| pubmed-article:15626732 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15626732 | lifeskim:mentions | umls-concept:C0014257 | lld:lifeskim |
| pubmed-article:15626732 | lifeskim:mentions | umls-concept:C1545588 | lld:lifeskim |
| pubmed-article:15626732 | lifeskim:mentions | umls-concept:C0483249 | lld:lifeskim |
| pubmed-article:15626732 | lifeskim:mentions | umls-concept:C0074992 | lld:lifeskim |
| pubmed-article:15626732 | lifeskim:mentions | umls-concept:C0173022 | lld:lifeskim |
| pubmed-article:15626732 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:15626732 | pubmed:dateCreated | 2005-4-1 | lld:pubmed |
| pubmed-article:15626732 | pubmed:abstractText | Endothelial cells normally form a dynamically regulated barrier at the blood-tissue interface, and breakdown of this barrier is a key pathogenic factor in inflammatory disorders such as sepsis. Pro-inflammatory signaling by the blood coagulation protease thrombin through protease activated receptor-1 (PAR1) can disrupt endothelial barrier integrity, whereas the bioactive lipid sphingosine 1-phosphate (S1P) recently has been demonstrated to have potent barrier protective effects. Activated protein C (APC) inhibits thrombin generation and has potent anti-inflammatory effects. Here, we show that APC enhanced endothelial barrier integrity in a dual-chamber system dependent on binding to endothelial protein C receptor, activation of PAR1, and activity of cellular sphingosine kinase. Small interfering RNA that targets sphingosine kinase-1 or S1P receptor-1 blocked this protective signaling by APC. Incubation of cells with PAR1 agonist peptide or low concentrations of thrombin (approximately 40 pM) had a similar barrier-enhancing effect. These results demonstrate that PAR1 activation on endothelial cells can have opposite biologic effects, reveal a role for cross-communication between the prototypical barrier-protective S1P and barrier-disruptive PAR1 pathway, and suggest that S1P receptor-1 mediates protective effects of APC in systemic inflammation. | lld:pubmed |
| pubmed-article:15626732 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15626732 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15626732 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15626732 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:15626732 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15626732 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15626732 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15626732 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15626732 | pubmed:issn | 0006-4971 | lld:pubmed |
| pubmed-article:15626732 | pubmed:author | pubmed-author:RiewaldMatthi... | lld:pubmed |
| pubmed-article:15626732 | pubmed:author | pubmed-author:FeistritzerCl... | lld:pubmed |
| pubmed-article:15626732 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15626732 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:15626732 | pubmed:volume | 105 | lld:pubmed |
| pubmed-article:15626732 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15626732 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15626732 | pubmed:pagination | 3178-84 | lld:pubmed |
| pubmed-article:15626732 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:15626732 | pubmed:meshHeading | pubmed-meshheading:15626732... | lld:pubmed |
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| pubmed-article:15626732 | pubmed:meshHeading | pubmed-meshheading:15626732... | lld:pubmed |
| pubmed-article:15626732 | pubmed:meshHeading | pubmed-meshheading:15626732... | lld:pubmed |
| pubmed-article:15626732 | pubmed:meshHeading | pubmed-meshheading:15626732... | lld:pubmed |
| pubmed-article:15626732 | pubmed:meshHeading | pubmed-meshheading:15626732... | lld:pubmed |
| pubmed-article:15626732 | pubmed:meshHeading | pubmed-meshheading:15626732... | lld:pubmed |
| pubmed-article:15626732 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15626732 | pubmed:articleTitle | Endothelial barrier protection by activated protein C through PAR1-dependent sphingosine 1-phosphate receptor-1 crossactivation. | lld:pubmed |
| pubmed-article:15626732 | pubmed:affiliation | Department of Immunology, The Scripps Research Institute, La Jolla, CA 92037, USA. | lld:pubmed |
| pubmed-article:15626732 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15626732 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15626732 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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