Mutant constructs of the beta-adrenergic receptor that are uncoupled from adenylyl cyclase retain functional activation of Na-H exchange.

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Article

Mutant constructs of the beta-adrenergic receptor that are uncoupled from adenylyl cyclase retain functional activation of Na-H exchange.

Molecular pharmacology - 1 Jun 1992

Barber D L, Ganz M B, Bongiorno P B, Strader C D

Abstract excerpt

beta-Adrenergic receptor (beta AR) agonists modulate a number of intracellular effectors; for example, they stimulate adenylyl cyclase and Ca2+ channels, inhibit Na+ channels and Mg2+ efflux, and activate Na-H exchange. Regulation of adenylyl cyclase, Ca2+, Na+, and Mg2+ by the beta AR is mediated through receptor coupling to the GTP-binding protein Gs. We have previously determined, however, that beta AR...

Topics

Adenylyl Cyclases
Amino Acid Sequence
Animals
Carrier Proteins
Cricetinae
Cyclic AMP
Enzyme Activation
GTP-Binding Proteins
Intracellular Fluid
Isoproterenol
L Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mice

Molecular Sequence Data

Mutation

Protein Conformation

Receptors, Adrenergic, beta

Sodium-Hydrogen Exchangers

Transfection

Source

Open in PubMed

Identifiers

PMID: 1319545

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1319545-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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