| pubmed-article:17332246 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17332246 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:17332246 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
| pubmed-article:17332246 | lifeskim:mentions | umls-concept:C0032191 | lld:lifeskim |
| pubmed-article:17332246 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:17332246 | lifeskim:mentions | umls-concept:C0001721 | lld:lifeskim |
| pubmed-article:17332246 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:17332246 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:17332246 | lifeskim:mentions | umls-concept:C0178587 | lld:lifeskim |
| pubmed-article:17332246 | lifeskim:mentions | umls-concept:C0332261 | lld:lifeskim |
| pubmed-article:17332246 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:17332246 | pubmed:dateCreated | 2007-6-7 | lld:pubmed |
| pubmed-article:17332246 | pubmed:abstractText | The impact of ligand density on integrin-mediated cell adhesion and outside-in signaling is not well understood. Using total internal reflection fluorescent microscopy, conformation-specific antibodies, and Ca(2+) flux measurements, we found that the surface density of fibrinogen affects alpha II b beta 3-mediated platelet signaling, adhesion, and spreading. Adhesion to fibrinogen immobilized at low density leads to rapid increases in cytosolic Ca(2+) and sequential formation of filopodia and lamellipodia. In contrast, adhesion to high-density fibrinogen results in transient or no increases in Ca(2+) and simultaneous formation of filopodia and lamellipodia. alpha II b beta 3 receptors at the basal surface of platelets engage fibrinogen in a ringlike pattern at the cell edges under both conditions. This engagement is, however, more dynamic and easily reversed on high-density fibrinogen. Src and Rac activity and actin polymerization are important for adhesion to low-density fibrinogen, whereas PKC/PI3 kinases contribute to platelet spreading on high-density fibrinogen. We conclude that 2 fundamentally different signaling mechanisms can be initiated by a single integrin receptor interacting with the same ligand when it is immobilized at different densities. | lld:pubmed |
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| pubmed-article:17332246 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17332246 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17332246 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:17332246 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17332246 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17332246 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:17332246 | pubmed:issn | 0006-4971 | lld:pubmed |
| pubmed-article:17332246 | pubmed:author | pubmed-author:CollerBarry... | lld:pubmed |
| pubmed-article:17332246 | pubmed:author | pubmed-author:JaiswalJyoti... | lld:pubmed |
| pubmed-article:17332246 | pubmed:author | pubmed-author:JirouskováMar... | lld:pubmed |
| pubmed-article:17332246 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17332246 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:17332246 | pubmed:volume | 109 | lld:pubmed |
| pubmed-article:17332246 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17332246 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17332246 | pubmed:pagination | 5260-9 | lld:pubmed |
| pubmed-article:17332246 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:17332246 | pubmed:meshHeading | pubmed-meshheading:17332246... | lld:pubmed |
| pubmed-article:17332246 | pubmed:meshHeading | pubmed-meshheading:17332246... | lld:pubmed |
