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Pharmacology and modulation of K(ATP) channels by protein kinase C and phosphatases in gallbladder smooth muscle.

Firth T, Mawe G, Nelson MT

American Journal of Physiology-Cell Physiology. 2000;278( 5):C1031-7.

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Abstract

ATP-sensitive K(+) (K(ATP)) channels exhibit pharmacological diversity, which is critical for the development of novel therapeutic agents. We have characterized K(ATP) channels in gallbladder smooth muscle to determine how their pharmacological properties compare to K(ATP) channels in other types of smooth muscle. K(ATP) currents were measured in myocytes isolated from gallbladder and mesenteric artery. The potencies of pinacidil, diazoxide, and glibenclamide were similar in gallbladder and vascular smooth muscle, suggesting that the regions of the channel conferring sensitivity to these agents are conserved among smooth muscle types. Activators of protein kinase C (PKC), however, were less effective at inhibiting K(ATP) currents in myocytes from gallbladder than mesenteric artery. The phosphatase inhibitor okadaic acid increased the efficacy of PKC activators and revealed ongoing basal activation of K(ATP) channels by protein kinase A in gallbladder. These results suggest that phosphatases and basal kinase activity play an important role in controlling K(ATP) channel activity.

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Place of publication:
UNITED STATES
Volume:
278( 5)
Start page:
C1031
End page:
7
Pagination:
C1031-7
Access state:
Active

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Record metadata

Manchester eScholar ID:
uk-ac-man-scw:1d16399
Created:
30th August, 2009, 13:56:35
Last modified:
3rd March, 2010, 17:06:52

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