<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Arce FT</submitter><funding>NHLBI NIH HHS</funding><pagination>886-94</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2440433</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>95(2)</volume><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</pubmed_abstract><journal>Biophysical journal</journal><pubmed_title>Regulation of the micromechanical properties of pulmonary endothelium by S1P and thrombin: role of cortactin.</pubmed_title><pmcid>PMC2440433</pmcid><funding_grant_id>P01 HL058064</funding_grant_id><funding_grant_id>R01 HL088144</funding_grant_id><funding_grant_id>K08 HL070013</funding_grant_id><funding_grant_id>P01 HL 58064</funding_grant_id><funding_grant_id>KO8 HL70013</funding_grant_id><pubmed_authors>Arce FT</pubmed_authors><pubmed_authors>Lal R</pubmed_authors><pubmed_authors>Arnsdorf MF</pubmed_authors><pubmed_authors>Whitlock JL</pubmed_authors><pubmed_authors>Birukov KG</pubmed_authors><pubmed_authors>Garcia JG</pubmed_authors><pubmed_authors>Birukova AA</pubmed_authors><pubmed_authors>Dudek SM</pubmed_authors></additional><is_claimable>false</is_claimable><name>Regulation of the micromechanical properties of pulmonary endothelium by S1P and thrombin: role of cortactin.</name><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</description><dates><release>2008-01-01T00:00:00Z</release><publication>2008 Jul</publication><modification>2025-06-01T01:08:53.667Z</modification><creation>2019-06-06T18:36:38Z</creation></dates><accession>S-EPMC2440433</accession><cross_references><pubmed>18408039</pubmed><doi>10.1529/biophysj.107.127167</doi></cross_references></HashMap>