rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
36
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pubmed:dateCreated |
2005-9-8
|
pubmed:abstractText |
Reelin, a large protein that regulates neuronal migration during embryonic development, activates a conserved signaling pathway that requires its receptors, very low-density lipoprotein receptor and apolipoprotein E receptor 2, the cytoplasmic adaptor protein Disabled-1 (Dab1), and Src family kinases (SFK). Reelin also markedly enhances long-term potentiation in the adult hippocampus, suggesting that this developmental signaling pathway can physiologically modulate learning and behavior. Here, we show that Reelin can regulate NMDA-type glutamate receptor activity through a mechanism that requires SFKs and Dab1. Reelin mediates tyrosine phosphorylation of and potentiates calcium influx through NMDA receptors in primary wild-type cortical neurons but not in Dab1 knock-out neurons or in cells in which Reelin binding to its receptors is blocked by a receptor antagonist. Inhibition of SFK abolishes Reelin-induced and glutamate-dependent enhancement of calcium influx. We also show that Reelin-induced augmentation of Ca2+ entry through NMDA receptors increases phosphorylation and nuclear translocation of the transcription factor cAMP-response element binding protein. Thus, Reelin may physiologically modulate learning and memory by modulating NMDA receptor functions.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/6-Cyano-7-nitroquinoxaline-2,3-dione,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules, Neuronal,
http://linkedlifedata.com/resource/pubmed/chemical/Excitatory Amino Acid Antagonists,
http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Matrix Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, N-Methyl-D-Aspartate,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/reelin protein
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
|
pubmed:issn |
1529-2401
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pubmed:author |
|
pubmed:issnType |
Electronic
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pubmed:day |
7
|
pubmed:volume |
25
|
pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8209-16
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16148228-6-Cyano-7-nitroquinoxaline-2,3-dione,
pubmed-meshheading:16148228-Animals,
pubmed-meshheading:16148228-Cell Adhesion Molecules, Neuronal,
pubmed-meshheading:16148228-Cerebral Cortex,
pubmed-meshheading:16148228-Excitatory Amino Acid Antagonists,
pubmed-meshheading:16148228-Extracellular Matrix Proteins,
pubmed-meshheading:16148228-Female,
pubmed-meshheading:16148228-Mice,
pubmed-meshheading:16148228-Nerve Tissue Proteins,
pubmed-meshheading:16148228-Neurons,
pubmed-meshheading:16148228-Pregnancy,
pubmed-meshheading:16148228-Rats,
pubmed-meshheading:16148228-Rats, Sprague-Dawley,
pubmed-meshheading:16148228-Receptors, N-Methyl-D-Aspartate,
pubmed-meshheading:16148228-Serine Endopeptidases,
pubmed-meshheading:16148228-Signal Transduction,
pubmed-meshheading:16148228-Synaptic Transmission
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pubmed:year |
2005
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pubmed:articleTitle |
Reelin modulates NMDA receptor activity in cortical neurons.
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pubmed:affiliation |
Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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