Source:http://linkedlifedata.com/resource/pubmed/id/18191896
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2008-2-18
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| pubmed:abstractText |
In the adult retina, N-methyl-D-aspartate (NMDA) neurotoxicity induces Müller cell reactive gliosis which is characterized by changes in gene expression that lead to proliferation and affect retinal physiology. The amino acid D-serine is synthesized in Müller cells and modulates these processes acting as a coagonist of NMDA receptors. We have found that the transcription factor DREAM (downstream regulatory element antagonist modulator), which acts as a transcriptional repressor by binding as a tetramer to regulatory elements located in the promoter region of target genes, is expressed in these cells and that its DNA-binding activity is modulated by NMDA receptor activation. Consistently, immunocytochemical analysis demonstrates that NMDA receptor activation induces changes in the nuclear localization of this transcription factor. DREAM is a pleiotropic transcription factor capable to repress and activate genes involved in several physiological events in different tissues. These results link, for the first time, this transcription factor with NMDA-receptor activation. Given the relevance of glutamatergic transmission in the retina and the remarkable functional plasticity of Müller cells, these findings support the notion that the NMDA receptor-dependent modulation of DREAM activity could play a role in relevant physiological processes ranging from retinal response to injury to differentiation capacity of retinal progenitor cells.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Csen protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Kv Channel-Interacting Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, N-Methyl-D-Aspartate,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0304-3940
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
20
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| pubmed:volume |
432
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
121-6
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| pubmed:meshHeading |
pubmed-meshheading:18191896-Active Transport, Cell Nucleus,
pubmed-meshheading:18191896-Animals,
pubmed-meshheading:18191896-Animals, Newborn,
pubmed-meshheading:18191896-Cell Differentiation,
pubmed-meshheading:18191896-Cells, Cultured,
pubmed-meshheading:18191896-DNA-Binding Proteins,
pubmed-meshheading:18191896-Down-Regulation,
pubmed-meshheading:18191896-Glutamic Acid,
pubmed-meshheading:18191896-Immunohistochemistry,
pubmed-meshheading:18191896-Kv Channel-Interacting Proteins,
pubmed-meshheading:18191896-Neuroglia,
pubmed-meshheading:18191896-Neuronal Plasticity,
pubmed-meshheading:18191896-Rats,
pubmed-meshheading:18191896-Rats, Long-Evans,
pubmed-meshheading:18191896-Receptors, N-Methyl-D-Aspartate,
pubmed-meshheading:18191896-Regulatory Elements, Transcriptional,
pubmed-meshheading:18191896-Repressor Proteins,
pubmed-meshheading:18191896-Retina,
pubmed-meshheading:18191896-Serine,
pubmed-meshheading:18191896-Signal Transduction,
pubmed-meshheading:18191896-Synaptic Transmission
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| pubmed:year |
2008
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| pubmed:articleTitle |
D-Serine/N-methyl-D-aspartate receptor signaling decreases DNA-binding activity of the transcriptional repressor DREAM in Müller glia from the retina.
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| pubmed:affiliation |
Departamento de Farmacobiología, Cinvestav Sede Sur, México DF, Mexico.
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| pubmed:publicationType |
Journal Article
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