Demonstration that CFTR is a chloride channel by alteration of its anion selectivity

Matthew P Anderson; Richard J Gregory; Simon Thompson; David W Souza; Sucharita Paul; Richard C Mulligan; Alan E Smith; Michael J Welsh

doi:10.1126/science.1712984

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Demonstration that CFTR is a chloride channel by alteration of its anion selectivity

Journal article

Peer reviewed

Demonstration that CFTR is a chloride channel by alteration of its anion selectivity

Matthew P Anderson, Richard J Gregory, Simon Thompson, David W Souza, Sucharita Paul, Richard C Mulligan, Alan E Smith and Michael J Welsh

Science (American Association for the Advancement of Science), Vol.253(5016), pp.202-205

1991

DOI: 10.1126/science.1712984

PMID: 1712984

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Abstract

Expression of the cystic fibrosis transmembrane conductance regulator (CFTR) generates adenosine 3',5'-monophosphate (cAMP)-regulated chloride channels, indicating that CFTR is either a chloride channel or a chloride channel regulator. To distinguish between these possibilities, basic amino acids in the putative transmembrane domains were mutated. The sequence of anion selectivity of cAMP-regulated channels in cells containing either endogenous or recombinant CFTR was bromide greater than chloride greater than iodide greater than fluoride. Mutation of the lysines at positions 95 or 335 to acidic amino acids converted the selectivity sequence to iodide greater than bromide greater than chloride greater than fluoride. These data indicate that CFTR is a cAMP-regulated chloride channel and that lysines 95 and 335 determine anion selectivity.

Gastroenterology. Liver. Pancreas. Abdomen

Biological and medical sciences

Medical sciences

Liver. Biliary tract. Portal circulation. Exocrine pancreas

Other diseases. Semiology

Details

Title: Subtitle: Demonstration that CFTR is a chloride channel by alteration of its anion selectivity
Creators: Matthew P Anderson - Univ. Iowa coll. medicine, Howard Hughes medical inst., dep. internal medicine, Iowa city IA 52242, United States
Richard J Gregory - Univ. Iowa coll. medicine, Howard Hughes medical inst., dep. internal medicine, Iowa city IA 52242, United States
Simon Thompson - Univ. Iowa coll. medicine, Howard Hughes medical inst., dep. internal medicine, Iowa city IA 52242, United States
David W Souza - Univ. Iowa coll. medicine, Howard Hughes medical inst., dep. internal medicine, Iowa city IA 52242, United States
Sucharita Paul - Univ. Iowa coll. medicine, Howard Hughes medical inst., dep. internal medicine, Iowa city IA 52242, United States
Richard C Mulligan - Univ. Iowa coll. medicine, Howard Hughes medical inst., dep. internal medicine, Iowa city IA 52242, United States
Alan E Smith - Univ. Iowa coll. medicine, Howard Hughes medical inst., dep. internal medicine, Iowa city IA 52242, United States
Michael J Welsh - Univ. Iowa coll. medicine, Howard Hughes medical inst., dep. internal medicine, Iowa city IA 52242, United States
Resource Type: Journal article
Publication Details: Science (American Association for the Advancement of Science), Vol.253(5016), pp.202-205
Publisher: American Association for the Advancement of Science; Washington, DC
DOI: 10.1126/science.1712984
PMID: 1712984
ISSN: 0036-8075
eISSN: 1095-9203
Language: English
Date published: 1991
Academic Unit: Neurology; Molecular Physiology and Biophysics; Neurosurgery; Internal Medicine
Record Identifier: 9984020720602771

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