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PMID: 8755607 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Sensitivity of a renal K+ channel (ROMK2) to the inhibitory sulfonylurea compound glibenclamide is enhanced by coexpression with the ATP-binding cassette transporter cystic fibrosis transmembrane regulator.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 93 ·No. 15 ·1996-07-23 ·Pages 8083-8

McNicholas CM, Guggino WB, Schwiebert EM, Hebert SC, Giebisch G, Egan ME

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.

MeSH Terms
Adenosine Triphosphate/pharmacology Animals Chloride Channels/physiology Cyclic AMP-Dependent Protein Kinases/pharmacology Cystic Fibrosis Transmembrane Conductance Regulator/biosynthesis,physiology Female Glyburide/pharmacology Kidney/physiology Membrane Potentials/drug effects,physiology Oocytes/drug effects,physiology Patch-Clamp Techniques Phosphorylation Potassium Channels/biosynthesis,drug effects,physiology Potassium Channels, Inwardly Rectifying Sodium Channels/physiology Xenopus laevis
Chemicals
Chloride Channels Potassium Channels Potassium Channels, Inwardly Rectifying Sodium Channels Cystic Fibrosis Transmembrane Conductance Regulator Adenosine Triphosphate Cyclic AMP-Dependent Protein Kinases Glyburide
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
McNicholas C M
Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06520-8026, USA.
Guggino W B
Schwiebert E M
Hebert S C
Giebisch G
Egan M E
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.93.15.8083
Published
1996-07-23
Pages
8083-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC38879
Subset
IM
Grants
NHLBI NIH HHS · HL47122 · United States
PHS HHS · DR32753 · United States
NIDDK NIH HHS · DK17433 · United States
NIDDK NIH HHS · R01 DK053428 · United States
NIDDK NIH HHS · P01 DK017433 · United States
External Links
PubMed source DOI: 10.1073/pnas.93.15.8083 PMC Full Text View journal details
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