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,Faculty of Medicine, Laboratory of Cellular and Molecular Physiology, Department of Physiology, Semmelweis University, H-1444 Budapest, Hungary
The
two-pore-domain K+ channel, TASK-1, was recently shown to
be a target of receptor-mediated regulation in neurons and in adrenal
glomerulosa cells. Here, we demonstrate that TASK-1 expressed in
Xenopus laevis oocytes is inhibited by different
Ca2+-mobilizing agonists. Lysophosphatidic acid, via its
endogenous receptor, and ANG II and carbachol, via their heterologously
expressed ANG II type 1a and M1 muscarinic receptors,
respectively, inhibit TASK-1. This effect can be mimicked by guanosine
5'-O-(3-thiotriphosphate), indicating the involvement
of GTP-binding protein(s). The phospholipase C inhibitor U-73122
reduced the receptor-mediated inhibition of TASK-1. Downstream signals
of phospholipase C action (inositol 1,4,5-trisphosphate, cytoplasmic
Ca2+ concentration, and diacylglycerol) do not mediate the
inhibition. Unlike the Gq-coupled receptors, stimulation of
the Gi-activating M2 muscarinic receptor
coexpressed with TASK-1 results in an only minimal decrease of the
TASK-1 current. However, additional coexpression of phospholipase
C-
2 (which is responsive also to Gi
-subunits) renders M2 receptor activation effective.
This indicates the significance of phospholipase C activity in the
receptor-mediated inhibition of TASK-1.
voltage clamp; two-pore channel; phosphatidylinositol bisphosphate; wortmannin
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