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Ribavirin uptake by cultured human choriocarcinoma (BeWo) cells and Xenopus laevis oocytes expressing recombinant plasma membrane human nucleoside transporters
We investigated the mechanism of the transport of ribavirin (1-β- d-ribofuranosyl-1,2,4-trizole-3-carboxamide) into placental epithelial cells using human choriocarcinoma (BeWo) cells and Xenopus oocytes expressing human nucleoside transporters. In BeWo cells, when a relatively low concentration (12...
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Published in: | European journal of pharmacology 2007-02, Vol.557 (1), p.1-8 |
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description | We investigated the mechanism of the transport of ribavirin (1-β-
d-ribofuranosyl-1,2,4-trizole-3-carboxamide) into placental epithelial cells using human choriocarcinoma (BeWo) cells and
Xenopus oocytes expressing human nucleoside transporters. In BeWo cells, when a relatively low concentration (123 nM) of ribavirin was used, both Na
+-dependent uptake and -independent uptake of ribavirin were observed. On the other hand, when a higher concentration (100 μM) of ribavirin was used, Na
+-independent uptake was observed, but there was only a slight Na
+-dependent uptake. In
Xenopus oocytes, influxes of ribavirin mediated by hCNT2 (concentrative nucleoside transporter 2), hCNT3 (concentrative nucleoside transporter 3), hENT1 (equilibrative nucleoside transporter 1) and hENT2 (equilibrative nucleoside transporter 2) were saturable, and apparent
K
m values were 18.0 μM, 14.2 μM, 3.46 mM and 3.71 mM, respectively. These data indicate that hCNT2 and hCNT3 have higher affinity for ribavirin than do hENT1 and hENT2. Moreover, analysis by RT-PCR showed that BeWo cells express mRNA of hCNT3, hENT1 and hENT2. These results suggest that ribavirin is taken up by BeWo cells via both the high-affinity Na
+-dependent transporter hCNT3 and the low-affinity Na
+-independent transporters hENT1 and hENT2. |
doi_str_mv | 10.1016/j.ejphar.2006.10.062 |
format | article |
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d-ribofuranosyl-1,2,4-trizole-3-carboxamide) into placental epithelial cells using human choriocarcinoma (BeWo) cells and
Xenopus oocytes expressing human nucleoside transporters. In BeWo cells, when a relatively low concentration (123 nM) of ribavirin was used, both Na
+-dependent uptake and -independent uptake of ribavirin were observed. On the other hand, when a higher concentration (100 μM) of ribavirin was used, Na
+-independent uptake was observed, but there was only a slight Na
+-dependent uptake. In
Xenopus oocytes, influxes of ribavirin mediated by hCNT2 (concentrative nucleoside transporter 2), hCNT3 (concentrative nucleoside transporter 3), hENT1 (equilibrative nucleoside transporter 1) and hENT2 (equilibrative nucleoside transporter 2) were saturable, and apparent
K
m values were 18.0 μM, 14.2 μM, 3.46 mM and 3.71 mM, respectively. These data indicate that hCNT2 and hCNT3 have higher affinity for ribavirin than do hENT1 and hENT2. Moreover, analysis by RT-PCR showed that BeWo cells express mRNA of hCNT3, hENT1 and hENT2. These results suggest that ribavirin is taken up by BeWo cells via both the high-affinity Na
+-dependent transporter hCNT3 and the low-affinity Na
+-independent transporters hENT1 and hENT2.</description><identifier>ISSN: 0014-2999</identifier><identifier>EISSN: 1879-0712</identifier><identifier>DOI: 10.1016/j.ejphar.2006.10.062</identifier><identifier>PMID: 17140564</identifier><identifier>CODEN: EJPHAZ</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>( Xenopus laevis) oocytes ; Animals ; Antiviral Agents - metabolism ; BeWo cells ; Biological and medical sciences ; Cell Line, Tumor ; Choriocarcinoma ; Concentrative nucleoside transporter ; Epithelial Cells - metabolism ; Equilibrative nucleoside transporter ; Humans ; Medical sciences ; Nucleoside Transport Proteins - genetics ; Nucleoside Transport Proteins - metabolism ; Oocytes - metabolism ; Pharmacology. Drug treatments ; Placenta - cytology ; Placenta - metabolism ; Recombinant Proteins - metabolism ; Ribavirin ; Ribavirin - metabolism ; RNA, Messenger - metabolism ; Sodium - metabolism ; Xenopus laevis</subject><ispartof>European journal of pharmacology, 2007-02, Vol.557 (1), p.1-8</ispartof><rights>2006 Elsevier B.V.</rights><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c456t-d3e15ae6a3e69b80cba65720521623565263640e8f3d6e91067c22d38757df723</citedby><cites>FETCH-LOGICAL-c456t-d3e15ae6a3e69b80cba65720521623565263640e8f3d6e91067c22d38757df723</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18479467$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17140564$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yamamoto, Takashi</creatorcontrib><creatorcontrib>Kuniki, Kenichi</creatorcontrib><creatorcontrib>Takekuma, Yoh</creatorcontrib><creatorcontrib>Hirano, Takeshi</creatorcontrib><creatorcontrib>Iseki, Ken</creatorcontrib><creatorcontrib>Sugawara, Mitsuru</creatorcontrib><title>Ribavirin uptake by cultured human choriocarcinoma (BeWo) cells and Xenopus laevis oocytes expressing recombinant plasma membrane human nucleoside transporters</title><title>European journal of pharmacology</title><addtitle>Eur J Pharmacol</addtitle><description>We investigated the mechanism of the transport of ribavirin (1-β-
d-ribofuranosyl-1,2,4-trizole-3-carboxamide) into placental epithelial cells using human choriocarcinoma (BeWo) cells and
Xenopus oocytes expressing human nucleoside transporters. In BeWo cells, when a relatively low concentration (123 nM) of ribavirin was used, both Na
+-dependent uptake and -independent uptake of ribavirin were observed. On the other hand, when a higher concentration (100 μM) of ribavirin was used, Na
+-independent uptake was observed, but there was only a slight Na
+-dependent uptake. In
Xenopus oocytes, influxes of ribavirin mediated by hCNT2 (concentrative nucleoside transporter 2), hCNT3 (concentrative nucleoside transporter 3), hENT1 (equilibrative nucleoside transporter 1) and hENT2 (equilibrative nucleoside transporter 2) were saturable, and apparent
K
m values were 18.0 μM, 14.2 μM, 3.46 mM and 3.71 mM, respectively. These data indicate that hCNT2 and hCNT3 have higher affinity for ribavirin than do hENT1 and hENT2. Moreover, analysis by RT-PCR showed that BeWo cells express mRNA of hCNT3, hENT1 and hENT2. These results suggest that ribavirin is taken up by BeWo cells via both the high-affinity Na
+-dependent transporter hCNT3 and the low-affinity Na
+-independent transporters hENT1 and hENT2.</description><subject>( Xenopus laevis) oocytes</subject><subject>Animals</subject><subject>Antiviral Agents - metabolism</subject><subject>BeWo cells</subject><subject>Biological and medical sciences</subject><subject>Cell Line, Tumor</subject><subject>Choriocarcinoma</subject><subject>Concentrative nucleoside transporter</subject><subject>Epithelial Cells - metabolism</subject><subject>Equilibrative nucleoside transporter</subject><subject>Humans</subject><subject>Medical sciences</subject><subject>Nucleoside Transport Proteins - genetics</subject><subject>Nucleoside Transport Proteins - metabolism</subject><subject>Oocytes - metabolism</subject><subject>Pharmacology. Drug treatments</subject><subject>Placenta - cytology</subject><subject>Placenta - metabolism</subject><subject>Recombinant Proteins - metabolism</subject><subject>Ribavirin</subject><subject>Ribavirin - metabolism</subject><subject>RNA, Messenger - metabolism</subject><subject>Sodium - metabolism</subject><subject>Xenopus laevis</subject><issn>0014-2999</issn><issn>1879-0712</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNp9kV-L1DAUxYMo7rj6DUTyoqwPHZO0TZsXQRf_wYIgir6FNLl1MrZJN7cddj6NX9UMU9g3nwKH3z259xxCnnO25YzLN_st7KedSVvBmMzSlknxgGx426iCNVw8JBvGeFUIpdQFeYK4Z4zVStSPyQVveMVqWW3I32--MweffKDLNJs_QLsjtcswLwkc3S2jCdTuYvLRmmR9iKOhV-_hZ3xNLQwDUhMc_QUhTgvSwcDBI43RHmdACndTAkQfftMENo6dDybMdBoMZpcRxi6ZAOsnYbEDRPQO6JxlnGKaIeFT8qg3A8Kz9b0kPz5--H79ubj5-unL9bubwla1nAtXAq8NSFOCVF3LbGdk3QhWCy5FWctayFJWDNq-dBIUZ7KxQriyberG9Y0oL8mrs--U4u0COOvR4-nCvGFcUMtWVUqWKoPVGbQpIibo9ZT8aNJRc6ZPxei9PhejT8Wc1FxMHnux-i_dCO5-aG0iAy9XwKA1Q58zsB7vubZqVCWbzL09c5DTOHhIGq2HYMH5HPKsXfT_3-Qf9_ixWg</recordid><startdate>20070214</startdate><enddate>20070214</enddate><creator>Yamamoto, Takashi</creator><creator>Kuniki, Kenichi</creator><creator>Takekuma, Yoh</creator><creator>Hirano, Takeshi</creator><creator>Iseki, Ken</creator><creator>Sugawara, Mitsuru</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>IQODW</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>20070214</creationdate><title>Ribavirin uptake by cultured human choriocarcinoma (BeWo) cells and Xenopus laevis oocytes expressing recombinant plasma membrane human nucleoside transporters</title><author>Yamamoto, Takashi ; Kuniki, Kenichi ; Takekuma, Yoh ; Hirano, Takeshi ; Iseki, Ken ; Sugawara, Mitsuru</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-d3e15ae6a3e69b80cba65720521623565263640e8f3d6e91067c22d38757df723</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>( Xenopus laevis) oocytes</topic><topic>Animals</topic><topic>Antiviral Agents - metabolism</topic><topic>BeWo cells</topic><topic>Biological and medical sciences</topic><topic>Cell Line, Tumor</topic><topic>Choriocarcinoma</topic><topic>Concentrative nucleoside transporter</topic><topic>Epithelial Cells - metabolism</topic><topic>Equilibrative nucleoside transporter</topic><topic>Humans</topic><topic>Medical sciences</topic><topic>Nucleoside Transport Proteins - genetics</topic><topic>Nucleoside Transport Proteins - metabolism</topic><topic>Oocytes - metabolism</topic><topic>Pharmacology. Drug treatments</topic><topic>Placenta - cytology</topic><topic>Placenta - metabolism</topic><topic>Recombinant Proteins - metabolism</topic><topic>Ribavirin</topic><topic>Ribavirin - metabolism</topic><topic>RNA, Messenger - metabolism</topic><topic>Sodium - metabolism</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yamamoto, Takashi</creatorcontrib><creatorcontrib>Kuniki, Kenichi</creatorcontrib><creatorcontrib>Takekuma, Yoh</creatorcontrib><creatorcontrib>Hirano, Takeshi</creatorcontrib><creatorcontrib>Iseki, Ken</creatorcontrib><creatorcontrib>Sugawara, Mitsuru</creatorcontrib><collection>Pascal-Francis</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>European journal of pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yamamoto, Takashi</au><au>Kuniki, Kenichi</au><au>Takekuma, Yoh</au><au>Hirano, Takeshi</au><au>Iseki, Ken</au><au>Sugawara, Mitsuru</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ribavirin uptake by cultured human choriocarcinoma (BeWo) cells and Xenopus laevis oocytes expressing recombinant plasma membrane human nucleoside transporters</atitle><jtitle>European journal of pharmacology</jtitle><addtitle>Eur J Pharmacol</addtitle><date>2007-02-14</date><risdate>2007</risdate><volume>557</volume><issue>1</issue><spage>1</spage><epage>8</epage><pages>1-8</pages><issn>0014-2999</issn><eissn>1879-0712</eissn><coden>EJPHAZ</coden><abstract>We investigated the mechanism of the transport of ribavirin (1-β-
d-ribofuranosyl-1,2,4-trizole-3-carboxamide) into placental epithelial cells using human choriocarcinoma (BeWo) cells and
Xenopus oocytes expressing human nucleoside transporters. In BeWo cells, when a relatively low concentration (123 nM) of ribavirin was used, both Na
+-dependent uptake and -independent uptake of ribavirin were observed. On the other hand, when a higher concentration (100 μM) of ribavirin was used, Na
+-independent uptake was observed, but there was only a slight Na
+-dependent uptake. In
Xenopus oocytes, influxes of ribavirin mediated by hCNT2 (concentrative nucleoside transporter 2), hCNT3 (concentrative nucleoside transporter 3), hENT1 (equilibrative nucleoside transporter 1) and hENT2 (equilibrative nucleoside transporter 2) were saturable, and apparent
K
m values were 18.0 μM, 14.2 μM, 3.46 mM and 3.71 mM, respectively. These data indicate that hCNT2 and hCNT3 have higher affinity for ribavirin than do hENT1 and hENT2. Moreover, analysis by RT-PCR showed that BeWo cells express mRNA of hCNT3, hENT1 and hENT2. These results suggest that ribavirin is taken up by BeWo cells via both the high-affinity Na
+-dependent transporter hCNT3 and the low-affinity Na
+-independent transporters hENT1 and hENT2.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>17140564</pmid><doi>10.1016/j.ejphar.2006.10.062</doi><tpages>8</tpages></addata></record> |
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subjects | ( Xenopus laevis) oocytes Animals Antiviral Agents - metabolism BeWo cells Biological and medical sciences Cell Line, Tumor Choriocarcinoma Concentrative nucleoside transporter Epithelial Cells - metabolism Equilibrative nucleoside transporter Humans Medical sciences Nucleoside Transport Proteins - genetics Nucleoside Transport Proteins - metabolism Oocytes - metabolism Pharmacology. Drug treatments Placenta - cytology Placenta - metabolism Recombinant Proteins - metabolism Ribavirin Ribavirin - metabolism RNA, Messenger - metabolism Sodium - metabolism Xenopus laevis |
title | Ribavirin uptake by cultured human choriocarcinoma (BeWo) cells and Xenopus laevis oocytes expressing recombinant plasma membrane human nucleoside transporters |
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