| pubmed-article:20713593 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20713593 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
| pubmed-article:20713593 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:20713593 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:20713593 | lifeskim:mentions | umls-concept:C1514762 | lld:lifeskim |
| pubmed-article:20713593 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:20713593 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:20713593 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:20713593 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:20713593 | pubmed:dateCreated | 2010-8-31 | lld:pubmed |
| pubmed-article:20713593 | pubmed:abstractText | Filamin A (FlnA) cross-links actin filaments and connects the Von Willebrand factor receptor GPIb-IX-V to the underlying cytoskeleton in platelets. Because FlnA deficiency is embryonic lethal, mice lacking FlnA in platelets were generated by breeding FlnA(loxP/loxP) females with GATA1-Cre males. FlnA(loxP/y) GATA1-Cre males have a macrothrombocytopenia and increased tail bleeding times. FlnA-null platelets have decreased expression and altered surface distribution of GPIbalpha because they lack the normal cytoskeletal linkage of GPIbalpha to underlying actin filaments. This results in approximately 70% less platelet coverage on collagen-coated surfaces at shear rates of 1,500/s, compared with wild-type platelets. Unexpectedly, however, immunoreceptor tyrosine-based activation motif (ITAM)- and ITAM-like-mediated signals are severely compromised in FlnA-null platelets. FlnA-null platelets fail to spread and have decreased alpha-granule secretion, integrin alphaIIbbeta3 activation, and protein tyrosine phosphorylation, particularly that of the protein tyrosine kinase Syk and phospholipase C-gamma2, in response to stimulation through the collagen receptor GPVI and the C-type lectin-like receptor 2. This signaling defect was traced to the loss of a novel FlnA-Syk interaction, as Syk binds to FlnA at immunoglobulin-like repeat 5. Our findings reveal that the interaction between FlnA and Syk regulates ITAM- and ITAM-like-containing receptor signaling and platelet function. | lld:pubmed |
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| pubmed-article:20713593 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20713593 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20713593 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20713593 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20713593 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20713593 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:20713593 | pubmed:issn | 1540-9538 | lld:pubmed |
| pubmed-article:20713593 | pubmed:author | pubmed-author:WatsonSteve... | lld:pubmed |
| pubmed-article:20713593 | pubmed:author | pubmed-author:HartwigJohn... | lld:pubmed |
| pubmed-article:20713593 | pubmed:author | pubmed-author:WagnerDenisa... | lld:pubmed |
| pubmed-article:20713593 | pubmed:author | pubmed-author:FaletHervéH | lld:pubmed |
| pubmed-article:20713593 | pubmed:author | pubmed-author:DuerschmiedDa... | lld:pubmed |
| pubmed-article:20713593 | pubmed:author | pubmed-author:BegonjaAntoni... | lld:pubmed |
| pubmed-article:20713593 | pubmed:author | pubmed-author:WeberSarah... | lld:pubmed |
| pubmed-article:20713593 | pubmed:author | pubmed-author:PollittAlice... | lld:pubmed |
| pubmed-article:20713593 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20713593 | pubmed:day | 30 | lld:pubmed |
