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Molecular characterization of the epithelial NaKCl cotransporter isoforms
Recent advances in the molecular characterization of specific isoforms of the NaKCl 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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Published in: | Current opinion in cell biology 1995, Vol.7 (4), p.493-503 |
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container_title | Current opinion in cell biology |
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creator | Payne, John A Forbush, Bliss |
description | Recent advances in the molecular characterization of specific isoforms of the NaKCl 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. |
doi_str_mv | 10.1016/0955-0674(95)80005-0 |
format | article |
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ispartof | Current opinion in cell biology, 1995, Vol.7 (4), p.493-503 |
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language | eng |
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source | ScienceDirect Journals |
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 |
title | Molecular characterization of the epithelial NaKCl cotransporter isoforms |
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