New mammalian chloride channel identified by expression cloning

ION channels selectively permeable to chloride ions regulate cell functions as diverse as excitability and control of cell volume 1–5 . Using expression cloning techniques, a complementary DNA from an epithelial cell line has been isolated, sequenced and its putative structure examined by site-direc...

Full description

Saved in:
Bibliographic Details
Published in:Nature (London) 1992-03, Vol.356 (6366), p.238-241
Main Authors: Paulmichl, Markus, Li, Yi, Wickman, Kevin, Ackerman, Michael, Peralta, Ernest, Clapham, David
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Biochemistry
Biological and medical sciences
Calcium
Cell Line
Cell membranes. Ionic channels. Membrane pores
Cell structures and functions
Cellular biology
Chloride Channels
Cloning
Cloning, Molecular
Deoxyribonucleic acid
DNA
DNA - chemistry
DNA - genetics
DNA - isolation & purification
Dogs
Electric Conductivity
Fundamental and applied biological sciences. Psychology
Gene Expression
Genetics
Humanities and Social Sciences
Kidney
Kinetics
letter
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - physiology
Molecular and cellular biology
Molecular Sequence Data
multidisciplinary
Mutagenesis, Site-Directed
Oocytes - metabolism
Plasmids
Ribonucleic acid
RNA
Science
Science (multidisciplinary)
Transfection
Xenopus laevis
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:ION channels selectively permeable to chloride ions regulate cell functions as diverse as excitability and control of cell volume 1–5 . Using expression cloning techniques, a complementary DNA from an epithelial cell line has been isolated, sequenced and its putative structure examined by site-directed mutagenesis. This cDNA, encoding a 235-amino-acid protein, gave rise to a chloride-selective outward current when expressed in Xenopus oocytes. The expressed, outwardly rectifying chloride current was calcium-insensitive and was blocked by nucleotides applied to the cell surface. Mutation of a putative nucleotide-binding site resulted in loss of nucleotide block but incurred dependence on extracellular calcium concentration. The unusual sequence of this putative channel protein suggests a new class of ion channels not related to other previously cloned chloride channels 6–11 .
ISSN:0028-0836
1476-4687
DOI:10.1038/356238a0