Evidence for Na+/Ca2+ Exchanger 1 Association with Caveolin‐1 and ‐2 in C6 Glioma Cells

The purpose of this study is to understand the interaction of Na+‐Ca2+ exchanger (NCX1), that is one of the essential regulators of Ca2+ homeostasis, with caveolin (Cav)‐1 and Cav‐2 in Cav‐3 null cell (rat C6 glioma cell). Both mRNA and protein expression of NCX1, Cav‐1 and Cav‐2 was observed, but n...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:IUBMB life 2004-10, Vol.56 (10), p.621-627
Hauptverfasser: Cha, Seok Ho, Shin, Sun Young, Jung, Sang Yong, Kim, Yun Tai, Park, Yong Joo, Kwak, Jin‐Oh, Kim, Hyun‐Woo, Suh, Chang Kook
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 627
container_issue 10
container_start_page 621
container_title IUBMB life
container_volume 56
creator Cha, Seok Ho
Shin, Sun Young
Jung, Sang Yong
Kim, Yun Tai
Park, Yong Joo
Kwak, Jin‐Oh
Kim, Hyun‐Woo
Suh, Chang Kook
description The purpose of this study is to understand the interaction of Na+‐Ca2+ exchanger (NCX1), that is one of the essential regulators of Ca2+ homeostasis, with caveolin (Cav)‐1 and Cav‐2 in Cav‐3 null cell (rat C6 glioma cell). Both mRNA and protein expression of NCX1, Cav‐1 and Cav‐2 was observed, but no expression of mRNA and protein of Cav‐3 were observed in C6 glioma cells. In isolated caveolae‐enriched membrane fraction, the NCX1, Cav‐1 and Cav‐2 proteins localized in same fractions. The experiment of immuno‐precipitation showed complex formation between the NCX1 and Cavs. Confocal microscopy also supported co‐localization of NCX1 and Cavs at the plasma membrane. Functionally, sodium‐free induced forward mode of NCX1 attenuated by Cav‐1 antisense ODN. When treated cells with Cav‐2 antisense ODN, both reverse and forward mode of NCX1 was attenuated. From these results, in the Cav‐3 lacking cells, the function of NCX1 might be regulated by binding with Cavs. Considering the decrement of NCX1 activity by antisense ODNs, caveolins may play an important role in diverse of pathophysiological process of NCX1‐related disorders in the body. IUBMB Life, 56: 621‐627, 2004
doi_str_mv 10.1080/15216540400020353
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67278649</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>67278649</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3258-31f99355f1df6b52e4625fac83ae08a7637438ada120a17a8a555d35585f45b33</originalsourceid><addsrcrecordid>eNqFkD1Ow0AQhVcIRELgADRoK5rIZGf_vJFoEisEpABNqCisib0mixw7ePNDOo7AGTkJjhJBQUE1b0bfexo9Qs6BXQEzrAOKg1aSScYYZ0KJA9Lc3gKtFBz-aCka5MT715piIesekwYoA1JqaJLnwcqltkgszcqKPmC7EyFv08F7MsXixVYUaM_7MnG4cGVB124xpRGubJm74uvjEygWKa0Fp66gkabD3JUzpJHNc39KjjLMvT3bzxZ5uhmMo9tg9Di8i3qjIBFcmUBA1u0KpTJIMz1R3ErNVYaJEWiZwVCLUAqDKQJnCCEaVEqltcGoTKqJEC1yucudV-Xb0vpFPHM-qT_AwpZLH-uQh0bLbg3CDkyq0vvKZvG8cjOsNjGweNto_KfR2nOxD19OZjb9dewrrIHrHbB2ud38nxiP-_f9EETI68WIb3F4fus</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>67278649</pqid></control><display><type>article</type><title>Evidence for Na+/Ca2+ Exchanger 1 Association with Caveolin‐1 and ‐2 in C6 Glioma Cells</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Wiley Free Content</source><creator>Cha, Seok Ho ; Shin, Sun Young ; Jung, Sang Yong ; Kim, Yun Tai ; Park, Yong Joo ; Kwak, Jin‐Oh ; Kim, Hyun‐Woo ; Suh, Chang Kook</creator><creatorcontrib>Cha, Seok Ho ; Shin, Sun Young ; Jung, Sang Yong ; Kim, Yun Tai ; Park, Yong Joo ; Kwak, Jin‐Oh ; Kim, Hyun‐Woo ; Suh, Chang Kook</creatorcontrib><description>The purpose of this study is to understand the interaction of Na+‐Ca2+ exchanger (NCX1), that is one of the essential regulators of Ca2+ homeostasis, with caveolin (Cav)‐1 and Cav‐2 in Cav‐3 null cell (rat C6 glioma cell). Both mRNA and protein expression of NCX1, Cav‐1 and Cav‐2 was observed, but no expression of mRNA and protein of Cav‐3 were observed in C6 glioma cells. In isolated caveolae‐enriched membrane fraction, the NCX1, Cav‐1 and Cav‐2 proteins localized in same fractions. The experiment of immuno‐precipitation showed complex formation between the NCX1 and Cavs. Confocal microscopy also supported co‐localization of NCX1 and Cavs at the plasma membrane. Functionally, sodium‐free induced forward mode of NCX1 attenuated by Cav‐1 antisense ODN. When treated cells with Cav‐2 antisense ODN, both reverse and forward mode of NCX1 was attenuated. From these results, in the Cav‐3 lacking cells, the function of NCX1 might be regulated by binding with Cavs. Considering the decrement of NCX1 activity by antisense ODNs, caveolins may play an important role in diverse of pathophysiological process of NCX1‐related disorders in the body. IUBMB Life, 56: 621‐627, 2004</description><identifier>ISSN: 1521-6543</identifier><identifier>EISSN: 1521-6551</identifier><identifier>DOI: 10.1080/15216540400020353</identifier><identifier>PMID: 15814461</identifier><language>eng</language><publisher>UK: Informa Healthcare</publisher><subject>Animals ; Binding Sites ; Blotting, Western ; C6 glioma cells ; Calcium - metabolism ; Caveolae ; Caveolin (Cav) ; Caveolin 1 ; Caveolin 2 ; Caveolins - metabolism ; Cell Line, Tumor ; Cell Membrane - metabolism ; Humans ; Immunoprecipitation ; Immuno‐precipitaion (IP) ; Ions ; Microscopy, Confocal ; Na+‐Ca2+ exchanger (NCX) ; Oligonucleotides, Antisense - pharmacology ; Protein Binding ; Rats ; Reverse Transcriptase Polymerase Chain Reaction ; RNA, Messenger - metabolism ; Sodium - pharmacology ; Sodium-Calcium Exchanger - metabolism ; Time Factors</subject><ispartof>IUBMB life, 2004-10, Vol.56 (10), p.621-627</ispartof><rights>Copyright © 2004 International Union of Biochemistry and Molecular Biology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3258-31f99355f1df6b52e4625fac83ae08a7637438ada120a17a8a555d35585f45b33</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1080%2F15216540400020353$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1080%2F15216540400020353$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,1432,27922,27923,45572,45573,46407,46831</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15814461$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cha, Seok Ho</creatorcontrib><creatorcontrib>Shin, Sun Young</creatorcontrib><creatorcontrib>Jung, Sang Yong</creatorcontrib><creatorcontrib>Kim, Yun Tai</creatorcontrib><creatorcontrib>Park, Yong Joo</creatorcontrib><creatorcontrib>Kwak, Jin‐Oh</creatorcontrib><creatorcontrib>Kim, Hyun‐Woo</creatorcontrib><creatorcontrib>Suh, Chang Kook</creatorcontrib><title>Evidence for Na+/Ca2+ Exchanger 1 Association with Caveolin‐1 and ‐2 in C6 Glioma Cells</title><title>IUBMB life</title><addtitle>IUBMB Life</addtitle><description>The purpose of this study is to understand the interaction of Na+‐Ca2+ exchanger (NCX1), that is one of the essential regulators of Ca2+ homeostasis, with caveolin (Cav)‐1 and Cav‐2 in Cav‐3 null cell (rat C6 glioma cell). Both mRNA and protein expression of NCX1, Cav‐1 and Cav‐2 was observed, but no expression of mRNA and protein of Cav‐3 were observed in C6 glioma cells. In isolated caveolae‐enriched membrane fraction, the NCX1, Cav‐1 and Cav‐2 proteins localized in same fractions. The experiment of immuno‐precipitation showed complex formation between the NCX1 and Cavs. Confocal microscopy also supported co‐localization of NCX1 and Cavs at the plasma membrane. Functionally, sodium‐free induced forward mode of NCX1 attenuated by Cav‐1 antisense ODN. When treated cells with Cav‐2 antisense ODN, both reverse and forward mode of NCX1 was attenuated. From these results, in the Cav‐3 lacking cells, the function of NCX1 might be regulated by binding with Cavs. Considering the decrement of NCX1 activity by antisense ODNs, caveolins may play an important role in diverse of pathophysiological process of NCX1‐related disorders in the body. IUBMB Life, 56: 621‐627, 2004</description><subject>Animals</subject><subject>Binding Sites</subject><subject>Blotting, Western</subject><subject>C6 glioma cells</subject><subject>Calcium - metabolism</subject><subject>Caveolae</subject><subject>Caveolin (Cav)</subject><subject>Caveolin 1</subject><subject>Caveolin 2</subject><subject>Caveolins - metabolism</subject><subject>Cell Line, Tumor</subject><subject>Cell Membrane - metabolism</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>Immuno‐precipitaion (IP)</subject><subject>Ions</subject><subject>Microscopy, Confocal</subject><subject>Na+‐Ca2+ exchanger (NCX)</subject><subject>Oligonucleotides, Antisense - pharmacology</subject><subject>Protein Binding</subject><subject>Rats</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA, Messenger - metabolism</subject><subject>Sodium - pharmacology</subject><subject>Sodium-Calcium Exchanger - metabolism</subject><subject>Time Factors</subject><issn>1521-6543</issn><issn>1521-6551</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkD1Ow0AQhVcIRELgADRoK5rIZGf_vJFoEisEpABNqCisib0mixw7ePNDOo7AGTkJjhJBQUE1b0bfexo9Qs6BXQEzrAOKg1aSScYYZ0KJA9Lc3gKtFBz-aCka5MT715piIesekwYoA1JqaJLnwcqltkgszcqKPmC7EyFv08F7MsXixVYUaM_7MnG4cGVB124xpRGubJm74uvjEygWKa0Fp66gkabD3JUzpJHNc39KjjLMvT3bzxZ5uhmMo9tg9Di8i3qjIBFcmUBA1u0KpTJIMz1R3ErNVYaJEWiZwVCLUAqDKQJnCCEaVEqltcGoTKqJEC1yucudV-Xb0vpFPHM-qT_AwpZLH-uQh0bLbg3CDkyq0vvKZvG8cjOsNjGweNto_KfR2nOxD19OZjb9dewrrIHrHbB2ud38nxiP-_f9EETI68WIb3F4fus</recordid><startdate>200410</startdate><enddate>200410</enddate><creator>Cha, Seok Ho</creator><creator>Shin, Sun Young</creator><creator>Jung, Sang Yong</creator><creator>Kim, Yun Tai</creator><creator>Park, Yong Joo</creator><creator>Kwak, Jin‐Oh</creator><creator>Kim, Hyun‐Woo</creator><creator>Suh, Chang Kook</creator><general>Informa Healthcare</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>200410</creationdate><title>Evidence for Na+/Ca2+ Exchanger 1 Association with Caveolin‐1 and ‐2 in C6 Glioma Cells</title><author>Cha, Seok Ho ; Shin, Sun Young ; Jung, Sang Yong ; Kim, Yun Tai ; Park, Yong Joo ; Kwak, Jin‐Oh ; Kim, Hyun‐Woo ; Suh, Chang Kook</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3258-31f99355f1df6b52e4625fac83ae08a7637438ada120a17a8a555d35585f45b33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Binding Sites</topic><topic>Blotting, Western</topic><topic>C6 glioma cells</topic><topic>Calcium - metabolism</topic><topic>Caveolae</topic><topic>Caveolin (Cav)</topic><topic>Caveolin 1</topic><topic>Caveolin 2</topic><topic>Caveolins - metabolism</topic><topic>Cell Line, Tumor</topic><topic>Cell Membrane - metabolism</topic><topic>Humans</topic><topic>Immunoprecipitation</topic><topic>Immuno‐precipitaion (IP)</topic><topic>Ions</topic><topic>Microscopy, Confocal</topic><topic>Na+‐Ca2+ exchanger (NCX)</topic><topic>Oligonucleotides, Antisense - pharmacology</topic><topic>Protein Binding</topic><topic>Rats</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA, Messenger - metabolism</topic><topic>Sodium - pharmacology</topic><topic>Sodium-Calcium Exchanger - metabolism</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cha, Seok Ho</creatorcontrib><creatorcontrib>Shin, Sun Young</creatorcontrib><creatorcontrib>Jung, Sang Yong</creatorcontrib><creatorcontrib>Kim, Yun Tai</creatorcontrib><creatorcontrib>Park, Yong Joo</creatorcontrib><creatorcontrib>Kwak, Jin‐Oh</creatorcontrib><creatorcontrib>Kim, Hyun‐Woo</creatorcontrib><creatorcontrib>Suh, Chang Kook</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>IUBMB life</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cha, Seok Ho</au><au>Shin, Sun Young</au><au>Jung, Sang Yong</au><au>Kim, Yun Tai</au><au>Park, Yong Joo</au><au>Kwak, Jin‐Oh</au><au>Kim, Hyun‐Woo</au><au>Suh, Chang Kook</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence for Na+/Ca2+ Exchanger 1 Association with Caveolin‐1 and ‐2 in C6 Glioma Cells</atitle><jtitle>IUBMB life</jtitle><addtitle>IUBMB Life</addtitle><date>2004-10</date><risdate>2004</risdate><volume>56</volume><issue>10</issue><spage>621</spage><epage>627</epage><pages>621-627</pages><issn>1521-6543</issn><eissn>1521-6551</eissn><abstract>The purpose of this study is to understand the interaction of Na+‐Ca2+ exchanger (NCX1), that is one of the essential regulators of Ca2+ homeostasis, with caveolin (Cav)‐1 and Cav‐2 in Cav‐3 null cell (rat C6 glioma cell). Both mRNA and protein expression of NCX1, Cav‐1 and Cav‐2 was observed, but no expression of mRNA and protein of Cav‐3 were observed in C6 glioma cells. In isolated caveolae‐enriched membrane fraction, the NCX1, Cav‐1 and Cav‐2 proteins localized in same fractions. The experiment of immuno‐precipitation showed complex formation between the NCX1 and Cavs. Confocal microscopy also supported co‐localization of NCX1 and Cavs at the plasma membrane. Functionally, sodium‐free induced forward mode of NCX1 attenuated by Cav‐1 antisense ODN. When treated cells with Cav‐2 antisense ODN, both reverse and forward mode of NCX1 was attenuated. From these results, in the Cav‐3 lacking cells, the function of NCX1 might be regulated by binding with Cavs. Considering the decrement of NCX1 activity by antisense ODNs, caveolins may play an important role in diverse of pathophysiological process of NCX1‐related disorders in the body. IUBMB Life, 56: 621‐627, 2004</abstract><cop>UK</cop><pub>Informa Healthcare</pub><pmid>15814461</pmid><doi>10.1080/15216540400020353</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1521-6543
ispartof IUBMB life, 2004-10, Vol.56 (10), p.621-627
issn 1521-6543
1521-6551
language eng
recordid cdi_proquest_miscellaneous_67278649
source MEDLINE; Wiley Online Library Journals Frontfile Complete; Wiley Free Content
subjects Animals
Binding Sites
Blotting, Western
C6 glioma cells
Calcium - metabolism
Caveolae
Caveolin (Cav)
Caveolin 1
Caveolin 2
Caveolins - metabolism
Cell Line, Tumor
Cell Membrane - metabolism
Humans
Immunoprecipitation
Immuno‐precipitaion (IP)
Ions
Microscopy, Confocal
Na+‐Ca2+ exchanger (NCX)
Oligonucleotides, Antisense - pharmacology
Protein Binding
Rats
Reverse Transcriptase Polymerase Chain Reaction
RNA, Messenger - metabolism
Sodium - pharmacology
Sodium-Calcium Exchanger - metabolism
Time Factors
title Evidence for Na+/Ca2+ Exchanger 1 Association with Caveolin‐1 and ‐2 in C6 Glioma Cells
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-09T17%3A02%3A27IST&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=Evidence%20for%20Na+/Ca2+%20Exchanger%201%20Association%20with%20Caveolin%E2%80%901%20and%20%E2%80%902%20in%20C6%20Glioma%20Cells&rft.jtitle=IUBMB%20life&rft.au=Cha,%20Seok%20Ho&rft.date=2004-10&rft.volume=56&rft.issue=10&rft.spage=621&rft.epage=627&rft.pages=621-627&rft.issn=1521-6543&rft.eissn=1521-6551&rft_id=info:doi/10.1080/15216540400020353&rft_dat=%3Cproquest_cross%3E67278649%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=67278649&rft_id=info:pmid/15814461&rfr_iscdi=true