pubmed-article:10516269 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10516269 | lifeskim:mentions | umls-concept:C0022009 | lld:lifeskim |
pubmed-article:10516269 | lifeskim:mentions | umls-concept:C0949771 | lld:lifeskim |
pubmed-article:10516269 | lifeskim:mentions | umls-concept:C0243046 | lld:lifeskim |
pubmed-article:10516269 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
pubmed-article:10516269 | lifeskim:mentions | umls-concept:C0552635 | lld:lifeskim |
pubmed-article:10516269 | lifeskim:mentions | umls-concept:C1880371 | lld:lifeskim |
pubmed-article:10516269 | pubmed:issue | 4 Pt 2 | lld:pubmed |
pubmed-article:10516269 | pubmed:dateCreated | 1999-11-17 | lld:pubmed |
pubmed-article:10516269 | pubmed:abstractText | Recent studies of glutamate transporters in the central nervous system indicate that in addition to their fundamental role in mediating neurotransmitter uptake, these proteins may contribute to the modulation of a variety of cellular processes. Activation of the excitatory amino acid (EAA) carriers generates an electrogenic current attibutable to ion-coupled cotransport. In addition to this transport-associated current, a substrate-gated thermodynamically uncoupled anion flux has been identified that has been proposed to dampen neuronal excitability. Arachidonic acid has been reported to modulate a variety of membrane proteins involved in cellular signaling. Here we discuss recent findings that indicate arachidonic acid stimulates a previously uncharacterized proton-selective conductance in the Purkinje cell-specific subtype, EAAT4. The unique channel-like porperties of the EAATs, their unexpected localization, and physiological evidence propose a modulatory role for the EAATs in neuronal signaling and suggest a broader role for glutamate transporters than simply the clearance of synaptically released glutamate. Thus, the identification of this arachidonate-stimulated proton conductance extends the complexity of mechanisms through which glutamate transporters modulate neuronal excitability. | lld:pubmed |
pubmed-article:10516269 | pubmed:language | eng | lld:pubmed |
pubmed-article:10516269 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10516269 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10516269 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10516269 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10516269 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10516269 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10516269 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10516269 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10516269 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10516269 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10516269 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10516269 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10516269 | pubmed:month | Oct | lld:pubmed |
pubmed-article:10516269 | pubmed:issn | 0002-9513 | lld:pubmed |
pubmed-article:10516269 | pubmed:author | pubmed-author:AmaraS GSG | lld:pubmed |
pubmed-article:10516269 | pubmed:author | pubmed-author:FairmanW AWA | lld:pubmed |
pubmed-article:10516269 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10516269 | pubmed:volume | 277 | lld:pubmed |
pubmed-article:10516269 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10516269 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10516269 | pubmed:pagination | F481-6 | lld:pubmed |
pubmed-article:10516269 | pubmed:dateRevised | 2005-11-17 | lld:pubmed |
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pubmed-article:10516269 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10516269 | pubmed:articleTitle | Functional diversity of excitatory amino acid transporters: ion channel and transport modes. | lld:pubmed |
pubmed-article:10516269 | pubmed:affiliation | Howard Hughes Medical Institute, Vollum Institute for Advanced Biomedical Research, Portland, Oregon 97201, USA. | lld:pubmed |
pubmed-article:10516269 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10516269 | pubmed:publicationType | Review | lld:pubmed |
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