Imidazoline binding sites are labeled by [3H]clonidine (I1) or by [3H]idazoxan (I2). I2-sites are mitochondrial. The subcellular localization of I1-sites in brain is unknown. Crude membranes from bovine rostral ventrolateral medulla (RVLM) were further purified by discontinuous sucrose density gradient.
This study sought to identify and characterize subtypes of alpha 2-adrenoceptors in rabbit ciliary body. Radioligand binding assays were performed with the alpha 2-agonist ligand [125I]-p-iodoclonidine ([125I]PIC) and the antagonist ligand [3H]rauwolscine. Both [125I]PIC and [3H]rauwolscine bound to a single
European journal of pharmacology, 258(1-2), 67-76 (1994-06-02)
Binding characteristics of alpha 2-adrenoceptors in rat cerebral cortical membranes were compared using the antagonist radioligands [3H]idazoxan, [3H]2-(2-methoxy-1,4-benzodioxan-2-yl)-2-imidazoline ([3H]RX821002), and the partial agonist radioligand [125I]2-[2,6-(dichloro-4-iodophenyl)imino]imidazoline ([125I]iodoclonidine). With [3H]RX821002 and alpha 2-adrenoceptor subtype-selective competitors, both alpha 2A/D- and alpha 2C-adrenoceptor subtypes
Journal of cardiovascular pharmacology, 24 Suppl 1, S1-S8 (1994-01-01)
The rostral ventrolateral medulla (RVLM) is the primary region maintaining vasomotor tone, and a site of action for central antihypertensive agents. In vitro [125I]p-iodoclonidine binding studies showed that moxonidine was selective for I1-imidazoline over alpha 2-adrenergic receptors in the RVLM.
The Journal of pharmacology and experimental therapeutics, 279(2), 694-702 (1996-11-01)
To identify selective compounds for nonadrenergic I1-imidazoline receptors (I1), the affinities of 22 ligands for [125I]p-iodoclonidine binding have been compared at human platelet I1-imidazoline binding sites (analyzed under norepinephrine mask of alpha-2 AR) and at human alpha-2A, alpha-2B and alpha-2C
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