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Content Provider | World Health Organization (WHO)-Global Index Medicus |
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Author | Egan, M. E. Guggino, W. B. Giebisch, G. Mcnicholas, C. M. Schwiebert, E. M. Hebert, S. C. |
Description | Author Affiliation: McNicholas CM ( Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06520-8026, USA.); |
Abstract | We demonstrate here that coexpression of ROMK2, an inwardly rectifying ATP-sensitive renal K+ channel (IKATP) with cystic fibrosis transmembrane regulator (CFTR) significantly enhances the sensitivity of ROMK2 to the sulfonylurea compound glibenclamide. When expressed alone, ROMK2 is relatively insensitive to glibenclamide. The interaction between ROMK2, CFTR, and glibenclamide is modulated by altering the phosphorylation state of either ROMK2, CFTR, or an associated protein, as exogenous MgATP and the catalytic subunit of protein kinase A significantly attenuate the inhibitory effect of glibenclamide on ROMK2. Thus CFTR, which has been demonstrated to interact with both Na+ and Cl- channels in airway epithelium, modulates the function of renal ROMK2 K+ channels. |
ISSN | 00278424 |
e-ISSN | 10916490 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Issue Number | 15 |
Volume Number | 93 |
Language | English |
Publisher | National Academy of Sciences |
Publisher Date | 1996-10-01 |
Publisher Place | United States |
Access Restriction | Open |
Subject Keyword | Adenosine Triphosphate Pharmacology Cystic Fibrosis Transmembrane Conductance Regulator Physiology Glyburide Kidney Potassium Channels, Inwardly Rectifying Potassium Channels Animals Chloride Channels Cyclic AMP-Dependent Protein Kinases Biosynthesis Membrane Potentials Drug Effects Oocytes Patch-Clamp Techniques Phosphorylation Sodium Channels Xenopus Laevis Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
Content Type | Text |
Resource Type | Article |
Subject | Multidisciplinary |
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