pubmed-article:14676308 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14676308 | lifeskim:mentions | umls-concept:C0699040 | lld:lifeskim |
pubmed-article:14676308 | lifeskim:mentions | umls-concept:C0134835 | lld:lifeskim |
pubmed-article:14676308 | lifeskim:mentions | umls-concept:C0001721 | lld:lifeskim |
pubmed-article:14676308 | lifeskim:mentions | umls-concept:C0806140 | lld:lifeskim |
pubmed-article:14676308 | lifeskim:mentions | umls-concept:C1136143 | lld:lifeskim |
pubmed-article:14676308 | lifeskim:mentions | umls-concept:C1704711 | lld:lifeskim |
pubmed-article:14676308 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:14676308 | pubmed:dateCreated | 2003-12-23 | lld:pubmed |
pubmed-article:14676308 | pubmed:abstractText | Flowing leukocytes roll on P-selectin that is mobilized from secretory granules to the surfaces of endothelial cells after stimulation with histamine or thrombin. Before it is internalized, P-selectin clusters in clathrin-coated pits, which enhances its ability to support leukocyte rolling. We found that thrombin and histamine induced comparable exocytosis of P-selectin on endothelial cells. However, compared with histamine, thrombin decreased the recruitment of P-selectin into clathrin-coated pits, slowed the internalization of P-selectin, and reduced the number and stability of neutrophils rolling on P-selectin. Significantly more RhoA was activated in thrombin- than in histamine-stimulated endothelial cells. Inhibitors of RhoA or its effector, Rho kinase, reversed thrombin's ability to inhibit the internalization and adhesive function of P-selectin in endothelial cells. Experiments with transfected cells confirmed that the inhibitory actions of thrombin and Rho kinase on P-selectin required its cytoplasmic domain. Thus, a signaling event affects both the function and clearance of a protein that enters the constitutive clathrin-mediated endocytic pathway. | lld:pubmed |
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pubmed-article:14676308 | pubmed:language | eng | lld:pubmed |
pubmed-article:14676308 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14676308 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:14676308 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:14676308 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14676308 | pubmed:month | Dec | lld:pubmed |
pubmed-article:14676308 | pubmed:issn | 0021-9525 | lld:pubmed |
pubmed-article:14676308 | pubmed:author | pubmed-author:McEverRodger... | lld:pubmed |
pubmed-article:14676308 | pubmed:author | pubmed-author:SetiadiHendra... | lld:pubmed |
pubmed-article:14676308 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:14676308 | pubmed:day | 22 | lld:pubmed |
pubmed-article:14676308 | pubmed:volume | 163 | lld:pubmed |
pubmed-article:14676308 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14676308 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14676308 | pubmed:pagination | 1385-95 | lld:pubmed |
pubmed-article:14676308 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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