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Research Communications |
dimers stimulate vascular L-type Ca2+ channels via phosphoinositide 3-kinase
a Laboratoire de Physiologie Cellulaire et Pharmacologie Moléculaire, CNRS ESA 5017, Université de Bordeaux II, 33076 Bordeaux, France; and
b Institut für Pharmakologie, Freie Universität Berlin, D-14195 Berlin, Germany
We have previously reported
that, in venous myocytes, Gß
scavengers inhibit angiotensin
AT1A receptor-induced stimulation of L-type
Ca2+ channels (1)
. Here, we demonstrate that intracellular
infusion of purified Gß complexes stimulates the L-type
Ca2+ channel current in a concentration-dependent manner.
Additional intracellular dialysis of GDP-bound inactive
G
o or of a peptide corresponding to the Gß binding
region of the ß-adrenergic receptor kinase completely inhibited the
Gß-induced stimulation of Ca2+ channel currents. The
gating properties of the channel were not affected by intracellular
application of Gß, suggesting that Gß increased the
whole-cell calcium conductance. In addition, both the angiotensin
AT1A receptor- and the Gß-induced stimulation of
L-type Ca2+ channels were blocked by pretreatment of the
cells with wortmannin, at nanomolar concentrations. Correspondingly,
intracellular infusion of an enzymatically active purified recombinant
Gß-sensitive phosphoinositide 3-kinase, PI3K, mimicked
Gß-induced stimulation of Ca2+ channels. Both Gß-
and PI3K-induced stimulations of Ca2+ channel currents
were reduced by protein kinase C inhibitors suggesting that the
Gß/PI3K-activated transduction pathway involves a protein
kinase C. These results indicate for the first time that Gß dimers
stimulate the vascular L-type Ca2+ channels through a
Gß-sensitive PI3K.—Viard, P., Exner, T., Maier, U., Mironneau,
J., Nürnberg, B., Macrez, N. Gß dimers stimulate vascular
L-type Ca2+ channels via phosphoinositide 3-kinase .
Key Words: G-protein • PI3K • protein kinase C • smooth muscle
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