Linked Life Data

16405496

Source:http://linkedlifedata.com/resource/pubmed/id/16405496

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:16405496rdf:typepubmed:Citationlld:pubmed
pubmed-article:16405496lifeskim:mentionsumls-concept:C0001675lld:lifeskim
pubmed-article:16405496lifeskim:mentionsumls-concept:C0027836lld:lifeskim
pubmed-article:16405496lifeskim:mentionsumls-concept:C1882598lld:lifeskim
pubmed-article:16405496lifeskim:mentionsumls-concept:C0013878lld:lifeskim
pubmed-article:16405496lifeskim:mentionsumls-concept:C0220839lld:lifeskim
pubmed-article:16405496lifeskim:mentionsumls-concept:C0030685lld:lifeskim
pubmed-article:16405496lifeskim:mentionsumls-concept:C1521827lld:lifeskim
pubmed-article:16405496lifeskim:mentionsumls-concept:C0680255lld:lifeskim
pubmed-article:16405496lifeskim:mentionsumls-concept:C0391871lld:lifeskim
pubmed-article:16405496lifeskim:mentionsumls-concept:C1283071lld:lifeskim
pubmed-article:16405496lifeskim:mentionsumls-concept:C1963578lld:lifeskim
pubmed-article:16405496pubmed:issue3lld:pubmed
pubmed-article:16405496pubmed:dateCreated2006-1-30lld:pubmed
pubmed-article:16405496pubmed:abstractTextGlial subcellular re-sealed particles (referred to as gliosomes here) were purified from rat cerebral cortex and investigated for their ability to release glutamate. Confocal microscopy showed that the glia-specific proteins glial fibrillary acidic protein (GFAP) and S-100, but not the neuronal proteins 95-kDa postsynaptic density protein (PSD-95), microtubule-associated protein 2 (MAP-2) and beta-tubulin III, were enriched in purified gliosomes. Furthermore, gliosomes exhibited labelling neither for integrin-alphaM nor for myelin basic protein, which are specific for microglia and oligodendrocytes respectively. The Ca2+ ionophore ionomycin (0.1-5 microm) efficiently stimulated the release of tritium from gliosomes pre-labelled with [3H]d-aspartate and of endogenous glutamate in a Ca(2+)-dependent and bafilomycin A1-sensitive manner, suggesting the involvement of an exocytotic process. Accordingly, ionomycin was found to induce a Ca(2+)-dependent increase in the vesicular fusion rate, when exocytosis was monitored with acridine orange. ATP stimulated [3H]d-aspartate release in a concentration- (0.1-3 mm) and Ca(2+)-dependent manner. The gliosomal fraction contained proteins of the exocytotic machinery [syntaxin-1, vesicular-associated membrane protein type 2 (VAMP-2), 23-kDa synaptosome-associated protein (SNAP-23) and 25-kDa synaptosome-associated protein (SNAP-25)] co-existing with GFAP immunoreactivity. Moreover, GFAP or VAMP-2 co-expressed with the vesicular glutamate transporter type 1. Consistent with ultrastructural analysis, several approximately 30-nm non-clustered vesicles were present in the gliosome cytoplasm. It is concluded that gliosomes purified from adult brain contain glutamate-accumulating vesicles and can release the amino acid by a process resembling neuronal exocytosis.lld:pubmed
pubmed-article:16405496pubmed:languageenglld:pubmed
pubmed-article:16405496pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:citationSubsetIMlld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16405496pubmed:statusMEDLINElld:pubmed
pubmed-article:16405496pubmed:monthFeblld:pubmed
pubmed-article:16405496pubmed:issn0022-3042lld:pubmed
pubmed-article:16405496pubmed:authorpubmed-author:TacchettiCarl...lld:pubmed
pubmed-article:16405496pubmed:authorpubmed-author:RaiteriLucaLlld:pubmed
pubmed-article:16405496pubmed:authorpubmed-author:StiglianiSara...lld:pubmed
pubmed-article:16405496pubmed:authorpubmed-author:BonannoGiamba...lld:pubmed
pubmed-article:16405496pubmed:authorpubmed-author:PassalacquaMa...lld:pubmed
pubmed-article:16405496pubmed:authorpubmed-author:MelloniEdonElld:pubmed
pubmed-article:16405496pubmed:authorpubmed-author:DiasproAlbert...lld:pubmed
pubmed-article:16405496pubmed:authorpubmed-author:UsaiCesareClld:pubmed
pubmed-article:16405496pubmed:authorpubmed-author:ZappettiniSim...lld:pubmed
pubmed-article:16405496pubmed:authorpubmed-author:VenturiConsue...lld:pubmed
pubmed-article:16405496pubmed:issnTypePrintlld:pubmed
pubmed-article:16405496pubmed:volume96lld:pubmed
pubmed-article:16405496pubmed:ownerNLMlld:pubmed
pubmed-article:16405496pubmed:authorsCompleteYlld:pubmed
pubmed-article:16405496pubmed:pagination656-68lld:pubmed
pubmed-article:16405496pubmed:dateRevised2009-9-16lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
pubmed-article:16405496pubmed:meshHeadingpubmed-meshheading:16405496...lld:pubmed
More...