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Phosphorylation‐activated chloride channels in human skin fibroblasts
Author(s) -
Bear Christine E.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80189-3
Subject(s) - chloride channel , dids , forskolin , cystic fibrosis transmembrane conductance regulator , chemistry , biophysics , patch clamp , electrophysiology , protein subunit , ion channel , membrane potential , phosphorylation , protein kinase a , microbiology and biotechnology , chloride , biochemistry , membrane , medicine , biology , receptor , gene , organic chemistry
A chloride‐selective channel has been found using patch‐clamp electrophysiology in human skin fibroblasts and it exhibits many of the biophysical properties of the Cl − channel found in airway epithelia. As in the case of epithelial Cl − channels, Cl − channels in fibroblasts are activated at depolarized membrane potentials in excised patches, rectifying in an outward direction with a unit conductance of 33 pS at 0 mV. Furthermore, the agonists forskolin and prostaglandin E 2 evoke Cl − channel activity in cell‐attached patches. The effect of these agonists can be mimicked by direct application of catalytic subunit of protein kinase A with ATP and Mg 2+ to the internal membrane surface of excised, inside‐out patches. The Cl − channel is also sensitive to inhibition by the stilbene derivative, DIDS. These results indicate that fibroblasts may provide a convenient and available model for the study of epithelial Cl − channel regulation and accelerate efforts to determine the regulatory defect expressed in cystic fibrosis.