Characterization of β-adrenoceptors on rat skeletal muscle cells grown in vitro

Marie Helene Disatnik, Sanford R. Sampson, Asher Shainberg

    Research output: Contribution to journalArticlepeer-review

    9 Scopus citations

    Abstract

    The binding properties of an hydrophilic β-adrenergic receptor radioligand, (-)[3H](4-(3-tert-butylamino-2-hydroxypropoxy)-benzimidazolo-2-one); ([3H]CGP-12177), were investigated in rat skeletal muscle cells in culture. The binding of [3H]CGP-12177 at 25° was saturable, reversible and of high affinity (Kd = 1.3 ± 0.3 nM). The maximal number of [3H]CGP-12177 binding sites was 30.6 ± 3.2 fmol/dish (34 ± 3.5 fmol/mg protein). β-Adrenergic agonists and antagonists inhibited [3H]CGP-12177 binding. The competing ligand inhibition binding is a typical one for β2-adrenoceptors. The increase in β-adrenoceptors was independent of cell fusion. Amiodarone (10-5 M) decreased the β-adrenoceptor number in skeletal muscle cells differentiated in vitro by 48%, while the affinity for [3H]CGP-12177 was not affected.

    Original languageEnglish
    Pages (from-to)1043-1048
    Number of pages6
    JournalBiochemical Pharmacology
    Volume40
    Issue number5
    DOIs
    StatePublished - 1 Sep 1990

    Fingerprint

    Dive into the research topics of 'Characterization of β-adrenoceptors on rat skeletal muscle cells grown in vitro'. Together they form a unique fingerprint.

    Cite this