Loading…

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...

Full description

Saved in:
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:
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!
cited_by cdi_FETCH-LOGICAL-c384t-6888f45ffe8ed6c6f2ea967012a6fc58a0ee82156bea8f2f9c4535e15b72603f3
cites cdi_FETCH-LOGICAL-c384t-6888f45ffe8ed6c6f2ea967012a6fc58a0ee82156bea8f2f9c4535e15b72603f3
container_end_page 503
container_issue 4
container_start_page 493
container_title Current opinion in cell biology
container_volume 7
creator Payne, John A
Forbush, Bliss
description 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.
doi_str_mv 10.1016/0955-0674(95)80005-0
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_77519231</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0955067495800050</els_id><sourcerecordid>77519231</sourcerecordid><originalsourceid>FETCH-LOGICAL-c384t-6888f45ffe8ed6c6f2ea967012a6fc58a0ee82156bea8f2f9c4535e15b72603f3</originalsourceid><addsrcrecordid>eNp9kE1OwzAQhS0EKuXnBiBlhWARsJPYcTZIqOJPFLqBteU6Y9XIiYOdIMFFuAqn4gy4tOqSxWg0eu_NaD6Ejgg-J5iwC1xRmmJWFqcVPeMY4zhtoTHhZZXiguBtNN5YdtFeCK_Rw3BWjdCoLKLC-BjNHp0FNVjpE7WQXqoevPmUvXFt4nTSLyCBzsRmjbTJk_z5-n6INbGJcr2Xbeicj5HEBKedb8IB2tHSBjhc9330cnP9PLlLp7Pb-8nVNFU5L_qUcc51QbUGDjVTTGcgK1ZikkmmFeUSA_CMUDYHyXWmK1XQnAKh8zJjONf5PjpZ7e28exsg9KIxQYG1sgU3BFGWlFRZTqKxWBmVdyF40KLzppH-QxAslhzFEpJYQhIVFX8cBY6x4_X-Yd5AvQmtwUX9cqVDfPLdgBdBGWgV1MaD6kXtzP8HfgG9eoUO</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>77519231</pqid></control><display><type>article</type><title>Molecular characterization of the epithelial NaKCl cotransporter isoforms</title><source>ScienceDirect Journals</source><creator>Payne, John A ; Forbush, Bliss</creator><creatorcontrib>Payne, John A ; Forbush, Bliss</creatorcontrib><description>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.</description><identifier>ISSN: 0955-0674</identifier><identifier>EISSN: 1879-0410</identifier><identifier>DOI: 10.1016/0955-0674(95)80005-0</identifier><identifier>PMID: 7495568</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>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</subject><ispartof>Current opinion in cell biology, 1995, Vol.7 (4), p.493-503</ispartof><rights>1995</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c384t-6888f45ffe8ed6c6f2ea967012a6fc58a0ee82156bea8f2f9c4535e15b72603f3</citedby><cites>FETCH-LOGICAL-c384t-6888f45ffe8ed6c6f2ea967012a6fc58a0ee82156bea8f2f9c4535e15b72603f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4023,27922,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7495568$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Payne, John A</creatorcontrib><creatorcontrib>Forbush, Bliss</creatorcontrib><title>Molecular characterization of the epithelial NaKCl cotransporter isoforms</title><title>Current opinion in cell biology</title><addtitle>Curr Opin Cell Biol</addtitle><description>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.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - metabolism</subject><subject>Chlorides - metabolism</subject><subject>Epithelium - chemistry</subject><subject>Epithelium - metabolism</subject><subject>Humans</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Potassium - metabolism</subject><subject>Sodium - metabolism</subject><subject>Sodium-Potassium-Chloride Symporters</subject><subject>Structure-Activity Relationship</subject><issn>0955-0674</issn><issn>1879-0410</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNp9kE1OwzAQhS0EKuXnBiBlhWARsJPYcTZIqOJPFLqBteU6Y9XIiYOdIMFFuAqn4gy4tOqSxWg0eu_NaD6Ejgg-J5iwC1xRmmJWFqcVPeMY4zhtoTHhZZXiguBtNN5YdtFeCK_Rw3BWjdCoLKLC-BjNHp0FNVjpE7WQXqoevPmUvXFt4nTSLyCBzsRmjbTJk_z5-n6INbGJcr2Xbeicj5HEBKedb8IB2tHSBjhc9330cnP9PLlLp7Pb-8nVNFU5L_qUcc51QbUGDjVTTGcgK1ZikkmmFeUSA_CMUDYHyXWmK1XQnAKh8zJjONf5PjpZ7e28exsg9KIxQYG1sgU3BFGWlFRZTqKxWBmVdyF40KLzppH-QxAslhzFEpJYQhIVFX8cBY6x4_X-Yd5AvQmtwUX9cqVDfPLdgBdBGWgV1MaD6kXtzP8HfgG9eoUO</recordid><startdate>1995</startdate><enddate>1995</enddate><creator>Payne, John A</creator><creator>Forbush, Bliss</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>1995</creationdate><title>Molecular characterization of the epithelial NaKCl cotransporter isoforms</title><author>Payne, John A ; Forbush, Bliss</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c384t-6888f45ffe8ed6c6f2ea967012a6fc58a0ee82156bea8f2f9c4535e15b72603f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - metabolism</topic><topic>Chlorides - metabolism</topic><topic>Epithelium - chemistry</topic><topic>Epithelium - metabolism</topic><topic>Humans</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Potassium - metabolism</topic><topic>Sodium - metabolism</topic><topic>Sodium-Potassium-Chloride Symporters</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Payne, John A</creatorcontrib><creatorcontrib>Forbush, Bliss</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Current opinion in cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Payne, John A</au><au>Forbush, Bliss</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular characterization of the epithelial NaKCl cotransporter isoforms</atitle><jtitle>Current opinion in cell biology</jtitle><addtitle>Curr Opin Cell Biol</addtitle><date>1995</date><risdate>1995</risdate><volume>7</volume><issue>4</issue><spage>493</spage><epage>503</epage><pages>493-503</pages><issn>0955-0674</issn><eissn>1879-0410</eissn><abstract>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.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>7495568</pmid><doi>10.1016/0955-0674(95)80005-0</doi><tpages>11</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0955-0674
ispartof Current opinion in cell biology, 1995, Vol.7 (4), p.493-503
issn 0955-0674
1879-0410
language eng
recordid cdi_proquest_miscellaneous_77519231
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 NaKCl cotransporter isoforms
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-09T06%3A24%3A12IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Molecular%20characterization%20of%20the%20epithelial%20Na%EE%97%B8K%EE%97%B8Cl%20cotransporter%20isoforms&rft.jtitle=Current%20opinion%20in%20cell%20biology&rft.au=Payne,%20John%20A&rft.date=1995&rft.volume=7&rft.issue=4&rft.spage=493&rft.epage=503&rft.pages=493-503&rft.issn=0955-0674&rft.eissn=1879-0410&rft_id=info:doi/10.1016/0955-0674(95)80005-0&rft_dat=%3Cproquest_cross%3E77519231%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c384t-6888f45ffe8ed6c6f2ea967012a6fc58a0ee82156bea8f2f9c4535e15b72603f3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=77519231&rft_id=info:pmid/7495568&rfr_iscdi=true