Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/10198
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dc.contributor.authorO'Shea, R Den
dc.contributor.authorManallack, D Ten
dc.contributor.authorConway, Elizabeth Len
dc.contributor.authorMercer, L Den
dc.contributor.authorBeart, P Men
dc.date.accessioned2015-05-15T23:34:22Z
dc.date.available2015-05-15T23:34:22Z
dc.date.issued1991-05-16en
dc.identifier.citationExperimental Brain Research; 86(3): 652-62en
dc.identifier.govdoc1684753en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/10198en
dc.description.abstractThe possible heterogeneity of the agonist and glycine sites of the N-methyl-D-aspartate (NMDA) receptor-complex was examined using receptor binding techniques. Binding of [3H]L-glutamate [( 3H]GLU) and [3H]glycine to synaptic membranes of cerebral and cerebellar cortices, and membranes of a granule cell preparation of rat cerebellum, was characterized. [3H]Glycine always labelled a single population of sites; densities of binding sites (Bmax) in cortical, cerebellar and "granule" membranes were 3.1, 0.87 and 3.6 pmol/mg protein, respectively. Dissociation constants (Kd) in the same three preparations were 0.13, 0.31 and 1.9 microM, respectively. In competition studies, D-cycloserine, but not D-serine and 7-chlorokynurenate, showed varying potency between the membrane preparations, and analysis of variance (ANOVA) revealed a significant interaction between ligands and membrane fractions. Binding of [3H]GLU was saturable and to a single population of sites: Kd 0.5-0.9 microM and Bmax 3.2-3.6 pmol/mg protein. In all three membrane preparations the rank order of potency of NMDA agonists as inhibitors of the binding of [3H]GLU was always L-aspartate greater than L-cysteate greater than L-cysteinesulphinate greater than L-serine-O-sulphate greater than ibotenate greater than L-homocysteate. NMDA, quinolinate and competitive NMDA antagonists were only weak inhibitors of the binding of [3H]GLU and never fully inhibited specific binding. Other subtype-selective excitatory amino acids were very weak or ineffective inhibitors of binding. Binding of NMDA agonists was better described by a two site model whereby the proportion of high affinity sites did not vary significantly across the three membrane preparations.(ABSTRACT TRUNCATED AT 250 WORDS)en
dc.language.isoenen
dc.subject.otherAnimalsen
dc.subject.otherAutoradiographyen
dc.subject.otherBinding, Competitive.drug effectsen
dc.subject.otherCerebellar Cortex.anatomy & histology.metabolismen
dc.subject.otherCerebral Cortex.anatomy & histology.metabolismen
dc.subject.otherCycloserine.pharmacologyen
dc.subject.otherGlutamates.metabolism.pharmacokineticsen
dc.subject.otherGlutamic Aciden
dc.subject.otherGlycine.metabolism.pharmacokineticsen
dc.subject.otherIn Vitro Techniquesen
dc.subject.otherKynurenic Acid.analogs & derivatives.pharmacologyen
dc.subject.otherLigandsen
dc.subject.otherMaleen
dc.subject.otherRatsen
dc.subject.otherRats, Inbred Strainsen
dc.subject.otherReceptors, Amino Aciden
dc.subject.otherReceptors, Cell Surface.metabolismen
dc.subject.otherReceptors, N-Methyl-D-Aspartate.antagonists & inhibitors.metabolismen
dc.subject.otherSerine.metabolismen
dc.titleEvidence for heterogenous glycine domains but conserved multiple states of the excitatory amino acid recognition site of the NMDA receptor: regional binding studies with [3H]glycine and [3H]L-glutamate.en
dc.typeJournal Articleen
dc.identifier.journaltitleExperimental Brain Researchen
dc.identifier.affiliationUniversity of Melbourne, Clinical Pharmacology and Therapeutics, Austin Hospital, Heidelberg, Victoria, Australiaen
dc.description.pages652-62en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/1684753en
dc.type.austinJournal Articleen
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairetypeJournal Article-
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