title: Characterization of the human liver alpha 1-adrenoceptors: predominance of the alpha 1A subtype.
abstract: The alpha 1-adrenoceptor subtype present in human liver membranes was studied using radioligand binding techniques. [3H]Prazosin binding was rapid, saturable and reversible. A kinetically derived Kd of 0.22 nM was obtained. Rosenthal analysis of saturation isotherms indicated a single class of binding sites with a Kd of 0.47 nM and a Bmax of 70 fmol/mg of protein. Membrane preincubation with chloroethylclonidine markedly decreased total binding (62% decrease) without altering the Kd for the radioligand. Binding competition experiments were performed and the order of potency for agonists was: oxymetazoline > epinephrine > or = norepinephrine > methoxamine. The binding affinity for epinephrine was modulated by the GTP analogue guanosine-5'-(beta,gamma-imido)triphosphate. For antagonists the potency order was: WB4101 > or = prazosin > or = (+)-niguldipine = 5-methylurapidil > or = benoxathian > or = phentolamine. The pharmacological profile of the [3H]prazosin binding sites of human liver membranes suggests that alpha 1A-adrenoceptors predominate (75%-85% of the alpha 1-adrenoceptors) in this tissue.
authors.affiliation: Departamento de Bioenergética, Universidad Nacional Autónoma de México, México, D.F.
authors.forename: J A
authors.initials: JA
authors.lastname: García-Sáinz
authors.forename: M T
authors.initials: MT
authors.lastname: Romero-Avila
authors.forename: M E
authors.initials: ME
authors.lastname: Tórres-Márquez
mesh_terms: D000328:Adult; D005260:Female; D006801:Humans; D066298:In Vitro Techniques; D008099:Liver / Q000378:metabolism*; D008297:Male; D008875:Middle Aged; D011224:Prazosin / Q000378:metabolism; D011869:Radioligand Assay; D018340:Receptors, Adrenergic, alpha-1 / Q000145:classification* / Q000378:metabolism
chemical_list: D018340:Receptors, Adrenergic, alpha-1; D011224:Prazosin