{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Grinnell KL"],"funding":["NHLBI NIH HHS"],"pagination":["623-32"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3359908"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["46(5)"],"pubmed_abstract":["One hallmark of acute lung injury is the disruption of the pulmonary endothelial barrier. Such disruption correlates with increased endothelial permeability, partly through the disruption of cell-cell contacts. Protein tyrosine phosphatases (PTPs) are known to affect the stability of both cell-extracellular matrix adhesions and intercellular adherens junctions (AJs). However, evidence for the role of select PTPs in regulating endothelial permeability is limited. Our investigations noted that the inhibition of PTP1B in cultured pulmonary endothelial cells (ECs), as well as in the vasculature of intact murine lungs via the transient overexpression of a catalytically inactive PTP1B, decreased the baseline resistance of cultured EC monolayers and increased the formation of edema in murine lung"],"journal":["American journal of respiratory cell and molecular biology"],"pubmed_title":["Protection against LPS-induced pulmonary edema through the attenuation of protein tyrosine phosphatase-1B oxidation."],"pmcid":["PMC3359908"],"funding_grant_id":["R01 HL67795","T32 HL094300","R01 HL067795"],"pubmed_authors":["Braza J","Duong H","Grinnell KL","Harrington EO","Chichger H"],"additional_accession":[]},"is_claimable":false,"name":"Protection against LPS-induced pulmonary edema through the attenuation of protein tyrosine phosphatase-1B oxidation.","description":"One hallmark of acute lung injury is the disruption of the pulmonary endothelial barrier. Such disruption correlates with increased endothelial permeability, partly through the disruption of cell-cell contacts. Protein tyrosine phosphatases (PTPs) are known to affect the stability of both cell-extracellular matrix adhesions and intercellular adherens junctions (AJs). However, evidence for the role of select PTPs in regulating endothelial permeability is limited. Our investigations noted that the inhibition of PTP1B in cultured pulmonary endothelial cells (ECs), as well as in the vasculature of intact murine lungs via the transient overexpression of a catalytically inactive PTP1B, decreased the baseline resistance of cultured EC monolayers and increased the formation of edema in murine lung","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 May","modification":"2025-04-04T14:32:27.36Z","creation":"2019-03-27T00:53:52Z"},"accession":"S-EPMC3359908","cross_references":{"pubmed":["22180868"],"doi":["10.1165/rcmb.2011-0271OC","10.1165/rcmb.2011-0271oc"]}}