|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
10
|
|
pubmed:dateCreated |
1997-11-25
|
|
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.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
AIM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigen-Antibody Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Focal Adhesion Kinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin alpha4beta1,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/PXN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Paxillin,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Ptk2b protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Pxn protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fibronectin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Lymphocyte Homing,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Nov
|
|
pubmed:issn |
0022-1767
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
15
|
|
pubmed:volume |
159
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
4729-36
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:9366396-Animals,
pubmed-meshheading:9366396-Antigen-Antibody Complex,
pubmed-meshheading:9366396-Calcium,
pubmed-meshheading:9366396-Cytoskeletal Proteins,
pubmed-meshheading:9366396-Focal Adhesion Kinase 2,
pubmed-meshheading:9366396-Humans,
pubmed-meshheading:9366396-Integrin alpha4beta1,
pubmed-meshheading:9366396-Integrins,
pubmed-meshheading:9366396-Jurkat Cells,
pubmed-meshheading:9366396-Killer Cells, Natural,
pubmed-meshheading:9366396-PC12 Cells,
pubmed-meshheading:9366396-Paxillin,
pubmed-meshheading:9366396-Phosphoproteins,
pubmed-meshheading:9366396-Phosphorylation,
pubmed-meshheading:9366396-Precipitin Tests,
pubmed-meshheading:9366396-Protein-Tyrosine Kinases,
pubmed-meshheading:9366396-Rats,
pubmed-meshheading:9366396-Receptors, Fibronectin,
pubmed-meshheading:9366396-Receptors, Lymphocyte Homing,
pubmed-meshheading:9366396-Tyrosine
|
|
pubmed:year |
1997
|
|
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.
|
|
pubmed:affiliation |
Department of Experimental Medicine and Pathology, University of Rome La Sapienza, Italy.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|
