About: The serine protease inhibitor camostat inhibits influenza virus replication and cytokine production in primary cultures of human tracheal epithelial cells

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About: The serine protease inhibitor camostat inhibits influenza virus replication and cytokine production in primary cultures of human tracheal epithelial cells Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The serine protease inhibitor camostat inhibits influenza virus replication and cytokine production in primary cultures of human tracheal epithelial cells
Creator	Nishimura, Hidekazu Shimotai, Yoshitaka Yamaya, Mutsuo Kitajima, Yasuo Hatachi, Yukimasa Homma, Morio Hongo, Seiji Kubo, Hiroshi Matsuo, Kaori Nagatomi, Ryoichi Tando, Yukiko Kalonji, Nadine
Source	Elsevier; Medline; PMC
abstract	BACKGROUND: Serine proteases act through the proteolytic cleavage of the hemagglutinin (HA) of influenza viruses for the entry of influenza virus into cells, resulting in infection. However, the inhibitory effects of serine protease inhibitors on influenza virus infection of human airway epithelial cells, and on their production of inflammatory cytokines are unclear. METHODS: Primary cultures of human tracheal epithelial cells were treated with four types of serine protease inhibitors, including camostat, and infected with A/Sendai-H/108/2009/(H1N1) pdm09 or A/New York/55/2004(H3N2). RESULTS: Camostat reduced the amounts of influenza viruses in the supernatants and viral RNA in the cells. It reduced the cleavage of an influenza virus precursor protein, HA0, into the subunit HA1. Camostat also reduced the concentrations of the cytokines interleukin (IL)-6 and tumor necrosis factor (TNF)-α in the supernatants. Gabexate and aprotinin reduced the viral titers and RNA levels in the cells, and aprotinin reduced the concentrations of TNF-α in the supernatants. The proteases transmembrane protease serine S1 member (TMPRSS) 2 and HAT (human trypsin-like protease: TMPRSS11D), which are known to cleave HA0 and to activate the virus, were detected at the cell membrane and in the cytoplasm. mRNA encoding TMPRSS2, TMPRSS4 and TMPRSS11D was detectable in the cells, and the expression levels were not affected by camostat. CONCLUSIONS: These findings suggest that human airway epithelial cells express these serine proteases and that serine protease inhibitors, especially camostat, may reduce influenza viral replication and the resultant production of inflammatory cytokines possibly through inhibition of activities of these proteases.
has issue date	2015-07-10(xsd:dateTime)
bibo:doi	10.1016/j.pupt.2015.07.001
bibo:pmid	26166259
has license	no-cc
sha1sum (hex)	0da6e2166a2e2a6eae8147a6516b466b40ea47e9
schema:url	https://doi.org/10.1016/j.pupt.2015.07.001
resource representing a document's title	The serine protease inhibitor camostat inhibits influenza virus replication and cytokine production in primary cultures of human tracheal epithelial cells
has PubMed Central identifier	PMC7110702
has PubMed identifier	26166259
schema:publication	Pulm Pharmacol Ther
resource representing a document's body	covid:0da6e2166a2e2a6eae8147a6516b466b40ea47e9#body_text
is schema:about of	named entity 'SERINE PROTEASE INHIBITOR' named entity 'inhibits' named entity 'PRIMARY CULTURES' named entity 'CAMOSTAT' named entity 'INFLUENZA VIRUS' named entity 'TRACHEAL' named entity 'EPITHELIAL CELLS' named entity 'CYTOKINE PRODUCTION' named entity 'HUMAN' named entity 'VIRUS REPLICATION' named entity 'production' named entity 'serine protease inhibitor' named entity 'influenza viruses' named entity 'supernatants' named entity 'HTE' named entity 'cell cultures' named entity 'supernatant' named entity 'influenza virus' named entity 'protease inhibitors' named entity 'conjugated' named entity 'proteases' named entity 'TaqMan' named entity 'mRNA' named entity 'viruses' named entity 'sivelestat' named entity 'primers' named entity 'camostat' named entity 'viruses' named entity 'gabexate' named entity 'hemagglutinin' named entity 'proteases' named entity 'camostat' named entity 'enzyme immunoassay' named entity 'ng/mL' named entity 'serine proteases' named entity 'heterodimers' named entity 'influenza virus' named entity 'cytopathic effects' named entity 'gabexate' named entity 'nucleus' named entity 'camostat' named entity 'TMPRSS2' named entity 'pulmonary diseases' named entity 'viral replication' named entity 'TMPRSS11D' named entity 'glycoproteins' named entity 'IL-6' named entity 'influenza virus' named entity 'Carl Zeiss' named entity 'influenza A/H1N1' named entity 'sivelestat' named entity 'TNF-a' named entity 'inflammatory cytokine' named entity 'viral replication' named entity 'IL-6' named entity 'influenza viruses' named entity 'human influenza' named entity 'camostat' named entity 'supernatants' named entity 'aprotinin' named entity 'Carl Zeiss' named entity 'Sivelestat' named entity 'gabexate' named entity 'Aprotinin' named entity 'viruses' named entity 'sivelestat' named entity 'virus' named entity 'serine protease inhibitors' named entity 'camostat' named entity 'camostat'

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