Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/9572
Full metadata record
DC FieldValueLanguage
dc.contributor.authorKing, P Ren
dc.contributor.authorGundlach, Andrew Len
dc.contributor.authorJarrott, Ben
dc.contributor.authorLouis, William Jen
dc.date.accessioned2015-05-15T22:43:15Z
dc.date.available2015-05-15T22:43:15Z
dc.date.issued1992-07-21en
dc.identifier.citationEuropean Journal of Pharmacology; 218(1): 101-8en
dc.identifier.govdoc1356804en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/9572en
dc.description.abstractThe kinetic and pharmacological characteristics of the binding of the oxazoline antihypertensive drug, [3H]rilmenidine, to membranes of rat cerebral cortex have been determined. Computerised resolution of curvi-linear, equilibrium binding isotherms was consistent with the existence of two distinct binding sites for [3H]rilmenidine: Kd 17.3 +/- 7.41 nM, Bmax 0.197 +/- 0.06 pmol/mg protein and Kd 254 +/- 48 nM, Bmax 1.59 +/- 0.08 pmol/mg protein. Moreover, the resolution of two association and dissociation rates also suggested the existence of two binding site populations. Drug inhibition studies revealed that specific binding of [3H]rilmenidine (2 nM) was only inhibited by a maximum of 50% by the catecholamines, adrenaline and noradrenaline, but was completely inhibited by some oxazolines, by guanabenz (a guanidino drug) and by several imidazoline compounds including naphazoline, oxymetazoline and clonidine. Binding isotherms for these drugs were also best fit by a two-site model. The relative Ki values at the high affinity site for [3H]rilmenidine and the number of these high affinity sites are consistent with this site being an alpha 2-adrenoceptor. The high affinity of oxymetazoline and low affinity of prazosin for high affinity [3H]rilmenidine binding sites together with the rank order of potency of oxymetazoline greater than phentolamine greater than SKF 104078 greater than ARC-239 greater than prazosin suggest that [3H]rilmenidine binds to the alpha 2A sub-type of adrenoceptor. Computer-resolved Ki values for drugs at the larger number of lower affinity binding sites were very similar to Ki values determined in the presence of 10 microM adrenaline (used to block alpha 2-adrenoceptor binding).(ABSTRACT TRUNCATED AT 250 WORDS)en
dc.language.isoenen
dc.subject.otherAdrenergic alpha-Agonists.metabolismen
dc.subject.otherAnimalsen
dc.subject.otherAntihypertensive Agents.metabolismen
dc.subject.otherBinding Sitesen
dc.subject.otherCatecholamines.pharmacologyen
dc.subject.otherCerebral Cortex.metabolismen
dc.subject.otherIn Vitro Techniquesen
dc.subject.otherOxazoles.metabolismen
dc.subject.otherRatsen
dc.subject.otherReceptors, Adrenergic, alpha.analysisen
dc.titleAlpha 2-adrenoceptor and catecholamine-insensitive binding sites for [3H]rilmenidine in membranes from rat cerebral cortex.en
dc.typeJournal Articleen
dc.identifier.journaltitleEuropean Journal of Pharmacologyen
dc.identifier.affiliationUniversity of Melbourne, Department of Medicine, Austin Hospital, Heidelberg, Victoria, Australiaen
dc.description.pages101-8en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/1356804en
dc.type.austinJournal Articleen
item.fulltextNo Fulltext-
item.openairetypeJournal Article-
item.languageiso639-1en-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
crisitem.author.deptClinical Pharmacology and Therapeutics-
Appears in Collections:Journal articles
Show simple item record

Google ScholarTM

Check


Items in AHRO are protected by copyright, with all rights reserved, unless otherwise indicated.