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• W2001668716 abstract "The β-adrenergic receptors in human adipose membranes were identified by the specific and saturable binding of the β-adrenergic antagonist (–)-[3H]dihydroalprenolol. The total number of sites in control membranes was 0.32 ± 0.03 pmol/mg protein and the equilibrium dissociation constant for binding (Kd) was 2.6 nM and 2.5 nM as determined by Scatchard analysis of experiments on equilibrium binding and kinetics respectively. The β1-adrenergic nature of the receptors was derived from the order of potencies of β-adrenergic agonists (isoproterenol > norepinephrine > epinephrine) to complete with (–)-[3H]dihydroalprenolol for binding. Studies of saturation binding, kinetics and competition binding revealed the presence of a single class of β1-adrenergic receptors. Prolonged incubation of human adipose cells in the presence of (–)-norepinephrine decreases the lipolytic response to β-adrenergic agonists, and reduces by 50% the concentration of β-adrenergic receptors. The Kd values for (–)-[3H]dihydroalprenolol and the β-adrenergic agonists remain unchanged. Catecholamines also produce a rapid conformational change of approximatively 50% of the receptors in control membranes as revealed by their increased sensitivity towards inactivation by the alkylating agent N-ethylmaleimide. This inactivation process is not observed in desensitized membranes, which indicates that desensitization and inactivation by agonists plus N-ethylmaleimide affect the same receptor population. The β-adrenergic receptors in human adipocytes can thus be divided into two subpopulations on the basis of the different consequences of their interaction with agonist molecules." @default.
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• W2001668716 date "1981-02-01" @default.
• W2001668716 modified "2023-10-01" @default.
• W2001668716 title "Distinction between Two Subpopulations of beta1-Adrenergic Receptors in Human Adipose Cells" @default.
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• W2001668716 doi "https://doi.org/10.1111/j.1432-1033.1981.tb05154.x" @default.
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