Modulation of the Ca2+-Activated Cl− Channel by 14-3-3ε

Modulation of the Ca2+-Activated Cl− Channel by 14-3-3ε

We have previously reported an association of 14-3-3ε isoform with calmodulin. Using the voltage-clamp technique, the present study investigated the potential role of 14-3-3 in modulating the Ca2+-activated Cl− channel (CaCC) endogenously expressed in Xenopus oocytes. Injection of 14-3-3ϵ antisense...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Biochemical and biophysical research communications 2000-04, Vol.270 (2), p.581-587
Hauptverfasser: Chan, H.C, Wu, W.L, So, S.C, Chung, Y.W, Tsang, L.L, Wang, X.F, Yan, Y.C, Luk, S.C.W, Siu, S.S, Tsui, S.K.W, Fung, K.P, Lee, C.Y, Waye, M.M.Y
Format: Artikel
Sprache:eng
Schlagworte:
14.3.3
calcium activated chloride channel
calmodulin
human
Xenopus
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 587
container_issue 2
container_start_page 581
container_title Biochemical and biophysical research communications
container_volume 270
creator Chan, H.C
Wu, W.L
So, S.C
Chung, Y.W
Tsang, L.L
Wang, X.F
Yan, Y.C
Luk, S.C.W
Siu, S.S
Tsui, S.K.W
Fung, K.P
Lee, C.Y
Waye, M.M.Y
description We have previously reported an association of 14-3-3ε isoform with calmodulin. Using the voltage-clamp technique, the present study investigated the potential role of 14-3-3 in modulating the Ca2+-activated Cl− channel (CaCC) endogenously expressed in Xenopus oocytes. Injection of 14-3-3ϵ antisense oligodeoxynucleotides resulted in potentiation of the ionomycin-induced Cl− current, while 14-3-3 peptide and calmodulin inhibitor, W13, suppressed the antisense-potentiated current. The data suggest that 14-3-3ϵ plays an inhibitory role in modulating the CaCC by interacting with the calmodulin-dependent pathway. The potential role of 14-3-3ϵ in other tissues and its therapeutic potential for cystic fibrosis are discussed.
doi_str_mv 10.1006/bbrc.2000.2454
format Article
fullrecord <record><control><sourceid>elsevier_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1006_bbrc_2000_2454</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X00924549</els_id><sourcerecordid>S0006291X00924549</sourcerecordid><originalsourceid>FETCH-LOGICAL-c218t-afe91d56de635796bd7808b55dec6e3400e9f0e3e37f3994ab67e76e4404c9b03</originalsourceid><addsrcrecordid>eNp1j81KxDAUhYMoOI5uXWcvqTdNmjbuhqKjMOJGwV3Izy0Tqa2kdWDewLXv4mv4ED6JU8atqwMHvsP5CDnnkHEAdelc8lkOAFkuC3lAZhw0sJyDPCSzXa1YrvnzMTkZhhcAzqXSM3J134f31o6x72jf0HGNtLb5BVv4MW7siIHW7c_HJ63XtuuwpW5LuWSCie-vU3LU2HbAs7-ck6eb68f6lq0elnf1YsV8zquR2QY1D4UKqERRauVCWUHliiKgVygkAOoGUKAoG6G1tE6VWCqUEqTXDsScZPtdn_phSNiYtxRfbdoaDmYyN5O5mczNZL4Dqj2Au1ebiMkMPmLnMcSEfjShj_-hv0UpXlU</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Modulation of the Ca2+-Activated Cl− Channel by 14-3-3ε</title><source>Access via ScienceDirect (Elsevier)</source><creator>Chan, H.C ; Wu, W.L ; So, S.C ; Chung, Y.W ; Tsang, L.L ; Wang, X.F ; Yan, Y.C ; Luk, S.C.W ; Siu, S.S ; Tsui, S.K.W ; Fung, K.P ; Lee, C.Y ; Waye, M.M.Y</creator><creatorcontrib>Chan, H.C ; Wu, W.L ; So, S.C ; Chung, Y.W ; Tsang, L.L ; Wang, X.F ; Yan, Y.C ; Luk, S.C.W ; Siu, S.S ; Tsui, S.K.W ; Fung, K.P ; Lee, C.Y ; Waye, M.M.Y</creatorcontrib><description>We have previously reported an association of 14-3-3ε isoform with calmodulin. Using the voltage-clamp technique, the present study investigated the potential role of 14-3-3 in modulating the Ca2+-activated Cl− channel (CaCC) endogenously expressed in Xenopus oocytes. Injection of 14-3-3ϵ antisense oligodeoxynucleotides resulted in potentiation of the ionomycin-induced Cl− current, while 14-3-3 peptide and calmodulin inhibitor, W13, suppressed the antisense-potentiated current. The data suggest that 14-3-3ϵ plays an inhibitory role in modulating the CaCC by interacting with the calmodulin-dependent pathway. The potential role of 14-3-3ϵ in other tissues and its therapeutic potential for cystic fibrosis are discussed.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.2000.2454</identifier><language>eng</language><publisher>Elsevier Inc</publisher><subject>14.3.3 ; calcium activated chloride channel ; calmodulin ; human ; Xenopus</subject><ispartof>Biochemical and biophysical research communications, 2000-04, Vol.270 (2), p.581-587</ispartof><rights>2000 Academic Press</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c218t-afe91d56de635796bd7808b55dec6e3400e9f0e3e37f3994ab67e76e4404c9b03</citedby><cites>FETCH-LOGICAL-c218t-afe91d56de635796bd7808b55dec6e3400e9f0e3e37f3994ab67e76e4404c9b03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/bbrc.2000.2454$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids></links><search><creatorcontrib>Chan, H.C</creatorcontrib><creatorcontrib>Wu, W.L</creatorcontrib><creatorcontrib>So, S.C</creatorcontrib><creatorcontrib>Chung, Y.W</creatorcontrib><creatorcontrib>Tsang, L.L</creatorcontrib><creatorcontrib>Wang, X.F</creatorcontrib><creatorcontrib>Yan, Y.C</creatorcontrib><creatorcontrib>Luk, S.C.W</creatorcontrib><creatorcontrib>Siu, S.S</creatorcontrib><creatorcontrib>Tsui, S.K.W</creatorcontrib><creatorcontrib>Fung, K.P</creatorcontrib><creatorcontrib>Lee, C.Y</creatorcontrib><creatorcontrib>Waye, M.M.Y</creatorcontrib><title>Modulation of the Ca2+-Activated Cl− Channel by 14-3-3ε</title><title>Biochemical and biophysical research communications</title><description>We have previously reported an association of 14-3-3ε isoform with calmodulin. Using the voltage-clamp technique, the present study investigated the potential role of 14-3-3 in modulating the Ca2+-activated Cl− channel (CaCC) endogenously expressed in Xenopus oocytes. Injection of 14-3-3ϵ antisense oligodeoxynucleotides resulted in potentiation of the ionomycin-induced Cl− current, while 14-3-3 peptide and calmodulin inhibitor, W13, suppressed the antisense-potentiated current. The data suggest that 14-3-3ϵ plays an inhibitory role in modulating the CaCC by interacting with the calmodulin-dependent pathway. The potential role of 14-3-3ϵ in other tissues and its therapeutic potential for cystic fibrosis are discussed.</description><subject>14.3.3</subject><subject>calcium activated chloride channel</subject><subject>calmodulin</subject><subject>human</subject><subject>Xenopus</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><recordid>eNp1j81KxDAUhYMoOI5uXWcvqTdNmjbuhqKjMOJGwV3Izy0Tqa2kdWDewLXv4mv4ED6JU8atqwMHvsP5CDnnkHEAdelc8lkOAFkuC3lAZhw0sJyDPCSzXa1YrvnzMTkZhhcAzqXSM3J134f31o6x72jf0HGNtLb5BVv4MW7siIHW7c_HJ63XtuuwpW5LuWSCie-vU3LU2HbAs7-ck6eb68f6lq0elnf1YsV8zquR2QY1D4UKqERRauVCWUHliiKgVygkAOoGUKAoG6G1tE6VWCqUEqTXDsScZPtdn_phSNiYtxRfbdoaDmYyN5O5mczNZL4Dqj2Au1ebiMkMPmLnMcSEfjShj_-hv0UpXlU</recordid><startdate>20000413</startdate><enddate>20000413</enddate><creator>Chan, H.C</creator><creator>Wu, W.L</creator><creator>So, S.C</creator><creator>Chung, Y.W</creator><creator>Tsang, L.L</creator><creator>Wang, X.F</creator><creator>Yan, Y.C</creator><creator>Luk, S.C.W</creator><creator>Siu, S.S</creator><creator>Tsui, S.K.W</creator><creator>Fung, K.P</creator><creator>Lee, C.Y</creator><creator>Waye, M.M.Y</creator><general>Elsevier Inc</general><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20000413</creationdate><title>Modulation of the Ca2+-Activated Cl− Channel by 14-3-3ε</title><author>Chan, H.C ; Wu, W.L ; So, S.C ; Chung, Y.W ; Tsang, L.L ; Wang, X.F ; Yan, Y.C ; Luk, S.C.W ; Siu, S.S ; Tsui, S.K.W ; Fung, K.P ; Lee, C.Y ; Waye, M.M.Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c218t-afe91d56de635796bd7808b55dec6e3400e9f0e3e37f3994ab67e76e4404c9b03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>14.3.3</topic><topic>calcium activated chloride channel</topic><topic>calmodulin</topic><topic>human</topic><topic>Xenopus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chan, H.C</creatorcontrib><creatorcontrib>Wu, W.L</creatorcontrib><creatorcontrib>So, S.C</creatorcontrib><creatorcontrib>Chung, Y.W</creatorcontrib><creatorcontrib>Tsang, L.L</creatorcontrib><creatorcontrib>Wang, X.F</creatorcontrib><creatorcontrib>Yan, Y.C</creatorcontrib><creatorcontrib>Luk, S.C.W</creatorcontrib><creatorcontrib>Siu, S.S</creatorcontrib><creatorcontrib>Tsui, S.K.W</creatorcontrib><creatorcontrib>Fung, K.P</creatorcontrib><creatorcontrib>Lee, C.Y</creatorcontrib><creatorcontrib>Waye, M.M.Y</creatorcontrib><collection>CrossRef</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chan, H.C</au><au>Wu, W.L</au><au>So, S.C</au><au>Chung, Y.W</au><au>Tsang, L.L</au><au>Wang, X.F</au><au>Yan, Y.C</au><au>Luk, S.C.W</au><au>Siu, S.S</au><au>Tsui, S.K.W</au><au>Fung, K.P</au><au>Lee, C.Y</au><au>Waye, M.M.Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Modulation of the Ca2+-Activated Cl− Channel by 14-3-3ε</atitle><jtitle>Biochemical and biophysical research communications</jtitle><date>2000-04-13</date><risdate>2000</risdate><volume>270</volume><issue>2</issue><spage>581</spage><epage>587</epage><pages>581-587</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>We have previously reported an association of 14-3-3ε isoform with calmodulin. Using the voltage-clamp technique, the present study investigated the potential role of 14-3-3 in modulating the Ca2+-activated Cl− channel (CaCC) endogenously expressed in Xenopus oocytes. Injection of 14-3-3ϵ antisense oligodeoxynucleotides resulted in potentiation of the ionomycin-induced Cl− current, while 14-3-3 peptide and calmodulin inhibitor, W13, suppressed the antisense-potentiated current. The data suggest that 14-3-3ϵ plays an inhibitory role in modulating the CaCC by interacting with the calmodulin-dependent pathway. The potential role of 14-3-3ϵ in other tissues and its therapeutic potential for cystic fibrosis are discussed.</abstract><pub>Elsevier Inc</pub><doi>10.1006/bbrc.2000.2454</doi><tpages>7</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0006-291X
ispartof Biochemical and biophysical research communications, 2000-04, Vol.270 (2), p.581-587
issn 0006-291X
1090-2104
language eng
recordid cdi_crossref_primary_10_1006_bbrc_2000_2454
source Access via ScienceDirect (Elsevier)
subjects 14.3.3
calcium activated chloride channel
calmodulin
human
Xenopus
title Modulation of the Ca2+-Activated Cl− Channel by 14-3-3ε
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-26T22%3A33%3A53IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-elsevier_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Modulation%20of%20the%20Ca2+-Activated%20Cl%E2%88%92%20Channel%20by%2014-3-3%CE%B5&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Chan,%20H.C&rft.date=2000-04-13&rft.volume=270&rft.issue=2&rft.spage=581&rft.epage=587&rft.pages=581-587&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1006/bbrc.2000.2454&rft_dat=%3Celsevier_cross%3ES0006291X00924549%3C/elsevier_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rft_els_id=S0006291X00924549&rfr_iscdi=true