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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1997-4-7
|
| pubmed:databankReference | |
| pubmed:abstractText |
Recent evidence suggests that Eph receptor tyrosine kinases and their ligands provide positional information in the developing visual system. We previously found that the Eph receptor Cek5 is more highly expressed in the ventral than dorsal chicken embryonic retina. We now report the identification of a chicken ligand for Cek5 (cCek5-L) that is 75% identical to the ligand LERK2. In situ hybridization experiments do not reveal a dorsoventral gradient of cCek5-L transcripts in the optic tectum at Embryonic Day 8, suggesting that this ligand is not involved in guiding Cek5-expressing axons in the tectum. Surprisingly, it is in the retina that high levels of cCek5-L mRNA are present. In the early retina, cCek5-L is more highly expressed in the dorsal than the ventral aspect. Similarly, a Cek5 Ig chimera labels dorsal but not ventral retina, indicating that even if several Cek5 ligands are present, their overall distribution is complementary to that of Cek5. Hence, Cek5 and cCek5-L may both contribute to define anatomical compartments within the early retina. In contrast, in the 11-day embryonic retina the distributions of Cek5 and its ligand(s) show considerable overlap, suggesting changing functions as development progresses. In dissociated cultures of dorsal or ventral retinal cells seeded on plates coated with either receptor or ligand Ig chimeras, the interaction between Cek5 and its ligand(s) or cCek5-L and its receptor(s) is sufficient to mediate cell adhesion and allows neurite outgrowth.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ephrin-B1,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, EphB2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0012-1606
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
182
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
256-69
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:9070326-Amino Acid Sequence,
pubmed-meshheading:9070326-Animals,
pubmed-meshheading:9070326-Cells, Cultured,
pubmed-meshheading:9070326-Chickens,
pubmed-meshheading:9070326-Cloning, Molecular,
pubmed-meshheading:9070326-Ephrin-B1,
pubmed-meshheading:9070326-Humans,
pubmed-meshheading:9070326-In Situ Hybridization,
pubmed-meshheading:9070326-Membrane Proteins,
pubmed-meshheading:9070326-Mice,
pubmed-meshheading:9070326-Molecular Sequence Data,
pubmed-meshheading:9070326-Proteins,
pubmed-meshheading:9070326-Receptor, EphB2,
pubmed-meshheading:9070326-Receptor Protein-Tyrosine Kinases,
pubmed-meshheading:9070326-Recombinant Fusion Proteins,
pubmed-meshheading:9070326-Retina,
pubmed-meshheading:9070326-Sequence Homology, Amino Acid,
pubmed-meshheading:9070326-Superior Colliculi
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
Reciprocal expression of the Eph receptor Cek5 and its ligand(s) in the early retina.
|
| pubmed:affiliation |
Burnham Institute, La Jolla, California 92037, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|