Influenza Virus—Cytokine-Protease Cycle in the Pathogenesis of Vascular Hyperpermeability in Severe Influenza
Identifieur interne : 000D35 ( Main/Exploration ); précédent : 000D34; suivant : 000D36Influenza Virus—Cytokine-Protease Cycle in the Pathogenesis of Vascular Hyperpermeability in Severe Influenza
Auteurs : Siye Wang [Japon] ; Trong Quang Le [Japon] ; Naoki Kurihara [Japon] ; Junji Chida [Japon] ; Youssouf Cisse [Japon] ; Mihiro Yano [Japon] ; Hiroshi Kido [Japon]Source :
- The Journal of Infectious Diseases [ 0022-1899 ] ; 2010.
Abstract
Background. Severe influenza is characterized by cytokine storm and multiorgan failure with edema. The aim of this study was to define the impact of the cytokine storm on the pathogenesis of vascular hyperpermeability in severe influenza. Methods. Weanling mice were infected with influenza A WSN/33(H1N1) virus. The levels of proinflammatory cytokines, tumor necrosis factor (TNF) α, interleukin (IL) 6, IL-1β, and trypsin were analyzed in the lung, brain, heart, and cultured human umbilical vein endothelial cells. The effects of transcriptional inhibitors on cytokine and trypsin expressions and viral replication were determined. Results. Influenza A virus infection resulted in significant increases in TNF-α, IL-6, IL-1β, viral hemagglutininprocessing protease trypsin levels, and viral replication with vascular hyperpermeability in lung and brain in the first 6 days of infection. Trypsin upregulation was suppressed by transcriptional inhibition of cytokines in vivo and by anti-cytokine antibodies in endothelial cells. Calcium mobilization and loss of tight junction constituent, zonula occludens-1, associated with cytokine- and trypsin-induced endothelial hyperpermeability were inhibited by a protease-activated receptor-2 antagonist and a trypsin inhibitor. Conclusions. The influenza virus-cytokine-protease cycle is one of the key mechanisms of vascular hyperpermeability in severe influenza.
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DOI: 10.1086/656044
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Tokushima</wicri:regionArea><wicri:noRegion>Tokushima</wicri:noRegion></affiliation><affiliation></affiliation></author><author><name sortKey="Kurihara, Naoki" sort="Kurihara, Naoki" uniqKey="Kurihara N" first="Naoki" last="Kurihara">Naoki Kurihara</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Tokushima</wicri:regionArea><wicri:noRegion>Tokushima</wicri:noRegion></affiliation></author><author><name sortKey="Chida, Junji" sort="Chida, Junji" uniqKey="Chida J" first="Junji" last="Chida">Junji Chida</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Tokushima</wicri:regionArea><wicri:noRegion>Tokushima</wicri:noRegion></affiliation></author><author><name sortKey="Cisse, Youssouf" sort="Cisse, Youssouf" uniqKey="Cisse Y" first="Youssouf" last="Cisse">Youssouf Cisse</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Tokushima</wicri:regionArea><wicri:noRegion>Tokushima</wicri:noRegion></affiliation></author><author><name sortKey="Yano, Mihiro" sort="Yano, Mihiro" uniqKey="Yano M" first="Mihiro" last="Yano">Mihiro Yano</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Tokushima</wicri:regionArea><wicri:noRegion>Tokushima</wicri:noRegion></affiliation></author><author><name sortKey="Kido, Hiroshi" sort="Kido, Hiroshi" uniqKey="Kido H" first="Hiroshi" last="Kido">Hiroshi Kido</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Tokushima</wicri:regionArea><wicri:noRegion>Tokushima</wicri:noRegion></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Japon</country></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">The Journal of Infectious Diseases</title><title level="j" type="abbrev">The Journal of Infectious Diseases</title><idno type="ISSN">0022-1899</idno><idno type="eISSN">1537-6613</idno><imprint><publisher>The University of Chicago Press</publisher><date when="2010-10-01">2010</date><biblScope unit="vol">202</biblScope><biblScope unit="issue">7</biblScope><biblScope unit="page" from="991">991</biblScope><biblScope unit="page" to="1001">1001</biblScope></imprint><idno type="ISSN">0022-1899</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0022-1899</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">Background. Severe influenza is characterized by cytokine storm and multiorgan failure with edema. The aim of this study was to define the impact of the cytokine storm on the pathogenesis of vascular hyperpermeability in severe influenza. Methods. Weanling mice were infected with influenza A WSN/33(H1N1) virus. The levels of proinflammatory cytokines, tumor necrosis factor (TNF) α, interleukin (IL) 6, IL-1β, and trypsin were analyzed in the lung, brain, heart, and cultured human umbilical vein endothelial cells. The effects of transcriptional inhibitors on cytokine and trypsin expressions and viral replication were determined. Results. Influenza A virus infection resulted in significant increases in TNF-α, IL-6, IL-1β, viral hemagglutininprocessing protease trypsin levels, and viral replication with vascular hyperpermeability in lung and brain in the first 6 days of infection. Trypsin upregulation was suppressed by transcriptional inhibition of cytokines in vivo and by anti-cytokine antibodies in endothelial cells. Calcium mobilization and loss of tight junction constituent, zonula occludens-1, associated with cytokine- and trypsin-induced endothelial hyperpermeability were inhibited by a protease-activated receptor-2 antagonist and a trypsin inhibitor. Conclusions. The influenza virus-cytokine-protease cycle is one of the key mechanisms of vascular hyperpermeability in severe influenza.</div></front></TEI><affiliations><list><country><li>Japon</li></country></list><tree><country name="Japon"><noRegion><name sortKey="Wang, Siye" sort="Wang, Siye" uniqKey="Wang S" first="Siye" last="Wang">Siye Wang</name></noRegion><name sortKey="Chida, Junji" sort="Chida, Junji" uniqKey="Chida J" first="Junji" last="Chida">Junji Chida</name><name sortKey="Cisse, Youssouf" sort="Cisse, Youssouf" uniqKey="Cisse Y" first="Youssouf" last="Cisse">Youssouf Cisse</name><name sortKey="Kido, Hiroshi" sort="Kido, Hiroshi" uniqKey="Kido H" first="Hiroshi" last="Kido">Hiroshi Kido</name><name sortKey="Kido, Hiroshi" sort="Kido, Hiroshi" uniqKey="Kido H" first="Hiroshi" last="Kido">Hiroshi Kido</name><name sortKey="Kurihara, Naoki" sort="Kurihara, Naoki" uniqKey="Kurihara N" first="Naoki" last="Kurihara">Naoki Kurihara</name><name sortKey="Le, Trong Quang" sort="Le, Trong Quang" uniqKey="Le T" first="Trong Quang" last="Le">Trong Quang Le</name><name sortKey="Yano, Mihiro" sort="Yano, Mihiro" uniqKey="Yano M" first="Mihiro" last="Yano">Mihiro Yano</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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