Secretion of S100A8, S100A9, and S100A12 by Neutrophils Involves Reactive Oxygen Species and Potassium Efflux
S100A8/A9 (calprotectin) and S100A12 proinflammatory mediators are found at inflammatory sites and in the serum of patients with inflammatory or autoimmune diseases. These cytoplasmic proteins are secreted by neutrophils at sites of inflammation via alternative secretion pathways of which little is...
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| Format: | Article |
| Language: | English |
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Wiley
2015-01-01
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| Series: | Journal of Immunology Research |
| Online Access: | http://dx.doi.org/10.1155/2015/296149 |
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| author | Mélanie R. Tardif Julie Andrea Chapeton-Montes Alma Posvandzic Nathalie Pagé Caroline Gilbert Philippe A. Tessier |
| author_facet | Mélanie R. Tardif Julie Andrea Chapeton-Montes Alma Posvandzic Nathalie Pagé Caroline Gilbert Philippe A. Tessier |
| author_sort | Mélanie R. Tardif |
| collection | DOAJ |
| description | S100A8/A9 (calprotectin) and S100A12 proinflammatory mediators are found at inflammatory sites and in the serum of patients with inflammatory or autoimmune diseases. These cytoplasmic proteins are secreted by neutrophils at sites of inflammation via alternative secretion pathways of which little is known. This study examined the nature of the stimuli leading to S100A8/A9 and S100A12 secretion as well as the mechanism involved in this alternative secretion pathway. Chemotactic agents, cytokines, and particulate molecules were used to stimulate human neutrophils. MSU crystals, PMA, and H2O2 induced the release of S100A8, S100A9, and S100A12 homodimers, as well as S100A8/A9 heterodimer. High concentrations of S100A8/A9 and S100A12 were secreted in response to nanoparticles like MSU, silica, TiO2, fullerene, and single-wall carbon nanotubes as well as in response to microbe-derived molecules, such as zymosan or HKCA. However, neutrophils exposed to the chemotactic factors fMLP failed to secrete S100A8/A9 or S100A12. Secretion of S100A8/A9 was dependent on the production of reactive oxygen species and required K+ exchanges through the ATP-sensitive K+ channel. Altogether, these findings suggest that S100A12 and S100A8/A9 are secreted independently either via distinct mechanisms of secretion or following the activation of different signal transduction pathways. |
| format | Article |
| id | doaj-art-752299e36eef4c19b49570058e5948bb |
| institution | Kabale University |
| issn | 2314-8861 2314-7156 |
| language | English |
| publishDate | 2015-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Journal of Immunology Research |
| spelling | doaj-art-752299e36eef4c19b49570058e5948bb2025-02-03T07:25:08ZengWileyJournal of Immunology Research2314-88612314-71562015-01-01201510.1155/2015/296149296149Secretion of S100A8, S100A9, and S100A12 by Neutrophils Involves Reactive Oxygen Species and Potassium EffluxMélanie R. Tardif0Julie Andrea Chapeton-Montes1Alma Posvandzic2Nathalie Pagé3Caroline Gilbert4Philippe A. Tessier5Axe de Recherche sur les Maladies Infectieuses et L’immunologie, Centre de Recherche du CHU de Québec-Université Laval, and Département de Microbiologie-Infectiologie et Immunologie, Faculté de Médecine, Université Laval, Québec, QC, G1V 0A6, CanadaAxe de Recherche sur les Maladies Infectieuses et L’immunologie, Centre de Recherche du CHU de Québec-Université Laval, and Département de Microbiologie-Infectiologie et Immunologie, Faculté de Médecine, Université Laval, Québec, QC, G1V 0A6, CanadaAxe de Recherche sur les Maladies Infectieuses et L’immunologie, Centre de Recherche du CHU de Québec-Université Laval, and Département de Microbiologie-Infectiologie et Immunologie, Faculté de Médecine, Université Laval, Québec, QC, G1V 0A6, CanadaAxe de Recherche sur les Maladies Infectieuses et L’immunologie, Centre de Recherche du CHU de Québec-Université Laval, and Département de Microbiologie-Infectiologie et Immunologie, Faculté de Médecine, Université Laval, Québec, QC, G1V 0A6, CanadaAxe de Recherche sur les Maladies Infectieuses et L’immunologie, Centre de Recherche du CHU de Québec-Université Laval, and Département de Microbiologie-Infectiologie et Immunologie, Faculté de Médecine, Université Laval, Québec, QC, G1V 0A6, CanadaAxe de Recherche sur les Maladies Infectieuses et L’immunologie, Centre de Recherche du CHU de Québec-Université Laval, and Département de Microbiologie-Infectiologie et Immunologie, Faculté de Médecine, Université Laval, Québec, QC, G1V 0A6, CanadaS100A8/A9 (calprotectin) and S100A12 proinflammatory mediators are found at inflammatory sites and in the serum of patients with inflammatory or autoimmune diseases. These cytoplasmic proteins are secreted by neutrophils at sites of inflammation via alternative secretion pathways of which little is known. This study examined the nature of the stimuli leading to S100A8/A9 and S100A12 secretion as well as the mechanism involved in this alternative secretion pathway. Chemotactic agents, cytokines, and particulate molecules were used to stimulate human neutrophils. MSU crystals, PMA, and H2O2 induced the release of S100A8, S100A9, and S100A12 homodimers, as well as S100A8/A9 heterodimer. High concentrations of S100A8/A9 and S100A12 were secreted in response to nanoparticles like MSU, silica, TiO2, fullerene, and single-wall carbon nanotubes as well as in response to microbe-derived molecules, such as zymosan or HKCA. However, neutrophils exposed to the chemotactic factors fMLP failed to secrete S100A8/A9 or S100A12. Secretion of S100A8/A9 was dependent on the production of reactive oxygen species and required K+ exchanges through the ATP-sensitive K+ channel. Altogether, these findings suggest that S100A12 and S100A8/A9 are secreted independently either via distinct mechanisms of secretion or following the activation of different signal transduction pathways.http://dx.doi.org/10.1155/2015/296149 |
| spellingShingle | Mélanie R. Tardif Julie Andrea Chapeton-Montes Alma Posvandzic Nathalie Pagé Caroline Gilbert Philippe A. Tessier Secretion of S100A8, S100A9, and S100A12 by Neutrophils Involves Reactive Oxygen Species and Potassium Efflux Journal of Immunology Research |
| title | Secretion of S100A8, S100A9, and S100A12 by Neutrophils Involves Reactive Oxygen Species and Potassium Efflux |
| title_full | Secretion of S100A8, S100A9, and S100A12 by Neutrophils Involves Reactive Oxygen Species and Potassium Efflux |
| title_fullStr | Secretion of S100A8, S100A9, and S100A12 by Neutrophils Involves Reactive Oxygen Species and Potassium Efflux |
| title_full_unstemmed | Secretion of S100A8, S100A9, and S100A12 by Neutrophils Involves Reactive Oxygen Species and Potassium Efflux |
| title_short | Secretion of S100A8, S100A9, and S100A12 by Neutrophils Involves Reactive Oxygen Species and Potassium Efflux |
| title_sort | secretion of s100a8 s100a9 and s100a12 by neutrophils involves reactive oxygen species and potassium efflux |
| url | http://dx.doi.org/10.1155/2015/296149 |
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