Characterization of Adrenergic Receptors in Membranes from the Rat Seminal Vesicle.

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概要

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• Characterization of adrenergic receptors in membranes from the rat seminal vesicle was studied by radioligand binding assay. Seminal vesicle membranes contained saturable and high affinity binding sites for the β-adrenergic receptor antagonist <SUP>3</SUP>H-dihydroalprenolol (<SUP>3</SUP>H-DHA)and for the α-adrenergic antagonist <SUP>3</SUP>H-prazosin. The observed order of potency for adrenergic agonists in competing for the <SUP>3</SUP>H-DHA binding sites: isoproterenol > epinephrine ≈ salbutamol > norepinephrine indicates that these membrane receptors have the properties of β<SUB>2</SUB>-adrenergic receptors. α<SUB>1</SUB>-Adrenergic receptors were defined mainly as α<SUB>1A</SUB> subtypes by demonstrating their insensitivity to pretreatment with chlorethylclonidine and the different rank orders of antagonist affinities. No significant binding sites for the α<SUB>2</SUB>-adrenergic receptor agonist <SUP>3</SUP>H-clonidine were observed. The GTP-induced reduction in the affinity of α<SUB>1</SUB>-adrenergic receptors for epinephrine was significantly reversed by the muscarinic cholinergic agonist carbachol. Atropine effectively antagonized this effect of carbachol on the competitive inhibition of <SUP>3</SUP>H-prazosin binding by epinephrine in the presence of GTP, which suggests that muscarinic cholinergic receptors regulate the affinity of α<SUB>1</SUB>-adrenergic receptors by modulating the effect of guanine nucleotides. The effect of GTP on decreasing the affinity of β<SUB>2</SUB>-adrenergic receptors was not influenced by the addition of carbachol.

• 公益社団法人 日本薬理学会の論文

著者

• Shima Sumio

  Department Of Biochemistry St.marianna University School Of Medicine

• SHIMA Sumio

  Department of Biochemistry, St. Marianna University School of Medicine

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• Characterization of Adrenergic Receptors in Membranes from the Rat Seminal Vesicle.

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