{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Arce FT"],"funding":["NHLBI NIH HHS"],"pagination":["886-94"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2440433"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["95(2)"],"pubmed_abstract":["Disruption of pulmonary endothelial cell (EC) barrier function is a critical pathophysiologic event in highly morbid inflammatory conditions such as sepsis and acute respiratory disease stress syndrome. Actin cytoskeleton, an essential regulator of endothelial permeability, is a dynamic structure whose stimuli-induced rearrangement is linked to barrier modulation. Here, we used atomic force microscopy to characterize structural and mechanical changes in the F-actin cytoskeleton of cultured human pulmonary artery EC in response to both barrier-enhancing (induced by sphingosine 1-phosphate (S1P)) and barrier-disrupting (induced by thrombin) conditions. Atomic force microscopy elasticity measurements show differential effects: for the barrier protecting molecule S1P, the elastic modulus was e"],"journal":["Biophysical journal"],"pubmed_title":["Regulation of the micromechanical properties of pulmonary endothelium by S1P and thrombin: role of cortactin."],"pmcid":["PMC2440433"],"funding_grant_id":["P01 HL058064","R01 HL088144","K08 HL070013","P01 HL 58064","KO8 HL70013"],"pubmed_authors":["Arce FT","Lal R","Arnsdorf MF","Whitlock JL","Birukov KG","Garcia JG","Birukova AA","Dudek SM"],"additional_accession":[]},"is_claimable":false,"name":"Regulation of the micromechanical properties of pulmonary endothelium by S1P and thrombin: role of cortactin.","description":"Disruption of pulmonary endothelial cell (EC) barrier function is a critical pathophysiologic event in highly morbid inflammatory conditions such as sepsis and acute respiratory disease stress syndrome. Actin cytoskeleton, an essential regulator of endothelial permeability, is a dynamic structure whose stimuli-induced rearrangement is linked to barrier modulation. Here, we used atomic force microscopy to characterize structural and mechanical changes in the F-actin cytoskeleton of cultured human pulmonary artery EC in response to both barrier-enhancing (induced by sphingosine 1-phosphate (S1P)) and barrier-disrupting (induced by thrombin) conditions. Atomic force microscopy elasticity measurements show differential effects: for the barrier protecting molecule S1P, the elastic modulus was e","dates":{"release":"2008-01-01T00:00:00Z","publication":"2008 Jul","modification":"2025-06-01T01:08:53.667Z","creation":"2019-06-06T18:36:38Z"},"accession":"S-EPMC2440433","cross_references":{"pubmed":["18408039"],"doi":["10.1529/biophysj.107.127167"]}}