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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2000-3-30
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pubmed:abstractText |
Thrombin-mediated changes in endothelial cell adherens junctions modulate vascular permeability. We demonstrate that the nonreceptor protein-tyrosine phosphatase SHP2 co-precipitates with VE-cadherin complexes in confluent, quiescent human umbilical vein endothelial cells. Ligand-binding blots using a SHP2-glutathione S-transferase fusion peptide established that SHP2 associates selectively with beta-catenin in VE-cadherin complexes. Thrombin treatment of human umbilical vein endothelial cells promotes SHP2 tyrosine phosphorylation and dissociation from VE-cadherin complexes. The loss of SHP2 from the cadherin complexes correlates with a dramatic increase in the tyrosine phosphorylation of beta-catenin, gamma-catenin, and p120-catenin complexed with VE-cadherin. We propose that thrombin regulates the tyrosine phosphorylation of VE-cadherin-associated beta-catenin, gamma-catenin, and p120-catenin by modulating the quantity of SHP2 associated with VE-cadherin complexes. Such changes in adherens junction complex composition likely underlie thrombin-elicited alterations in endothelial monolayer permeability.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/CTNNB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hemostatics,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN11 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombin,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin,
http://linkedlifedata.com/resource/pubmed/chemical/cadherin 5
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5983-6
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10681592-Antigens, CD,
pubmed-meshheading:10681592-Cadherins,
pubmed-meshheading:10681592-Cytoskeletal Proteins,
pubmed-meshheading:10681592-Endothelium, Vascular,
pubmed-meshheading:10681592-Hemostatics,
pubmed-meshheading:10681592-Humans,
pubmed-meshheading:10681592-Immunoblotting,
pubmed-meshheading:10681592-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:10681592-Ligands,
pubmed-meshheading:10681592-Phosphorylation,
pubmed-meshheading:10681592-Precipitin Tests,
pubmed-meshheading:10681592-Protein Tyrosine Phosphatase, Non-Receptor Type 11,
pubmed-meshheading:10681592-Protein Tyrosine Phosphatase, Non-Receptor Type 6,
pubmed-meshheading:10681592-Protein Tyrosine Phosphatases,
pubmed-meshheading:10681592-Recombinant Fusion Proteins,
pubmed-meshheading:10681592-Thrombin,
pubmed-meshheading:10681592-Time Factors,
pubmed-meshheading:10681592-Trans-Activators,
pubmed-meshheading:10681592-Umbilical Veins,
pubmed-meshheading:10681592-beta Catenin
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pubmed:year |
2000
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pubmed:articleTitle |
SHP2 association with VE-cadherin complexes in human endothelial cells is regulated by thrombin.
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pubmed:affiliation |
Department of Physiology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107-6799, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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