Molecular characterization of the epithelial NaKCl cotransporter isoforms

Recent advances in the molecular characterization of specific isoforms of the NaKCl cotransporter have allowed rapid progress in the study of the structure, function, and regulation of these members of a family of Cl-dependent cation cotransporters. Two distinct isoforms have been identified, one...

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Bibliographic Details
Published in:Current opinion in cell biology 1995, Vol.7 (4), p.493-503
Main Authors: Payne, John A, Forbush, Bliss
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Carrier Proteins - chemistry
Carrier Proteins - metabolism
Chlorides - metabolism
Epithelium - chemistry
Epithelium - metabolism
Humans
Membrane Proteins - chemistry
Membrane Proteins - metabolism
Molecular Sequence Data
Potassium - metabolism
Sodium - metabolism
Sodium-Potassium-Chloride Symporters
Structure-Activity Relationship
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Summary:Recent advances in the molecular characterization of specific isoforms of the NaKCl cotransporter have allowed rapid progress in the study of the structure, function, and regulation of these members of a family of Cl-dependent cation cotransporters. Two distinct isoforms have been identified, one from Cl −-secretory epithelia and another found specifically in the diluting segment of the vertebrate kidney, a Cl −-absorptive epithelium. The discovery of three alternatively spliced variants of the absorptive isoform, which differ only by 31 amino acids and which appear to be differentially distributed within the mammalian thick ascending limb of the loop of Henle, highlight this spliced region as an important functional component of the protein.
ISSN:0955-0674
1879-0410
DOI:10.1016/0955-0674(95)80005-0