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rdf:type |
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lifeskim:mentions |
umls-concept:C0007226,
umls-concept:C0023688,
umls-concept:C0031437,
umls-concept:C0205369,
umls-concept:C0332516,
umls-concept:C0386040,
umls-concept:C0596988,
umls-concept:C0597357,
umls-concept:C1167322,
umls-concept:C1414431,
umls-concept:C1527148,
umls-concept:C2752508
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pubmed:issue |
3
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pubmed:dateCreated |
1999-10-29
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pubmed:abstractText |
Ephrin-B2 is a transmembrane ligand that is specifically expressed on arteries but not veins and that is essential for cardiovascular development. However, ephrin-B2 is also expressed in nonvascular tissues and interacts with multiple EphB class receptors expressed in both endothelial and nonendothelial cell types. Thus, the identity of the relevant receptor for ephrin-B2 and the site(s) where these molecules interact to control angiogenesis were not clear. Here we show that EphB4, a specific receptor for ephrin-B2, is exclusively expressed by vascular endothelial cells in embryos and is preferentially expressed on veins. A targeted mutation in EphB4 essentially phenocopies the mutation in ephrin-B2. These data indicate that ephrin-B2-EphB4 interactions are intrinsically required in vascular endothelial cells and are consistent with the idea that they mediate bidirectional signaling essential for angiogenesis.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
403-14
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10518221-Animals,
pubmed-meshheading:10518221-Arteries,
pubmed-meshheading:10518221-Blood Circulation,
pubmed-meshheading:10518221-Cardiovascular System,
pubmed-meshheading:10518221-Endothelium, Vascular,
pubmed-meshheading:10518221-Ephrin-B2,
pubmed-meshheading:10518221-Genotype,
pubmed-meshheading:10518221-Head,
pubmed-meshheading:10518221-Heart,
pubmed-meshheading:10518221-Heterozygote,
pubmed-meshheading:10518221-Ligands,
pubmed-meshheading:10518221-Membrane Proteins,
pubmed-meshheading:10518221-Mice,
pubmed-meshheading:10518221-Mice, Inbred C57BL,
pubmed-meshheading:10518221-Mice, Mutant Strains,
pubmed-meshheading:10518221-Morphogenesis,
pubmed-meshheading:10518221-Mutagenesis, Site-Directed,
pubmed-meshheading:10518221-Myocardial Contraction,
pubmed-meshheading:10518221-Neovascularization, Physiologic,
pubmed-meshheading:10518221-Phenotype,
pubmed-meshheading:10518221-Receptor, EphB2,
pubmed-meshheading:10518221-Receptor Protein-Tyrosine Kinases,
pubmed-meshheading:10518221-Restriction Mapping,
pubmed-meshheading:10518221-Tissue Distribution,
pubmed-meshheading:10518221-Veins,
pubmed-meshheading:10518221-Yolk Sac
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pubmed:year |
1999
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pubmed:articleTitle |
Symmetrical mutant phenotypes of the receptor EphB4 and its specific transmembrane ligand ephrin-B2 in cardiovascular development.
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pubmed:affiliation |
Division of Biology, Howard Hughes Medical Institute, California Institute of Technology, Pasadena 91125, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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