biomarker: Recent Biochemical and Pathological Perspectives. Med Sci (Basel) 2018 Apr 18;6(2).
                doi: 10.3390/medsci6020033pubmed: 29669993google scholar: lookup
              4. Flemmig J, Zschaler J, Remmler J, Arnhold J. The fluorescein-derived dye aminophenyl fluorescein is a suitable tool to detect hypobromous acid (HOBr)-producing activity in eosinophils. J Biol Chem 2012 Aug 10;287(33):27913-23.
                doi: 10.1074/jbc.M112.364299pubmed: 22718769google scholar: lookup
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