Mutation in CFTR associated with mild-disease-form Cl- channels with altered pore properties

David N Sheppard; Devra P Rich; Lynda S Ostedgaard; Richard J Gregory; Alan E Smith; Michael J Welsh

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Mutation in CFTR associated with mild-disease-form Cl- channels with altered pore properties

Journal article

Peer reviewed

Mutation in CFTR associated with mild-disease-form Cl- channels with altered pore properties

David N Sheppard, Devra P Rich, Lynda S Ostedgaard, Richard J Gregory, Alan E Smith and Michael J Welsh

Nature (London), Vol.362(6416), p.160

03/11/1993

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Abstract

Missense mutations of the cystic fibrosis transmembrane conductance regulator (CFTR) are associated with milder cystic fibrosis. Replacements of arginine with histidine at residue 117, tryptophan at residue 334 or proline at residue 347 affect basic amino acids located at the external end of the second and the sixth putative membrane-spanning sequences. It is reported that all three mutants are correctly processed and generate cyclic AMP-regulated Cl- currents when expressed in heterologous epithelial cells.

Cystic Fibrosis

Ion Channels

Mutagenesis

Research

Details

Title: Subtitle: Mutation in CFTR associated with mild-disease-form Cl- channels with altered pore properties
Creators: David N Sheppard
Devra P Rich
Lynda S Ostedgaard
Richard J Gregory
Alan E Smith
Michael J Welsh
Resource Type: Journal article
Publication Details: Nature (London), Vol.362(6416), p.160
Publisher: Nature Publishing Group
ISSN: 0028-0836
eISSN: 1476-4687
Language: English
Date published: 03/11/1993
Description audience: Academic
Academic Unit: Molecular Physiology and Biophysics; Neurosurgery; Fraternal Order of Eagles Diabetes Research Center; Internal Medicine; Neurology; Pulmonary, Critical Care, and Occupational Medicine
Record Identifier: 9984259505702771

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