Multiple Modes of Regulation of Na+/H+ Exchangers

: Mammalian Na+/H+ exchangers (NHE) mediate electroneutral countertransport of H+ for Na+ across the plasmalemmal and organellar membranes. They contribute to cellular and organellar pH and volume regulation and transepithelial Na+ transport. The aim of this review is to illustrate the complex regul...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Annals of the New York Academy of Sciences 2002-11, Vol.976 (1), p.248-258
Hauptverfasser: HAYASHI, HISAYOSHI, SZÁSZI, KATALIN, GRINSTEIN, SERGIO
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 258
container_issue 1
container_start_page 248
container_title Annals of the New York Academy of Sciences
container_volume 976
creator HAYASHI, HISAYOSHI
SZÁSZI, KATALIN
GRINSTEIN, SERGIO
description : Mammalian Na+/H+ exchangers (NHE) mediate electroneutral countertransport of H+ for Na+ across the plasmalemmal and organellar membranes. They contribute to cellular and organellar pH and volume regulation and transepithelial Na+ transport. The aim of this review is to illustrate the complex regulation of these transporters by focusing on the multiple mechanisms controlling the epithelial isoform, NHE3. A variety of agents and conditions (e.g., hormones, growth factors, cellular pH, and medium osmolarity) act in concert to achieve short‐term and long‐term regulation of this isoform. The underlying mechanism involves changes in the number of transporters on the cell surface and/or altered activity of the individual exchangers due to allosteric activation by intracellular protons, phosphorylation and interaction with accessory proteins and the cytoskeleton. A similar regulatory versatility probably applies to other NHE isoforms, and the lessons learned from studying members of the NHE family could serve as a useful reference when exploring the modes and levels of regulation of other transporters.
doi_str_mv 10.1111/j.1749-6632.2002.tb04747.x
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_72791669</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>72791669</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4758-1f2a9d8eaa213c17c1b30b8644b005ee261d6c178fe119e4f9386124e63fc9993</originalsourceid><addsrcrecordid>eNqVkFtPwjAYhhujEUT_giFeeEM2elq7emOQcDABTDwRr5pufMPhYLhucfx7t0Dw2t40_b73fZo8CN0Q7JLqdFcukVw5QjDqUoypmweYSy7d8gQ1j6tT1MRYSsdXlDXQhbUrjAn1uTxHDUI9TD0hm4hMiySPtwm0p-kCbDuN2s-wLBKTx-mmfs1MpzvutAdl-Gk2S8jsJTqLTGLh6nC30Ntw8NofO5On0WO_N3FCLj3fIRE1auGDMZSwkMiQBAwHvuA8wNgDoIIsRDX3IyBEAY8U8wWhHASLQqUUa6HbPXebpd8F2FyvYxtCkpgNpIXVkkpFhKiDd_tgmKXWZhDpbRavTbbTBOtamF7p2oqurehamD4I02VVvj78UgRrWPxVD4aqwP0-8BMnsPsHWs8-ei-U-xXB2RNim0N5JJjsS1d86en5bKQf5uJ9yCjWHvsF2gSHwg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>72791669</pqid></control><display><type>article</type><title>Multiple Modes of Regulation of Na+/H+ Exchangers</title><source>Wiley-Blackwell Journals</source><source>MEDLINE</source><creator>HAYASHI, HISAYOSHI ; SZÁSZI, KATALIN ; GRINSTEIN, SERGIO</creator><creatorcontrib>HAYASHI, HISAYOSHI ; SZÁSZI, KATALIN ; GRINSTEIN, SERGIO</creatorcontrib><description>: Mammalian Na+/H+ exchangers (NHE) mediate electroneutral countertransport of H+ for Na+ across the plasmalemmal and organellar membranes. They contribute to cellular and organellar pH and volume regulation and transepithelial Na+ transport. The aim of this review is to illustrate the complex regulation of these transporters by focusing on the multiple mechanisms controlling the epithelial isoform, NHE3. A variety of agents and conditions (e.g., hormones, growth factors, cellular pH, and medium osmolarity) act in concert to achieve short‐term and long‐term regulation of this isoform. The underlying mechanism involves changes in the number of transporters on the cell surface and/or altered activity of the individual exchangers due to allosteric activation by intracellular protons, phosphorylation and interaction with accessory proteins and the cytoskeleton. A similar regulatory versatility probably applies to other NHE isoforms, and the lessons learned from studying members of the NHE family could serve as a useful reference when exploring the modes and levels of regulation of other transporters.</description><identifier>ISSN: 0077-8923</identifier><identifier>EISSN: 1749-6632</identifier><identifier>DOI: 10.1111/j.1749-6632.2002.tb04747.x</identifier><identifier>PMID: 12502567</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Animals ; Biological Transport ; Cell Membrane - metabolism ; Electrophysiology ; epithelial Na+/H+ exchanger ; Hormones - physiology ; Hydrogen-Ion Concentration ; Intracellular Membranes - metabolism ; intracellular pH ; NHE ; Phosphorylation ; Protons ; Sodium - metabolism ; Sodium-Hydrogen Exchanger 3 ; Sodium-Hydrogen Exchangers - genetics ; Sodium-Hydrogen Exchangers - physiology ; transport regulation</subject><ispartof>Annals of the New York Academy of Sciences, 2002-11, Vol.976 (1), p.248-258</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4758-1f2a9d8eaa213c17c1b30b8644b005ee261d6c178fe119e4f9386124e63fc9993</citedby><cites>FETCH-LOGICAL-c4758-1f2a9d8eaa213c17c1b30b8644b005ee261d6c178fe119e4f9386124e63fc9993</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1749-6632.2002.tb04747.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1749-6632.2002.tb04747.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27915,27916,45565,45566</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12502567$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>HAYASHI, HISAYOSHI</creatorcontrib><creatorcontrib>SZÁSZI, KATALIN</creatorcontrib><creatorcontrib>GRINSTEIN, SERGIO</creatorcontrib><title>Multiple Modes of Regulation of Na+/H+ Exchangers</title><title>Annals of the New York Academy of Sciences</title><addtitle>Ann N Y Acad Sci</addtitle><description>: Mammalian Na+/H+ exchangers (NHE) mediate electroneutral countertransport of H+ for Na+ across the plasmalemmal and organellar membranes. They contribute to cellular and organellar pH and volume regulation and transepithelial Na+ transport. The aim of this review is to illustrate the complex regulation of these transporters by focusing on the multiple mechanisms controlling the epithelial isoform, NHE3. A variety of agents and conditions (e.g., hormones, growth factors, cellular pH, and medium osmolarity) act in concert to achieve short‐term and long‐term regulation of this isoform. The underlying mechanism involves changes in the number of transporters on the cell surface and/or altered activity of the individual exchangers due to allosteric activation by intracellular protons, phosphorylation and interaction with accessory proteins and the cytoskeleton. A similar regulatory versatility probably applies to other NHE isoforms, and the lessons learned from studying members of the NHE family could serve as a useful reference when exploring the modes and levels of regulation of other transporters.</description><subject>Animals</subject><subject>Biological Transport</subject><subject>Cell Membrane - metabolism</subject><subject>Electrophysiology</subject><subject>epithelial Na+/H+ exchanger</subject><subject>Hormones - physiology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Intracellular Membranes - metabolism</subject><subject>intracellular pH</subject><subject>NHE</subject><subject>Phosphorylation</subject><subject>Protons</subject><subject>Sodium - metabolism</subject><subject>Sodium-Hydrogen Exchanger 3</subject><subject>Sodium-Hydrogen Exchangers - genetics</subject><subject>Sodium-Hydrogen Exchangers - physiology</subject><subject>transport regulation</subject><issn>0077-8923</issn><issn>1749-6632</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkFtPwjAYhhujEUT_giFeeEM2elq7emOQcDABTDwRr5pufMPhYLhucfx7t0Dw2t40_b73fZo8CN0Q7JLqdFcukVw5QjDqUoypmweYSy7d8gQ1j6tT1MRYSsdXlDXQhbUrjAn1uTxHDUI9TD0hm4hMiySPtwm0p-kCbDuN2s-wLBKTx-mmfs1MpzvutAdl-Gk2S8jsJTqLTGLh6nC30Ntw8NofO5On0WO_N3FCLj3fIRE1auGDMZSwkMiQBAwHvuA8wNgDoIIsRDX3IyBEAY8U8wWhHASLQqUUa6HbPXebpd8F2FyvYxtCkpgNpIXVkkpFhKiDd_tgmKXWZhDpbRavTbbTBOtamF7p2oqurehamD4I02VVvj78UgRrWPxVD4aqwP0-8BMnsPsHWs8-ei-U-xXB2RNim0N5JJjsS1d86en5bKQf5uJ9yCjWHvsF2gSHwg</recordid><startdate>200211</startdate><enddate>200211</enddate><creator>HAYASHI, HISAYOSHI</creator><creator>SZÁSZI, KATALIN</creator><creator>GRINSTEIN, SERGIO</creator><general>Blackwell Publishing Ltd</general><scope>BSCLL</scope><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>200211</creationdate><title>Multiple Modes of Regulation of Na+/H+ Exchangers</title><author>HAYASHI, HISAYOSHI ; SZÁSZI, KATALIN ; GRINSTEIN, SERGIO</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4758-1f2a9d8eaa213c17c1b30b8644b005ee261d6c178fe119e4f9386124e63fc9993</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Biological Transport</topic><topic>Cell Membrane - metabolism</topic><topic>Electrophysiology</topic><topic>epithelial Na+/H+ exchanger</topic><topic>Hormones - physiology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Intracellular Membranes - metabolism</topic><topic>intracellular pH</topic><topic>NHE</topic><topic>Phosphorylation</topic><topic>Protons</topic><topic>Sodium - metabolism</topic><topic>Sodium-Hydrogen Exchanger 3</topic><topic>Sodium-Hydrogen Exchangers - genetics</topic><topic>Sodium-Hydrogen Exchangers - physiology</topic><topic>transport regulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>HAYASHI, HISAYOSHI</creatorcontrib><creatorcontrib>SZÁSZI, KATALIN</creatorcontrib><creatorcontrib>GRINSTEIN, SERGIO</creatorcontrib><collection>Istex</collection><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>Annals of the New York Academy of Sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>HAYASHI, HISAYOSHI</au><au>SZÁSZI, KATALIN</au><au>GRINSTEIN, SERGIO</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Multiple Modes of Regulation of Na+/H+ Exchangers</atitle><jtitle>Annals of the New York Academy of Sciences</jtitle><addtitle>Ann N Y Acad Sci</addtitle><date>2002-11</date><risdate>2002</risdate><volume>976</volume><issue>1</issue><spage>248</spage><epage>258</epage><pages>248-258</pages><issn>0077-8923</issn><eissn>1749-6632</eissn><abstract>: Mammalian Na+/H+ exchangers (NHE) mediate electroneutral countertransport of H+ for Na+ across the plasmalemmal and organellar membranes. They contribute to cellular and organellar pH and volume regulation and transepithelial Na+ transport. The aim of this review is to illustrate the complex regulation of these transporters by focusing on the multiple mechanisms controlling the epithelial isoform, NHE3. A variety of agents and conditions (e.g., hormones, growth factors, cellular pH, and medium osmolarity) act in concert to achieve short‐term and long‐term regulation of this isoform. The underlying mechanism involves changes in the number of transporters on the cell surface and/or altered activity of the individual exchangers due to allosteric activation by intracellular protons, phosphorylation and interaction with accessory proteins and the cytoskeleton. A similar regulatory versatility probably applies to other NHE isoforms, and the lessons learned from studying members of the NHE family could serve as a useful reference when exploring the modes and levels of regulation of other transporters.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>12502567</pmid><doi>10.1111/j.1749-6632.2002.tb04747.x</doi><tpages>11</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0077-8923
ispartof Annals of the New York Academy of Sciences, 2002-11, Vol.976 (1), p.248-258
issn 0077-8923
1749-6632
language eng
recordid cdi_proquest_miscellaneous_72791669
source Wiley-Blackwell Journals; MEDLINE
subjects Animals
Biological Transport
Cell Membrane - metabolism
Electrophysiology
epithelial Na+/H+ exchanger
Hormones - physiology
Hydrogen-Ion Concentration
Intracellular Membranes - metabolism
intracellular pH
NHE
Phosphorylation
Protons
Sodium - metabolism
Sodium-Hydrogen Exchanger 3
Sodium-Hydrogen Exchangers - genetics
Sodium-Hydrogen Exchangers - physiology
transport regulation
title Multiple Modes of Regulation of Na+/H+ Exchangers
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-14T20%3A23%3A57IST&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=Multiple%20Modes%20of%20Regulation%20of%20Na+/H+%20Exchangers&rft.jtitle=Annals%20of%20the%20New%20York%20Academy%20of%20Sciences&rft.au=HAYASHI,%20HISAYOSHI&rft.date=2002-11&rft.volume=976&rft.issue=1&rft.spage=248&rft.epage=258&rft.pages=248-258&rft.issn=0077-8923&rft.eissn=1749-6632&rft_id=info:doi/10.1111/j.1749-6632.2002.tb04747.x&rft_dat=%3Cproquest_cross%3E72791669%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=72791669&rft_id=info:pmid/12502567&rfr_iscdi=true