The Human Promyelocytic Leukemia Cell (HL-60 Cell) β-Adrenergic Receptor

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Abstract
We have characterized the β-adrenergic receptor binding site and the β-adrenergic cAMP response of the HL-60 cell. The hydrophilic ligand [3H]-(–)-CGP-12177 was specifically and reversibly bound to one single class of binding sites (Kd 220 pM and Bmax 1,970 sites/cell). The adrenergic agonists inhibited the specific radioligand binding. The order of potency was isoproterenol > epinephrine > norepinephrine. The β-2 selective antagonist ICI 118551 had a binding affinity 3 orders of potency higher than the β-1 selective antagonist, atenolol. The adrenergic agonists elevated the cAMP accumulation in a concentration-dependent mode. The order of potency was isoproterenol > epinephrine > norepinephrine. Both the binding and the functional studies revealed stereospecificity and reversibility. The present data show that HL-60 cells possess β-2 adrenergic receptors functionally coupled to adenylate cyclase.