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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
2001-4-5
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pubmed:abstractText |
Eph receptors have been implicated in cell-to-cell interaction during embryogenesis. We generated EphA2 mutant mice using a gene trap method. Homozygous mutant mice developed short and kinky tails. In situ hybridization using a Brachyury probe found the notochord to be abnormally bifurcated at the caudal end between 11.5 and 12.5 days post coitum. EphA2 was expressed at the tip of the tail notochord, while one of its ligands, ephrinA1, was at the tail bud in normal mice. In contrast, EphA2-deficient notochordal cells were spread broadly into the tail bud. These observations suggest that EphA2 and its ligands are involved in the positioning of the tail notochord through repulsive signals between cells expressing these molecules on the surface.
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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/5-bromo-4-chloro-3-indolyl...,
http://linkedlifedata.com/resource/pubmed/chemical/Brachyury protein,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Ephrin-A1,
http://linkedlifedata.com/resource/pubmed/chemical/Fetal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Galactosides,
http://linkedlifedata.com/resource/pubmed/chemical/Hedgehog Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Indoles,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, EphA2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/T-Box Domain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0925-4773
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
102
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
95-105
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11287184-Animals,
pubmed-meshheading:11287184-Base Sequence,
pubmed-meshheading:11287184-Blotting, Northern,
pubmed-meshheading:11287184-Blotting, Southern,
pubmed-meshheading:11287184-Cell Communication,
pubmed-meshheading:11287184-DNA, Complementary,
pubmed-meshheading:11287184-Ephrin-A1,
pubmed-meshheading:11287184-Female,
pubmed-meshheading:11287184-Fetal Proteins,
pubmed-meshheading:11287184-Galactosides,
pubmed-meshheading:11287184-Genetic Vectors,
pubmed-meshheading:11287184-Hedgehog Proteins,
pubmed-meshheading:11287184-Homozygote,
pubmed-meshheading:11287184-In Situ Hybridization,
pubmed-meshheading:11287184-Indoles,
pubmed-meshheading:11287184-Ligands,
pubmed-meshheading:11287184-Male,
pubmed-meshheading:11287184-Mice,
pubmed-meshheading:11287184-Mice, Inbred C57BL,
pubmed-meshheading:11287184-Mice, Mutant Strains,
pubmed-meshheading:11287184-Mice, Transgenic,
pubmed-meshheading:11287184-Models, Genetic,
pubmed-meshheading:11287184-Molecular Sequence Data,
pubmed-meshheading:11287184-Notochord,
pubmed-meshheading:11287184-Phenotype,
pubmed-meshheading:11287184-Protein Binding,
pubmed-meshheading:11287184-Protein Biosynthesis,
pubmed-meshheading:11287184-Proteins,
pubmed-meshheading:11287184-Receptor, EphA2,
pubmed-meshheading:11287184-Receptor Protein-Tyrosine Kinases,
pubmed-meshheading:11287184-Signal Transduction,
pubmed-meshheading:11287184-T-Box Domain Proteins,
pubmed-meshheading:11287184-Tail,
pubmed-meshheading:11287184-Time Factors,
pubmed-meshheading:11287184-Trans-Activators,
pubmed-meshheading:11287184-Tretinoin
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pubmed:year |
2001
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pubmed:articleTitle |
Involvement of EphA2 in the formation of the tail notochord via interaction with ephrinA1.
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pubmed:affiliation |
Division of Cell Biology, Center for Experimental Medicine, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, 108-8639, Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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