Source:http://linkedlifedata.com/resource/pubmed/id/15028767
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
11
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| pubmed:dateCreated |
2004-3-18
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| pubmed:abstractText |
Nerve growth factor (NGF) functions as a ligand for two receptors, the TrkA tyrosine kinase receptor and the p75 neurotrophin receptor (p75NTR). The Ig-like domains of Trk receptors and the cysteine-rich repeats of p75NTR are involved in binding to the neurotrophins. Recently, a closely related gene to p75NTR called neurotrophin receptor homolog-2 (NRH2) was identified; however, the function of NRH2 and its relevance to neurotrophin signaling are unclear. NRH2 contains a similar transmembrane and intracellular domain as p75NTR but lacks the characteristic cysteine-rich repeats in the extracellular domain. Here we show that NRH2 is expressed in several neuronal populations that also express p75NTR and Trk receptors. NRH2 does not bind to NGF; however, coimmunoprecipitation experiments demonstrate that NRH2 is capable of interacting with TrkA receptors. Coexpression of NRH2 with TrkA receptors resulted in the formation of high-affinity binding sites for NGF. These results indicate that a transmembrane protein related to p75NTR is capable of modulating Trk receptor binding properties.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/NRH2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Nerve Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, trkA,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Nerve Growth Factor
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| pubmed:status |
MEDLINE
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| pubmed:month |
Mar
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| pubmed:issn |
1529-2401
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:day |
17
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| pubmed:volume |
24
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
2742-9
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:15028767-Amino Acid Sequence,
pubmed-meshheading:15028767-Animals,
pubmed-meshheading:15028767-Animals, Newborn,
pubmed-meshheading:15028767-Cells, Cultured,
pubmed-meshheading:15028767-Cross-Linking Reagents,
pubmed-meshheading:15028767-Ganglia, Spinal,
pubmed-meshheading:15028767-Kidney,
pubmed-meshheading:15028767-Mice,
pubmed-meshheading:15028767-Molecular Sequence Data,
pubmed-meshheading:15028767-Nerve Growth Factor,
pubmed-meshheading:15028767-Neurons,
pubmed-meshheading:15028767-Organ Specificity,
pubmed-meshheading:15028767-Protein Binding,
pubmed-meshheading:15028767-Rats,
pubmed-meshheading:15028767-Receptor, Nerve Growth Factor,
pubmed-meshheading:15028767-Receptor, trkA,
pubmed-meshheading:15028767-Receptors, Nerve Growth Factor,
pubmed-meshheading:15028767-Sequence Homology, Amino Acid,
pubmed-meshheading:15028767-Spinal Cord
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| pubmed:year |
2004
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| pubmed:articleTitle |
A novel p75 neurotrophin receptor-related protein, NRH2, regulates nerve growth factor binding to the TrkA receptor.
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| pubmed:affiliation |
Skirball Institute of Bimolecular Medicine, New York University School of Medicine, New York, New York 10016, USA. s.murray@hfi.unimelb.edu.au
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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