Source:http://linkedlifedata.com/resource/pubmed/id/12118063
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
Pt 15
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| pubmed:dateCreated |
2002-7-15
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| pubmed:abstractText |
Ephrin-B/EphB family proteins are implicated in bidirectional signaling and were initially defined through the function of their ectodomain sequences in activating EphB receptor tyrosine kinases. Ephrin-B1-3 are transmembrane proteins sharing highly conserved C-terminal cytoplasmic sequences. Here we use a soluble EphB1 ectodomain fusion protein (EphB1/Fc) to demonstrate that ephrin-B1 transduces signals that regulate cell attachment and migration. EphB1/Fc induced endothelial ephrin-B1 tyrosine phosphorylation, migration and integrin-mediated (alpha(v)beta(3) and alpha(5)beta(1)) attachment and promoted neovascularization, in vivo, in a mouse corneal micropocket assay. Activation of ephrin-B1 by EphB1/Fc induced phosphorylation of p46 JNK but not ERK-1/2 or p38 MAPkinases. By contrast, mutant ephrin-B1s bearing either a cytoplasmic deletion (ephrin-B1DeltaCy) or a deletion of four C-terminal amino acids (ephrin-B1DeltaPDZbd) fail to activate p46 JNK. Transient expression of intact ephin-B1 conferred EphB1/Fc migration responses on CHO cells, whereas the ephrin-B1DeltaCy and ephrin-B1DeltaPDZbd mutants were inactive. Thus ephrin-B1 transduces 'outside-in' signals through C-terminal protein interactions that affect integrin-mediated attachment and migration.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Aug
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| pubmed:issn |
0021-9533
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
1
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| pubmed:volume |
115
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
3073-81
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:12118063-Amino Acid Sequence,
pubmed-meshheading:12118063-Animals,
pubmed-meshheading:12118063-CHO Cells,
pubmed-meshheading:12118063-Cell Adhesion,
pubmed-meshheading:12118063-Cell Membrane,
pubmed-meshheading:12118063-Cell Movement,
pubmed-meshheading:12118063-Cornea,
pubmed-meshheading:12118063-Cricetinae,
pubmed-meshheading:12118063-Endothelium, Vascular,
pubmed-meshheading:12118063-Ephrin-B1,
pubmed-meshheading:12118063-Humans,
pubmed-meshheading:12118063-Integrins,
pubmed-meshheading:12118063-MAP Kinase Signaling System,
pubmed-meshheading:12118063-Male,
pubmed-meshheading:12118063-Mice,
pubmed-meshheading:12118063-Mutation,
pubmed-meshheading:12118063-Neovascularization, Physiologic,
pubmed-meshheading:12118063-Organ Culture Techniques,
pubmed-meshheading:12118063-Phosphorylation,
pubmed-meshheading:12118063-Protein Structure, Tertiary,
pubmed-meshheading:12118063-Receptor, EphB1,
pubmed-meshheading:12118063-Recombinant Fusion Proteins,
pubmed-meshheading:12118063-Signal Transduction
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| pubmed:year |
2002
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| pubmed:articleTitle |
Ephrin-B1 transduces signals to activate integrin-mediated migration, attachment and angiogenesis.
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| pubmed:affiliation |
Vanderbilt-Ingram Cancer Center, Departments of Medicine, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
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| pubmed:publicationType |
Journal Article
|