NADPH oxidases as novel pharmacologic targets against influenza A virus infection.
Identifieur interne : 000450 ( PubMed/Corpus ); précédent : 000449; suivant : 000451NADPH oxidases as novel pharmacologic targets against influenza A virus infection.
Auteurs : Ross Vlahos ; Stavros SelemidisSource :
- Molecular pharmacology [ 1521-0111 ] ; 2014.
English descriptors
- KwdEn :
- Enzyme Inhibitors (therapeutic use), Humans, Influenza A virus (enzymology), Influenza, Human (drug therapy), Macrophages, Alveolar (enzymology), Membrane Glycoproteins (antagonists & inhibitors), Membrane Lipids (chemistry), NADPH Oxidase 2, NADPH Oxidases (antagonists & inhibitors), NADPH Oxidases (chemistry), NADPH Oxidases (physiology), Phospholipids (chemistry), Reactive Oxygen Species (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Membrane Glycoproteins, NADPH Oxidases.
- chemical , chemistry : Membrane Lipids, NADPH Oxidases, Phospholipids.
- chemical , metabolism : Reactive Oxygen Species.
- chemical , physiology : NADPH Oxidases.
- chemical , therapeutic use : Enzyme Inhibitors.
- drug therapy : Influenza, Human.
- enzymology : Influenza A virus, Macrophages, Alveolar.
- Humans, NADPH Oxidase 2.
Abstract
Influenza A viruses represent a major global health care challenge, with imminent pandemics, emerging antiviral resistance, and long lag times for vaccine development, raising a pressing need for novel pharmacologic strategies that ideally target the pathology irrespective of the infecting strain. Reactive oxygen species (ROS) pervade all facets of cell biology with both detrimental and protective properties. Indeed, there is compelling evidence that activation of the NADPH oxidase 2 (NOX2) isoform of the NADPH oxidase family of ROS-producing enzymes promotes lung oxidative stress, inflammation, injury, and dysfunction resulting from influenza A viruses of low to high pathogenicity, as well as impeding virus clearance. By contrast, the dual oxidase isoforms produce ROS that provide vital protective antiviral effects for the host. In this review, we propose that inhibitors of NOX2 are better alternatives than broad-spectrum antioxidant approaches for treatment of influenza pathologies, for which clinical efficacy may have been limited owing to poor bioavailability and inadvertent removal of beneficial ROS. Finally, we briefly describe the current suite of NADPH oxidase inhibitors and the molecular features of the NADPH oxidase enzymes that could be exploited by drug discovery for development of more specific and novel inhibitors to prevent or treat disease caused by influenza.
DOI: 10.1124/mol.114.095216
PubMed: 25301784
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pubmed:25301784Le document en format XML
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Reactive oxygen species (ROS) pervade all facets of cell biology with both detrimental and protective properties. Indeed, there is compelling evidence that activation of the NADPH oxidase 2 (NOX2) isoform of the NADPH oxidase family of ROS-producing enzymes promotes lung oxidative stress, inflammation, injury, and dysfunction resulting from influenza A viruses of low to high pathogenicity, as well as impeding virus clearance. By contrast, the dual oxidase isoforms produce ROS that provide vital protective antiviral effects for the host. In this review, we propose that inhibitors of NOX2 are better alternatives than broad-spectrum antioxidant approaches for treatment of influenza pathologies, for which clinical efficacy may have been limited owing to poor bioavailability and inadvertent removal of beneficial ROS. Finally, we briefly describe the current suite of NADPH oxidase inhibitors and the molecular features of the NADPH oxidase enzymes that could be exploited by drug discovery for development of more specific and novel inhibitors to prevent or treat disease caused by influenza. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25301784</PMID><DateCompleted><Year>2015</Year><Month>02</Month><Day>12</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1521-0111</ISSN><JournalIssue CitedMedium="Internet"><Volume>86</Volume><Issue>6</Issue><PubDate><Year>2014</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Molecular pharmacology</Title><ISOAbbreviation>Mol. Pharmacol.</ISOAbbreviation></Journal><ArticleTitle>NADPH oxidases as novel pharmacologic targets against influenza A virus infection.</ArticleTitle><Pagination><MedlinePgn>747-59</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1124/mol.114.095216</ELocationID><Abstract><AbstractText>Influenza A viruses represent a major global health care challenge, with imminent pandemics, emerging antiviral resistance, and long lag times for vaccine development, raising a pressing need for novel pharmacologic strategies that ideally target the pathology irrespective of the infecting strain. Reactive oxygen species (ROS) pervade all facets of cell biology with both detrimental and protective properties. Indeed, there is compelling evidence that activation of the NADPH oxidase 2 (NOX2) isoform of the NADPH oxidase family of ROS-producing enzymes promotes lung oxidative stress, inflammation, injury, and dysfunction resulting from influenza A viruses of low to high pathogenicity, as well as impeding virus clearance. By contrast, the dual oxidase isoforms produce ROS that provide vital protective antiviral effects for the host. In this review, we propose that inhibitors of NOX2 are better alternatives than broad-spectrum antioxidant approaches for treatment of influenza pathologies, for which clinical efficacy may have been limited owing to poor bioavailability and inadvertent removal of beneficial ROS. Finally, we briefly describe the current suite of NADPH oxidase inhibitors and the molecular features of the NADPH oxidase enzymes that could be exploited by drug discovery for development of more specific and novel inhibitors to prevent or treat disease caused by influenza. </AbstractText><CopyrightInformation>Copyright © 2014 by The American Society for Pharmacology and Experimental Therapeutics.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Vlahos</LastName><ForeName>Ross</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Respiratory Research Group, Lung Health Research Centre, Department of Pharmacology and Therapeutics, University of Melbourne (R.V.), and Oxidant and Inflammation Biology Group, Department of Pharmacology, Monash University (S.S.), Victoria, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Selemidis</LastName><ForeName>Stavros</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Respiratory Research Group, Lung Health Research Centre, Department of Pharmacology and Therapeutics, University of Melbourne (R.V.), and Oxidant and Inflammation Biology Group, Department of Pharmacology, Monash University (S.S.), Victoria, Australia Stavros.selemidis@monash.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>10</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol 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MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008563" MajorTopicYN="N">Membrane Lipids</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000074662" MajorTopicYN="N">NADPH Oxidase 2</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019255" MajorTopicYN="N">NADPH Oxidases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010743" MajorTopicYN="N">Phospholipids</DescriptorName><QualifierName UI="Q000737" 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