| pubmed-article:9366396 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9366396 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:9366396 | lifeskim:mentions | umls-concept:C0022688 | lld:lifeskim |
| pubmed-article:9366396 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
| pubmed-article:9366396 | lifeskim:mentions | umls-concept:C0135575 | lld:lifeskim |
| pubmed-article:9366396 | lifeskim:mentions | umls-concept:C1138422 | lld:lifeskim |
| pubmed-article:9366396 | lifeskim:mentions | umls-concept:C1416496 | lld:lifeskim |
| pubmed-article:9366396 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:9366396 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:9366396 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:9366396 | pubmed:dateCreated | 1997-11-25 | lld:pubmed |
| pubmed-article:9366396 | pubmed:abstractText | Recent evidence indicates that integrin ligation results in activation of focal adhesion kinase (pp125FAK), the prototype of a new subfamily of nonreceptor protein tyrosine kinase (PTK), including FAKB and the proline-rich tyrosine kinase 2 (PYK-2), also termed cell adhesion kinase-beta or related adhesion focal tyrosine kinase. We have previously shown that cross-linking of alpha 4 beta 1 and alpha 5 beta 1 fibronectin receptors on human NK cells stimulates tyrosine phosphorylation of two proteins migrating at 105 and 115 kDa. Here we report that cross-linking of beta 1 integrins on human NK cells stimulates tyrosine phosphorylation and PTK activity of PYK-2. PYK-2 tyrosine phosphorylation was maximal at 1 min and started to decline 20 min after stimulation. Engagement of alpha 4 beta 1 and alpha 5 beta 1 either with specific mAbs or after cell adhesion to fibronectin or its 120- and 40-kDa fragments also triggered PYK-2 tyrosine phosphorylation. Stimulation of PYK-2 tyrosine phosphorylation was inhibited by the tyrosine kinase inhibitor herbimycin A, but not by EGTA, indicating that PYK-2 tyrosine phosphorylation is PTK, but not calcium, dependent. We also demonstrate that PYK-2 is constitutively associated with paxillin, which undergoes tyrosine phosphorylation with the same kinetics of PYK-2 upon beta 1 integrin ligation. | lld:pubmed |
| pubmed-article:9366396 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9366396 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9366396 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:9366396 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9366396 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9366396 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9366396 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9366396 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9366396 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:9366396 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:9366396 | pubmed:author | pubmed-author:PalmieriGG | lld:pubmed |
| pubmed-article:9366396 | pubmed:author | pubmed-author:PiccoliMM | lld:pubmed |
| pubmed-article:9366396 | pubmed:author | pubmed-author:SantoniAA | lld:pubmed |
| pubmed-article:9366396 | pubmed:author | pubmed-author:FratiLL | lld:pubmed |
| pubmed-article:9366396 | pubmed:author | pubmed-author:GismondiAA | lld:pubmed |
| pubmed-article:9366396 | pubmed:author | pubmed-author:MainieroFF | lld:pubmed |
| pubmed-article:9366396 | pubmed:author | pubmed-author:BisognoLL | lld:pubmed |
| pubmed-article:9366396 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9366396 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:9366396 | pubmed:volume | 159 | lld:pubmed |
| pubmed-article:9366396 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9366396 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9366396 | pubmed:pagination | 4729-36 | lld:pubmed |
| pubmed-article:9366396 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:9366396 | pubmed:meshHeading | pubmed-meshheading:9366396-... | lld:pubmed |
| pubmed-article:9366396 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9366396 | pubmed:articleTitle | Proline-rich tyrosine kinase-2 activation by beta 1 integrin fibronectin receptor cross-linking and association with paxillin in human natural killer cells. | lld:pubmed |
| pubmed-article:9366396 | pubmed:affiliation | Department of Experimental Medicine and Pathology, University of Rome La Sapienza, Italy. | lld:pubmed |
| pubmed-article:9366396 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9366396 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:9366396 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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