Relationship between an altered membrane form and a low affinity form of the β-adrenergic receptor occurring during catecholamine-induced desensitization. Evidence for receptor internalization

M. L. Toews, G. L. Waldo, T. K. Harden, J. P. Perkins

Research output: Contribution to journalArticlepeer-review

55 Scopus citations

Abstract

We have investigated the relationship between the catecholamine-induced occurrence in 1321N1 human astrocytoma cells of β-adrenergic receptors that exhibit low apparent affinity for hydrophilic ligands in short-time assays with intact cells and a population of β-adrenergic receptors that migrate in a light vesicle fraction on sucrose density gradients. Pretreatment of cells with concanavalin A prevents the generation of both of these forms of the receptor during incubation with agonists but does not prevent the agonist-induced decrease in isoproterenol-stimulated cyclic AMP production that also ocurs during desensitization. Selective labelling of the low affinity β-receptors with 125I-pindolol followed by centrifugation on sucrose density gradients revealed that all of the receptors in the light vesicle fraction from desensitized cells were of the low affinity type, but that a portion of the low affinity receptors also migrated in a heavier sucrose fraction together with the plasma membrane. In contrast, in control cells, no lower affinity receptors were present in the heavy sucrose fractions. The agonist-induced occurrence of these various forms of the β-adrenergic receptor can be explained on the basis of the current models of desensitization involving agonist-induced internalization of β-adrenergic receptors.

Original languageEnglish (US)
Pages (from-to)11844-11850
Number of pages7
JournalJournal of Biological Chemistry
Volume259
Issue number19
StatePublished - 1984

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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