| pubmed-article:15737330 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15737330 | lifeskim:mentions | umls-concept:C0043167 | lld:lifeskim |
| pubmed-article:15737330 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:15737330 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:15737330 | lifeskim:mentions | umls-concept:C0079281 | lld:lifeskim |
| pubmed-article:15737330 | lifeskim:mentions | umls-concept:C0017638 | lld:lifeskim |
| pubmed-article:15737330 | lifeskim:mentions | umls-concept:C0005528 | lld:lifeskim |
| pubmed-article:15737330 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:15737330 | lifeskim:mentions | umls-concept:C0220839 | lld:lifeskim |
| pubmed-article:15737330 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:15737330 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:15737330 | pubmed:dateCreated | 2005-3-1 | lld:pubmed |
| pubmed-article:15737330 | pubmed:abstractText | Endothelin-1 (ET-1) is a 21 amino acids peptide that exerts several biological activities through interaction with specific G-protein coupled receptors. Increased ET-1 expression is frequently associated with pathological situations involving alterations in glutamate levels. In the present study, a brief exposure to ET-1 was found to increase aspartate uptake in C6 glioma cells, which endogenously express the neuronal glutamate transporter EAAC1 (pEC50 of 9.89). The stimulatory effect of ET-1 mediated by ETA receptors corresponds to a 62% increase in the Vmax with no modification of the affinity for the substrate. While protein kinase C activity is known to participate in the regulation of EAAC1, the effect of ET-1 on the glutamate uptake was found to be independent of this kinase activation. In contrast, the inactivation of Go/i type G-protein dependent signaling with pertussis toxin was found to impair ET-1-mediated regulation of EAAC1. An examination of the cell surface expression of EAAC1 by protein biotinylation studies or by confocal analysis of immuno-fluorescence staining demonstrated that ET-1 stimulates EAAC1 translocation to the cell surface. Hence, the disruption of the cytoskeleton with cytochalasin D prevented ET-1-stimulated aspartate uptake. Together, the data presented in the current study suggest that ET-1 participates in the acute regulation of glutamate transport in glioma cells. Considering the documented role of glutamate excitotoxicity in the development of brain tumors, endothelinergic system constitutes a putative target for the pharmacological control of glutamate transmission at the vicinity of glioma cells. | lld:pubmed |
| pubmed-article:15737330 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15737330 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15737330 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15737330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15737330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15737330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15737330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15737330 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15737330 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:15737330 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:15737330 | pubmed:author | pubmed-author:HermansEmmanu... | lld:pubmed |
| pubmed-article:15737330 | pubmed:author | pubmed-author:NajimiMustaph... | lld:pubmed |
| pubmed-article:15737330 | pubmed:author | pubmed-author:MaloteauxJean... | lld:pubmed |
| pubmed-article:15737330 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15737330 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:15737330 | pubmed:volume | 1668 | lld:pubmed |
| pubmed-article:15737330 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15737330 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15737330 | pubmed:pagination | 195-202 | lld:pubmed |
| pubmed-article:15737330 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:15737330 | pubmed:meshHeading | pubmed-meshheading:15737330... | lld:pubmed |
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| pubmed-article:15737330 | pubmed:meshHeading | pubmed-meshheading:15737330... | lld:pubmed |
| pubmed-article:15737330 | pubmed:meshHeading | pubmed-meshheading:15737330... | lld:pubmed |
| pubmed-article:15737330 | pubmed:meshHeading | pubmed-meshheading:15737330... | lld:pubmed |
| pubmed-article:15737330 | pubmed:meshHeading | pubmed-meshheading:15737330... | lld:pubmed |
| pubmed-article:15737330 | pubmed:meshHeading | pubmed-meshheading:15737330... | lld:pubmed |
| pubmed-article:15737330 | pubmed:meshHeading | pubmed-meshheading:15737330... | lld:pubmed |
| pubmed-article:15737330 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15737330 | pubmed:articleTitle | Pertussis toxin-sensitive modulation of glutamate transport by endothelin-1 type A receptors in glioma cells. | lld:pubmed |
| pubmed-article:15737330 | pubmed:affiliation | Laboratoire de Pharmacologie Expérimentale, Université Catholique de Louvain, 54.10, Avenue Hippocrate 54, 1200 Bruxelles, Belgium. mustapha.najimi@farl.ucl.ac.be | lld:pubmed |
| pubmed-article:15737330 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15737330 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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