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Calprotectin (S100A8/S100A9) and Myeloperoxidase: Co-Regulators of Formation of Reactive Oxygen Species
Inflammatory mediators trigger polymorphonuclear neutrophils (PMN) to produce reactive oxygen species (ROS: O(2)(-), H(2)O(2), ∙OH). Mediated by myeloperoxidase in PMN, HOCl is formed, detectable in a chemiluminescence (CL) assay. We have shown that the abundant cytosolic PMN protein calprotectin (S...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Molecular Diversity Preservation International
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3206613/ https://www.ncbi.nlm.nih.gov/pubmed/22069549 http://dx.doi.org/10.3390/toxins2010095 |
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author | Bøyum, Arne Skrede, Knut Kristian Myhre, Oddvar Tennfjord, Vivi-Ann Neurauter, Christine Gran Tolleshaug, Helge Knudsen, Eirunn Opstad, Per Kristian Bjørås, Magnar Benestad, Haakon B. |
author_facet | Bøyum, Arne Skrede, Knut Kristian Myhre, Oddvar Tennfjord, Vivi-Ann Neurauter, Christine Gran Tolleshaug, Helge Knudsen, Eirunn Opstad, Per Kristian Bjørås, Magnar Benestad, Haakon B. |
author_sort | Bøyum, Arne |
collection | PubMed |
description | Inflammatory mediators trigger polymorphonuclear neutrophils (PMN) to produce reactive oxygen species (ROS: O(2)(-), H(2)O(2), ∙OH). Mediated by myeloperoxidase in PMN, HOCl is formed, detectable in a chemiluminescence (CL) assay. We have shown that the abundant cytosolic PMN protein calprotectin (S100A8/A9) similarly elicits CL in response to H(2)O(2) in a cell-free system. Myeloperoxidase and calprotectin worked synergistically. Calprotectin-induced CL increased, whereas myeloperoxidase-triggered CL decreased with pH > 7.5. Myeloperoxidase needed NaCl for CL, calprotectin did not. 4-hydroxybenzoic acid, binding ∙OH, almost abrogated calprotectin CL, but moderately increased myeloperoxidase activity. The combination of native calprotectin, or recombinant S100A8/A9 proteins, with NaOCl markedly enhanced CL. NaOCl may be the synergistic link between myeloperoxidase and calprotectin. Surprisingly- and unexplained- at higher concentration of S100A9 the stimulation vanished, suggesting a switch from pro-oxidant to anti-oxidant function. We propose that the ∙OH is predominant in ROS production by calprotectin, a function not described before. |
format | Online Article Text |
id | pubmed-3206613 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Molecular Diversity Preservation International |
record_format | MEDLINE/PubMed |
spelling | pubmed-32066132011-11-08 Calprotectin (S100A8/S100A9) and Myeloperoxidase: Co-Regulators of Formation of Reactive Oxygen Species Bøyum, Arne Skrede, Knut Kristian Myhre, Oddvar Tennfjord, Vivi-Ann Neurauter, Christine Gran Tolleshaug, Helge Knudsen, Eirunn Opstad, Per Kristian Bjørås, Magnar Benestad, Haakon B. Toxins (Basel) Article Inflammatory mediators trigger polymorphonuclear neutrophils (PMN) to produce reactive oxygen species (ROS: O(2)(-), H(2)O(2), ∙OH). Mediated by myeloperoxidase in PMN, HOCl is formed, detectable in a chemiluminescence (CL) assay. We have shown that the abundant cytosolic PMN protein calprotectin (S100A8/A9) similarly elicits CL in response to H(2)O(2) in a cell-free system. Myeloperoxidase and calprotectin worked synergistically. Calprotectin-induced CL increased, whereas myeloperoxidase-triggered CL decreased with pH > 7.5. Myeloperoxidase needed NaCl for CL, calprotectin did not. 4-hydroxybenzoic acid, binding ∙OH, almost abrogated calprotectin CL, but moderately increased myeloperoxidase activity. The combination of native calprotectin, or recombinant S100A8/A9 proteins, with NaOCl markedly enhanced CL. NaOCl may be the synergistic link between myeloperoxidase and calprotectin. Surprisingly- and unexplained- at higher concentration of S100A9 the stimulation vanished, suggesting a switch from pro-oxidant to anti-oxidant function. We propose that the ∙OH is predominant in ROS production by calprotectin, a function not described before. Molecular Diversity Preservation International 2010-01-20 /pmc/articles/PMC3206613/ /pubmed/22069549 http://dx.doi.org/10.3390/toxins2010095 Text en © 2010 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland http://creativecommons.org/licenses/by/3.0/ This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Bøyum, Arne Skrede, Knut Kristian Myhre, Oddvar Tennfjord, Vivi-Ann Neurauter, Christine Gran Tolleshaug, Helge Knudsen, Eirunn Opstad, Per Kristian Bjørås, Magnar Benestad, Haakon B. Calprotectin (S100A8/S100A9) and Myeloperoxidase: Co-Regulators of Formation of Reactive Oxygen Species |
title | Calprotectin (S100A8/S100A9) and Myeloperoxidase: Co-Regulators of Formation of Reactive Oxygen Species |
title_full | Calprotectin (S100A8/S100A9) and Myeloperoxidase: Co-Regulators of Formation of Reactive Oxygen Species |
title_fullStr | Calprotectin (S100A8/S100A9) and Myeloperoxidase: Co-Regulators of Formation of Reactive Oxygen Species |
title_full_unstemmed | Calprotectin (S100A8/S100A9) and Myeloperoxidase: Co-Regulators of Formation of Reactive Oxygen Species |
title_short | Calprotectin (S100A8/S100A9) and Myeloperoxidase: Co-Regulators of Formation of Reactive Oxygen Species |
title_sort | calprotectin (s100a8/s100a9) and myeloperoxidase: co-regulators of formation of reactive oxygen species |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3206613/ https://www.ncbi.nlm.nih.gov/pubmed/22069549 http://dx.doi.org/10.3390/toxins2010095 |
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