Premium
The Human Promyelocytic Leukemia Cell (HL‐60 Cell) β‐Adrenergic Receptor
Author(s) -
Sager G.,
Bang B.E.,
Pedersen M.,
Aarbakke J.
Publication year - 1988
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.44.1.41
Subject(s) - receptor , endocrinology , medicine , cyclase , atenolol , biology , adenylate kinase , adrenergic receptor , potency , antagonist , adrenergic , agonist , radioligand , alprenolol , epinephrine , adrenergic antagonist , biochemistry , in vitro , blood pressure
We have characterized the β‐adrenergic receptor binding site and the β‐adrenergic cAMP response of the HL‐60 cell. The hydrophilic ligand [ 3 H]‐(–)‐CGP‐12177 was specifically and reversibly bound to one single class of binding sites (K d 220 pM and B max 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.