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Endothelins activate Ca(2+)-gated K(+) channels via endothelin B receptors in CD-1 mouse erythrocytes


, : Endothelins activate Ca(2+)-gated K(+) channels via endothelin B receptors in CD-1 mouse erythrocytes. American Journal of Physiology 277(4 Pt 1): C746-C754

Cell dehydration mediated by Ca2+-activated K+ channels plays an important role in the pathogenesis of sickle cell disease. CD-1 mouse erythrocytes possess a Ca2+-activated K+ channel (Gardos channel) with maximal velocity (Vmax) of 0.154 [plus or minus] 0.02 mmol.l cells-1.min-1 and an affinity constant (K0.5) for Ca2+ of 286 [plus or minus] 83 nM in the presence of A-23187. Cells pretreated with 500 nM endothelin-1 (ET-1) increased their Vmax by 88 [plus or minus] 9% (n = 8) and decreased their K0.5 for Ca2+ to 139 [plus or minus] 63 nM (P < 0.05; n = 4). Activation of the Gardos channel resulted in an EC50 of 75 [plus or minus] 20 nM for ET-1 and 374 [plus or minus] 97 nM for ET-3. Analysis of the affinity of unlabeled ET-1 for its receptor showed two classes of binding sites with apparent dissociation constants of 167 [plus or minus] 51 and 785 [plus or minus] 143 nM and with capacity of binding sites of 298 [plus or minus] 38 and 1,568 [plus or minus] 211 sites/cell, respectively. The Gardos channel was activated by the endothelin B (ETB) receptor agonist IRL 1620 and inhibited by BQ-788, demonstrating the involvement of ETB receptors. Calphostin C inhibited 73% of ET-1-induced Gardos activation and 84% of the ET-1-induced membrane protein kinase C activity. Thus endothelins regulate erythrocyte Gardos channels via ETB receptors and a calphostin-sensitive mechanism. Reprinted by permission of the publisher.

US$29.90

PMID: 10516105


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