Characterization of α-adrenoceptors in rat and guinea pig tissues using radiolabeled agonists and antagonists

B. Jarrott, R. J. Summers, A. J. Culvenor, W. J. Louis

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Abstract

Tritium-labeled preparations of the selective α2-adrenoceptor agonist, clonidine, and the selective α1-adrenoceptor antagonists, prazosin and WB4101, were examined for their suitability as ligands for receptor assay. In the rat brain, 3H-clonidine bound specifically with high affinity to membrane sites, and drug displacement studies indicated that these were α2-adrenoceptors. The structural requirements for this receptor were defined by examining a range of clonidine analogues. 3H-Clonidine binding to peripheral tissues of the rat was very low, although peripheral tissues from guinea pig exhibited higher binding. Specific 3H-clonidine binding was not reduced after chemical sympathectomy, suggesting that the binding site, although having characteristics of an α2-adrenoceptor, was not located presynaptically. Studies with 3H-WB 4101 in rat cerebral cortex indicated that this ligand bound to an α1-adrenoceptor which was independent of the 3H-clonidine binding site. 3H-Prazosin was a ligand for α1-adrenoceptors in guinea pig brain and also in membranes from seminal vesicle. However, in the latter tissue, characterization of the binding site was hampered by a high degree of nonspecific binding (50% of total binding).

Original languageEnglish
JournalCirculation Research
Volume46
Issue number6 II
Publication statusPublished - 1 Dec 1980

Cite this

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abstract = "Tritium-labeled preparations of the selective α2-adrenoceptor agonist, clonidine, and the selective α1-adrenoceptor antagonists, prazosin and WB4101, were examined for their suitability as ligands for receptor assay. In the rat brain, 3H-clonidine bound specifically with high affinity to membrane sites, and drug displacement studies indicated that these were α2-adrenoceptors. The structural requirements for this receptor were defined by examining a range of clonidine analogues. 3H-Clonidine binding to peripheral tissues of the rat was very low, although peripheral tissues from guinea pig exhibited higher binding. Specific 3H-clonidine binding was not reduced after chemical sympathectomy, suggesting that the binding site, although having characteristics of an α2-adrenoceptor, was not located presynaptically. Studies with 3H-WB 4101 in rat cerebral cortex indicated that this ligand bound to an α1-adrenoceptor which was independent of the 3H-clonidine binding site. 3H-Prazosin was a ligand for α1-adrenoceptors in guinea pig brain and also in membranes from seminal vesicle. However, in the latter tissue, characterization of the binding site was hampered by a high degree of nonspecific binding (50{\%} of total binding).",
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Characterization of α-adrenoceptors in rat and guinea pig tissues using radiolabeled agonists and antagonists. / Jarrott, B.; Summers, R. J.; Culvenor, A. J.; Louis, W. J.

In: Circulation Research, Vol. 46, No. 6 II, 01.12.1980.

Research output: Contribution to journalArticleResearchpeer-review

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T1 - Characterization of α-adrenoceptors in rat and guinea pig tissues using radiolabeled agonists and antagonists

AU - Jarrott, B.

AU - Summers, R. J.

AU - Culvenor, A. J.

AU - Louis, W. J.

PY - 1980/12/1

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N2 - Tritium-labeled preparations of the selective α2-adrenoceptor agonist, clonidine, and the selective α1-adrenoceptor antagonists, prazosin and WB4101, were examined for their suitability as ligands for receptor assay. In the rat brain, 3H-clonidine bound specifically with high affinity to membrane sites, and drug displacement studies indicated that these were α2-adrenoceptors. The structural requirements for this receptor were defined by examining a range of clonidine analogues. 3H-Clonidine binding to peripheral tissues of the rat was very low, although peripheral tissues from guinea pig exhibited higher binding. Specific 3H-clonidine binding was not reduced after chemical sympathectomy, suggesting that the binding site, although having characteristics of an α2-adrenoceptor, was not located presynaptically. Studies with 3H-WB 4101 in rat cerebral cortex indicated that this ligand bound to an α1-adrenoceptor which was independent of the 3H-clonidine binding site. 3H-Prazosin was a ligand for α1-adrenoceptors in guinea pig brain and also in membranes from seminal vesicle. However, in the latter tissue, characterization of the binding site was hampered by a high degree of nonspecific binding (50% of total binding).

AB - Tritium-labeled preparations of the selective α2-adrenoceptor agonist, clonidine, and the selective α1-adrenoceptor antagonists, prazosin and WB4101, were examined for their suitability as ligands for receptor assay. In the rat brain, 3H-clonidine bound specifically with high affinity to membrane sites, and drug displacement studies indicated that these were α2-adrenoceptors. The structural requirements for this receptor were defined by examining a range of clonidine analogues. 3H-Clonidine binding to peripheral tissues of the rat was very low, although peripheral tissues from guinea pig exhibited higher binding. Specific 3H-clonidine binding was not reduced after chemical sympathectomy, suggesting that the binding site, although having characteristics of an α2-adrenoceptor, was not located presynaptically. Studies with 3H-WB 4101 in rat cerebral cortex indicated that this ligand bound to an α1-adrenoceptor which was independent of the 3H-clonidine binding site. 3H-Prazosin was a ligand for α1-adrenoceptors in guinea pig brain and also in membranes from seminal vesicle. However, in the latter tissue, characterization of the binding site was hampered by a high degree of nonspecific binding (50% of total binding).

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