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• W2021139210 abstract "Natriuretic peptides bind with natriuretic peptide receptor (NPR)-C, which can alter cellular function through its interaction with the G(i) protein complex. NPR-C has been found to mediate the activation of K(+) channels and non-selective cation channels in vascular smooth muscle and cardiac fibroblast cells, respectively. However, the electrophysiological effect of NPR-C activation on endothelial cells (EC) has not been previously examined. In this study we sought to elucidate the effect of cANF(4-23), a selective NPR-C ligand, on EC membrane potential (E(m)).Changes in EC E(m) was measured through non-invasive fluorescence imaging. EC were preincubated in the potentiometric dye, DiBAC(4)(3) and subsequently exposed to cANF(4-23), in the presence of selective inhibitors of ion-channels or second messengers. NPR-C expression in rat lung microvascular endothelial cells was assessed by RT-PCR. cANF(4-23) induced a sustained decrease in EC cellular fluorescence, indicating endothelial cell hyperpolarization. The cANF-induced hyperpolarization could not be attenuated by TEA, barium, ouabain or by the reduction of extracellular Ca(2+). Further, the cANF-induced hyperpolarization was insensitive to inhibition of G(i) and protein kinase G (PKG), downstream messengers of NPRs. However, the Cl(-) channel inhibitors, 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid, niflumic acid, and hypertonic saline attenuated the cANF-induced hyperpolarization. Perforated patch clamp recordings confirmed the cANF-induced current was carried by Cl(-) and could be inhibited by niflumic acid. RT-PCR confirmed expression of NPR-C in vascular smooth muscle cells but not in EC.cANF causes hyperpolarization that is most likely mediated via activation of Cl(-) channels by a PKG and G(i) independent mechanism." @default.
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• W2021139210 date "2009-12-01" @default.
• W2021139210 modified "2023-09-23" @default.
• W2021139210 title "cANF causes endothelial cell hyperpolarization by activation of chloride channels" @default.
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• W2021139210 doi "https://doi.org/10.1016/j.peptides.2009.08.006" @default.
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