Artículo

Differential effects of inhibitory G protein isoforms on G protein-gated inwardly rectifying K + currents in adult murine atria

Nobles, Muriel ; Montaigne, David ; Sebastian, Sonia ; Birnbaumer, Lutz Icon; Tinker, Andrew

Otros responsables

Fecha

05/2018

Editorial

American Physiological Society

Revista

American journal of physiology. Cell physiology

Título del libro

Nombre del evento

Fecha del evento

Institución organizadora

ISSN

1522-1563

eISSN

ISBN

Idioma

Inglés

Tipo del evento

Clasificación temática

Resumen

G protein-gated inwardly rectifying K+ (GIRK) channels are the major inwardly rectifying K+ currents in cardiac atrial myocytes and an important determinant of atrial electrophysiology. Inhibitory G protein α-subunits can both mediate activation via acetylcholine but can also suppress basal currents in the absence of agonist. We studied this phenomenon using whole cell patch clamping in murine atria from mice with global genetic deletion of Gαi2, combined deletion of Gαi1/Gαi3, and littermate controls. We found that mice with deletion of Gαi2 had increased basal and agonist-activated currents, particularly in the right atria while in contrast those with Gαi1/Gαi3 deletion had reduced currents. Mice with global genetic deletion of Gαi2 had decreased action potential duration. Tissue preparations of the left atria studied with a multielectrode array from Gαi2 knockout mice showed a shorter effective refractory period, with no change in conduction velocity, than littermate controls. Transcriptional studies revealed increased expression of GIRK channel subunit genes in Gαi2 knockout mice. Thus different G protein isoforms have differential effects on GIRK channel behavior and paradoxically Gαi2 act to increase basal and agonist-activated GIRK currents. Deletion of Gαi2 is potentially proarrhythmic in the atria.

Aprobación

Revisión

Complementado por

Referenciado por

Licencia Creative Commons

Excepto donde se indique lo contrario, la licencia de este ítem se describe como by-nc-sa