TY - JOUR
T1 - Receptor-mediated regulation of IsK, a very slowly activating, voltage-dependent K+ channel in Xenopus oocytes
AU - Honore, Eric
AU - Attali, Bernard
AU - Lesage, Florian
AU - Barhanin, Jacques
AU - Lazdunski, Michel
N1 - Funding Information:
Acknowledgments. We are grateful to Dr. E. Van Obberghen-Schilling for providing the Chinese hamster 5-HT2 receptor clone. This work was supported by the Centre National de la Recherche Scientifique, the Association pour la Recherche sur le Cancer, and the Association pour la Recherche sur la Scl~rose en Plaques. B.A. is a recipient of an ARC fellowship. We thank F. Aguila and C. Roulinat for expert technical assistance.
PY - 1992/5/15
Y1 - 1992/5/15
N2 - Expression of IsK in Xenopus oocytes has been obtained in 2 ways: (i) by injection of cardiac polyA+ RNA from neonatal mouse heart; (ii) by injection of a cRNA synthesized in vitro. It was observed that polyA+ RNA not only directs the expression of the IsK channel but also contains purinergic P2 and endothelin receptors. Stimulation of these receptors, that produce intracellular Ca2+ increase together with diacylglycerol production activating protein kinase C, increases IsK activity. The same type of results and the same conclusions were obtained by co-injecting cRNA's corresponding to the 5-HT2 receptor and the IsK channel into oocytes. This stimulatory effect was shown to be due to Ca2+ via a calmodulin-dependent kinase process. Conversely, activation of protein kinase C pathway alone by phorbol esters leads to inhibition of IsK activity.
AB - Expression of IsK in Xenopus oocytes has been obtained in 2 ways: (i) by injection of cardiac polyA+ RNA from neonatal mouse heart; (ii) by injection of a cRNA synthesized in vitro. It was observed that polyA+ RNA not only directs the expression of the IsK channel but also contains purinergic P2 and endothelin receptors. Stimulation of these receptors, that produce intracellular Ca2+ increase together with diacylglycerol production activating protein kinase C, increases IsK activity. The same type of results and the same conclusions were obtained by co-injecting cRNA's corresponding to the 5-HT2 receptor and the IsK channel into oocytes. This stimulatory effect was shown to be due to Ca2+ via a calmodulin-dependent kinase process. Conversely, activation of protein kinase C pathway alone by phorbol esters leads to inhibition of IsK activity.
UR - https://www.scopus.com/pages/publications/0026654208
U2 - 10.1016/S0006-291X(05)80001-4
DO - 10.1016/S0006-291X(05)80001-4
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AN - SCOPUS:0026654208
SN - 0006-291X
VL - 184
SP - 1135
EP - 1141
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -