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rdf:type |
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lifeskim:mentions |
umls-concept:C0004083,
umls-concept:C0015744,
umls-concept:C0035647,
umls-concept:C0037083,
umls-concept:C0078058,
umls-concept:C0205263,
umls-concept:C0300423,
umls-concept:C0378796,
umls-concept:C0441712,
umls-concept:C1171892,
umls-concept:C1312062,
umls-concept:C1705297,
umls-concept:C1710082,
umls-concept:C2587213,
umls-concept:C2911691
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pubmed:issue |
4
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pubmed:dateCreated |
2002-4-12
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pubmed:abstractText |
Vascular endothelial (VE)-cadherin is endothelium specific, mediates homophilic adhesion, and is clustered at intercellular junctions. VE-cadherin is required for normal development of the vasculature in the embryo and for angiogenesis in the adult. Here, we report that VE-cadherin is associated with VE growth factor (VEGF) receptor-2 (VEGFR-2) on the exposure of endothelial cells to VEGF. The binding parallels receptor phosphorylation on tyrosine residues, which is maximal at 5 minutes and then declines within 30 minutes. Tyrosine phosphorylation of VE-cadherin was maximal at 30 minutes after the addition of the growth factor. At this time point, the protein could be coimmunoprecipitated with the adaptor protein Shc. Pull-down experiments with different Shc domains and mutants of the VE-cadherin cytoplasmic tail have shown that Shc binds to the carboxy-terminal domain of the VE-cadherin tail through its Src homology 2 domain (SH2). We found that Shc phosphorylation lasts longer in endothelial cells carrying a targeted null mutation in the VE-cadherin gene than in VE-cadherin-positive cells. These data suggest that VE-cadherin expression exerts a negative effect on Shc phosphorylation by VEGFR-2. We speculate that VE-cadherin binding to Shc promotes its dephosphorylation through associated phosphatases.
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
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/Endothelial Growth Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphokines,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Vascular Endothelial...,
http://linkedlifedata.com/resource/pubmed/chemical/SHC1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Shc Signaling Adaptor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Vascular Endothelial Growth Factor A,
http://linkedlifedata.com/resource/pubmed/chemical/Vascular Endothelial Growth Factors,
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 |
Apr
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pubmed:issn |
1524-4636
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
617-22
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11950700-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:11950700-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:11950700-Antigens, CD,
pubmed-meshheading:11950700-Cadherins,
pubmed-meshheading:11950700-Cytoskeletal Proteins,
pubmed-meshheading:11950700-Endothelial Growth Factors,
pubmed-meshheading:11950700-Endothelium, Vascular,
pubmed-meshheading:11950700-Humans,
pubmed-meshheading:11950700-Lymphokines,
pubmed-meshheading:11950700-Mutation,
pubmed-meshheading:11950700-Phosphorylation,
pubmed-meshheading:11950700-Proteins,
pubmed-meshheading:11950700-Receptor Protein-Tyrosine Kinases,
pubmed-meshheading:11950700-Receptors, Growth Factor,
pubmed-meshheading:11950700-Receptors, Vascular Endothelial Growth Factor,
pubmed-meshheading:11950700-Shc Signaling Adaptor Proteins,
pubmed-meshheading:11950700-Trans-Activators,
pubmed-meshheading:11950700-Vascular Endothelial Growth Factor A,
pubmed-meshheading:11950700-Vascular Endothelial Growth Factors,
pubmed-meshheading:11950700-beta Catenin,
pubmed-meshheading:11950700-src Homology Domains
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pubmed:year |
2002
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pubmed:articleTitle |
Vascular endothelial growth factor induces SHC association with vascular endothelial cadherin: a potential feedback mechanism to control vascular endothelial growth factor receptor-2 signaling.
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pubmed:affiliation |
Mario Negri Institute of Pharmacological Research, Milan, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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