Interactions of beta-adrenergic receptors with a membrane protein other than the stimulatory guanine nucleotide-binding protein.

Abstract:

:Beta-adrenergic receptors on membranes prepared from rat lung, wild-type S49 lymphoma cells, and the adenylate cyclase-deficient variant of S49 lymphoma cells (cyc-) bind the agonist [3H]hydroxybenzylisoproterenol ([3H]HBI) with high affinity and this binding of [3H]HBI can be inhibited by GTP. Membranes prepared from these tissues were incubated with the agonist [3H]HBI or the antagonist [125I]iodopindolol ([125I]IPIN), labeled receptors were solubilized with digitonin, and the apparent molecular sizes of the ligand-bound receptor complexes were determined by high-performance size-exclusion chromatography. Results with all three tissues demonstrated that receptors labeled with [125I]IPIN were retained by the size-exclusion columns longer than receptors labeled with [3H]HBI. Thus, the apparent molecular size of soluble beta-adrenergic receptors from rat lung, wild-type S49 cells, and cyc- S49 cells was larger when receptors were occupied with an agonist rather than an antagonist. The results suggest that receptors, including those on cyc- S49 cells, interact with a membrane protein, presumably a guanine nucleotide-binding protein. Since cyc- S49 cells do not contain a functional stimulatory guanine nucleotide-binding protein, but do contain a functional inhibitory guanine nucleotide-binding protein, an interaction between beta-adrenergic receptors and the inhibitory guanine nucleotide-binding protein may be responsible for the apparent increase in the molecular size of the receptor after occupation of the receptor with an agonist.

journal_name

Biochem Pharmacol

journal_title

Biochemical pharmacology

authors

Abramson SN,Shorr RG,Molinoff PB

doi

10.1016/0006-2952(87)90589-2

subject

Has Abstract

pub_date

1987-07-15 00:00:00

pages

2263-9

issue

14

eissn

0006-2952

issn

1873-2968

pii

0006-2952(87)90589-2

journal_volume

36

pub_type

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