Redox-active protein thioredoxin-1 administration ameliorates influenza A virus (H1N1)-induced acute lung injury in mice.
Identifieur interne : 000543 ( PubMed/Curation ); précédent : 000542; suivant : 000544Redox-active protein thioredoxin-1 administration ameliorates influenza A virus (H1N1)-induced acute lung injury in mice.
Auteurs : Masato Yashiro [Japon] ; Hirokazu Tsukahara ; Akihiro Matsukawa ; Mutsuko Yamada ; Yosuke Fujii ; Yoshiharu Nagaoka ; Mitsuru Tsuge ; Nobuko Yamashita ; Toshihiro Ito ; Masao Yamada ; Hiroshi Masutani ; Junji Yodoi ; Tsuneo MorishimaSource :
- Critical care medicine [ 1530-0293 ] ; 2013.
Descripteurs français
- KwdFr :
- Analyse de survie, Animaux, Antioxydants (pharmacologie), Antioxydants (usage thérapeutique), Charge virale (), Chimiokine CXCL1 (), Chimiokine CXCL1 (métabolisme), Facteur de nécrose tumorale alpha (), Facteur de nécrose tumorale alpha (métabolisme), Grippe humaine (traitement médicamenteux), Humains, Infiltration par les neutrophiles (), Lésion pulmonaire aigüe (anatomopathologie), Lésion pulmonaire aigüe (immunologie), Lésion pulmonaire aigüe (traitement médicamenteux), Lésion pulmonaire aigüe (virologie), Mâle, Pneumopathie virale (traitement médicamenteux), Protéines recombinantes (pharmacologie), Protéines recombinantes (usage thérapeutique), Souris, Souris de lignée C57BL, Sous-type H1N1 du virus de la grippe A, Thiorédoxines (pharmacologie), Thiorédoxines (usage thérapeutique), Études prospectives.
- MESH :
- anatomopathologie : Lésion pulmonaire aigüe.
- immunologie : Lésion pulmonaire aigüe.
- métabolisme : Chimiokine CXCL1, Facteur de nécrose tumorale alpha.
- pharmacologie : Antioxydants, Protéines recombinantes, Thiorédoxines.
- traitement médicamenteux : Grippe humaine, Lésion pulmonaire aigüe, Pneumopathie virale.
- usage thérapeutique : Antioxydants, Protéines recombinantes, Thiorédoxines.
- virologie : Lésion pulmonaire aigüe.
- Analyse de survie, Animaux, Charge virale, Chimiokine CXCL1, Facteur de nécrose tumorale alpha, Humains, Infiltration par les neutrophiles, Mâle, Souris, Souris de lignée C57BL, Sous-type H1N1 du virus de la grippe A, Études prospectives.
English descriptors
- KwdEn :
- Acute Lung Injury (drug therapy), Acute Lung Injury (immunology), Acute Lung Injury (pathology), Acute Lung Injury (virology), Animals, Antioxidants (pharmacology), Antioxidants (therapeutic use), Chemokine CXCL1 (drug effects), Chemokine CXCL1 (metabolism), Humans, Influenza A Virus, H1N1 Subtype, Influenza, Human (drug therapy), Male, Mice, Mice, Inbred C57BL, Neutrophil Infiltration (drug effects), Pneumonia, Viral (drug therapy), Prospective Studies, Recombinant Proteins (pharmacology), Recombinant Proteins (therapeutic use), Survival Analysis, Thioredoxins (pharmacology), Thioredoxins (therapeutic use), Tumor Necrosis Factor-alpha (drug effects), Tumor Necrosis Factor-alpha (metabolism), Viral Load (drug effects).
- MESH :
- chemical , drug effects : Chemokine CXCL1, Tumor Necrosis Factor-alpha.
- chemical , metabolism : Chemokine CXCL1, Tumor Necrosis Factor-alpha.
- chemical , pharmacology : Antioxidants, Recombinant Proteins, Thioredoxins.
- drug effects : Neutrophil Infiltration, Viral Load.
- drug therapy : Acute Lung Injury, Influenza, Human, Pneumonia, Viral.
- immunology : Acute Lung Injury.
- pathology : Acute Lung Injury.
- chemical , therapeutic use : Antioxidants, Recombinant Proteins, Thioredoxins.
- virology : Acute Lung Injury.
- Animals, Humans, Influenza A Virus, H1N1 Subtype, Male, Mice, Mice, Inbred C57BL, Prospective Studies, Survival Analysis.
Abstract
Influenza virus infections can cause severe acute lung injury leading to significant morbidity and mortality. Thioredoxin-1 is a redox-active defensive protein induced in response to stress conditions. Animal experiments have revealed that thioredoxin-1 has protective effects against various severe disorders. This study was undertaken to evaluate the protective effects of recombinant human thioredoxin-1 administration on influenza A virus (H1N1)-induced acute lung injury in mice.
DOI: 10.1097/CCM.0b013e3182676352
PubMed: 23222257
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pubmed:23222257Le document en format XML
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<term>Chemokine CXCL1 (metabolism)</term>
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<term>Thiorédoxines (usage thérapeutique)</term>
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<front><div type="abstract" xml:lang="en">Influenza virus infections can cause severe acute lung injury leading to significant morbidity and mortality. Thioredoxin-1 is a redox-active defensive protein induced in response to stress conditions. Animal experiments have revealed that thioredoxin-1 has protective effects against various severe disorders. This study was undertaken to evaluate the protective effects of recombinant human thioredoxin-1 administration on influenza A virus (H1N1)-induced acute lung injury in mice.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23222257</PMID>
<DateCompleted><Year>2013</Year>
<Month>03</Month>
<Day>04</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>12</Month>
<Day>10</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1530-0293</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>41</Volume>
<Issue>1</Issue>
<PubDate><Year>2013</Year>
<Month>Jan</Month>
</PubDate>
</JournalIssue>
<Title>Critical care medicine</Title>
<ISOAbbreviation>Crit. Care Med.</ISOAbbreviation>
</Journal>
<ArticleTitle>Redox-active protein thioredoxin-1 administration ameliorates influenza A virus (H1N1)-induced acute lung injury in mice.</ArticleTitle>
<Pagination><MedlinePgn>171-81</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1097/CCM.0b013e3182676352</ELocationID>
<Abstract><AbstractText Label="OBJECTIVES" NlmCategory="OBJECTIVE">Influenza virus infections can cause severe acute lung injury leading to significant morbidity and mortality. Thioredoxin-1 is a redox-active defensive protein induced in response to stress conditions. Animal experiments have revealed that thioredoxin-1 has protective effects against various severe disorders. This study was undertaken to evaluate the protective effects of recombinant human thioredoxin-1 administration on influenza A virus (H1N1)-induced acute lung injury in mice.</AbstractText>
<AbstractText Label="DESIGN" NlmCategory="METHODS">Prospective animal trial.</AbstractText>
<AbstractText Label="SETTING" NlmCategory="METHODS">Research laboratory.</AbstractText>
<AbstractText Label="SUBJECTS" NlmCategory="METHODS">Nine-week-old male C57BL/6 mice inoculated with H1N1.</AbstractText>
<AbstractText Label="INTERVENTION" NlmCategory="METHODS">The mice were divided into a vehicle-treated group and recombinant human thioredoxin-1-treated group. For survival rate analysis, the vehicle or recombinant human thioredoxin-1 was administered intraperitoneally every second day from day -1 to day 13. For lung lavage and pathological analyses, vehicle or recombinant human thioredoxin-1 was administered intraperitoneally on days -1, 1, and 3.</AbstractText>
<AbstractText Label="MEASUREMENTS AND MAIN RESULTS" NlmCategory="RESULTS">Lung lavage and pathological analyses were performed at 24, 72, and 120 hrs after inoculation. The recombinant human thioredoxin-1 treatment significantly improved the survival rate of H1N1-inoculated mice, although the treatment did not affect virus propagation in the lung. The treatment significantly attenuated the histological changes and neutrophil infiltration in the lung of H1N1-inoculated mice. The treatment significantly attenuated the production of tumor necrosis factor-α and chemokine (C-X-C motif) ligand 1 in the lung and oxidative stress enhancement, which were observed in H1N1-inoculated mice. H1N1 induced expressions of tumor necrosis factor-α and chemokine (C-X-C motif) ligand 1 in murine lung epithelial cells MLE-12, which were inhibited by the addition of recombinant human thioredoxin-1. The recombinant human thioredoxin-1 treatment started 30 mins after H1N1 inoculation also significantly improved the survival of the mice.</AbstractText>
<AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">Exogenous administration of recombinant human thioredoxin-1 significantly improved the survival rate and attenuated lung histological changes in the murine model of influenza pneumonia. The protective mechanism of thioredoxin-1 might be explained by its potent antioxidative and anti-inflammatory actions. Consequently, recombinant human thioredoxin-1 might be a possible pharmacological strategy for severe influenza virus infection in humans.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yashiro</LastName>
<ForeName>Masato</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Department of Pediatrics, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Tsukahara</LastName>
<ForeName>Hirokazu</ForeName>
<Initials>H</Initials>
</Author>
<Author ValidYN="Y"><LastName>Matsukawa</LastName>
<ForeName>Akihiro</ForeName>
<Initials>A</Initials>
</Author>
<Author ValidYN="Y"><LastName>Yamada</LastName>
<ForeName>Mutsuko</ForeName>
<Initials>M</Initials>
</Author>
<Author ValidYN="Y"><LastName>Fujii</LastName>
<ForeName>Yosuke</ForeName>
<Initials>Y</Initials>
</Author>
<Author ValidYN="Y"><LastName>Nagaoka</LastName>
<ForeName>Yoshiharu</ForeName>
<Initials>Y</Initials>
</Author>
<Author ValidYN="Y"><LastName>Tsuge</LastName>
<ForeName>Mitsuru</ForeName>
<Initials>M</Initials>
</Author>
<Author ValidYN="Y"><LastName>Yamashita</LastName>
<ForeName>Nobuko</ForeName>
<Initials>N</Initials>
</Author>
<Author ValidYN="Y"><LastName>Ito</LastName>
<ForeName>Toshihiro</ForeName>
<Initials>T</Initials>
</Author>
<Author ValidYN="Y"><LastName>Yamada</LastName>
<ForeName>Masao</ForeName>
<Initials>M</Initials>
</Author>
<Author ValidYN="Y"><LastName>Masutani</LastName>
<ForeName>Hiroshi</ForeName>
<Initials>H</Initials>
</Author>
<Author ValidYN="Y"><LastName>Yodoi</LastName>
<ForeName>Junji</ForeName>
<Initials>J</Initials>
</Author>
<Author ValidYN="Y"><LastName>Morishima</LastName>
<ForeName>Tsuneo</ForeName>
<Initials>T</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D023362">Evaluation Study</PublicationType>
<PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
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<MedlineTA>Crit Care Med</MedlineTA>
<NlmUniqueID>0355501</NlmUniqueID>
<ISSNLinking>0090-3493</ISSNLinking>
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<NameOfSubstance UI="D000975">Antioxidants</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054360">Chemokine CXCL1</NameOfSubstance>
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<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
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