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The novel putative bile acid transporter SLC10A5 is highly expressed in liver and kidney
Here we report the identification, cloning, and characterization of SLC10A5, which is a new member of Solute Carrier Family 10 (SLC10), also known as the “sodium/bile acid cotransporter family”. Expression of SLC10A5/Slc10a5 was examined by quantitative real-time PCR and revealed its highest express...
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Published in: | Biochemical and biophysical research communications 2007-09, Vol.361 (1), p.26-32 |
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container_title | Biochemical and biophysical research communications |
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creator | Fernandes, Carla F. Godoy, José R. Döring, Barbara Cavalcanti, Marcia C.O. Bergmann, Martin Petzinger, Ernst Geyer, Joachim |
description | Here we report the identification, cloning, and characterization of SLC10A5, which is a new member of Solute Carrier Family 10 (SLC10), also known as the “sodium/bile acid cotransporter family”. Expression of SLC10A5/Slc10a5 was examined by quantitative real-time PCR and revealed its highest expression levels in liver and kidney in humans, rat and mouse. In rat liver and kidney, Slc10a5 expression was localized by
in situ hybridization to hepatocytes and proximal tubules, respectively. A SLC10A5-FLAG fusion protein was expressed in HEK293 cells and showed an apparent molecular weight of 42
kDa after immunoprecipitation. When expressed in
Xenopus laevis oocytes, the SLC10A5-FLAG protein was detected in the oocyte’s plasma membrane but showed no transport activity for taurocholate, cholate, estrone-3-sulfate, or dehydroepiandrosterone sulfate. As bile acid carriers are the most related carriers to SLC10A5 though, we strongly suppose that SLC10A5 is an orphan carrier with yet non-identified substrates. |
doi_str_mv | 10.1016/j.bbrc.2007.06.160 |
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in situ hybridization to hepatocytes and proximal tubules, respectively. A SLC10A5-FLAG fusion protein was expressed in HEK293 cells and showed an apparent molecular weight of 42
kDa after immunoprecipitation. When expressed in
Xenopus laevis oocytes, the SLC10A5-FLAG protein was detected in the oocyte’s plasma membrane but showed no transport activity for taurocholate, cholate, estrone-3-sulfate, or dehydroepiandrosterone sulfate. As bile acid carriers are the most related carriers to SLC10A5 though, we strongly suppose that SLC10A5 is an orphan carrier with yet non-identified substrates.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2007.06.160</identifier><identifier>PMID: 17632081</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>60 APPLIED LIFE SCIENCES ; Amino Acid Sequence ; Animals ; Bile acid transport ; BILE ACIDS ; CARRIERS ; Cloning, Molecular ; ESTRONE ; Gene Expression ; Humans ; HYDROXYANDROSTENONE ; IN-SITU HYBRIDIZATION ; Kidney - metabolism ; LIVER ; Liver - metabolism ; LIVER CELLS ; MICE ; Molecular Sequence Data ; NTCP ; OOCYTES ; Oocytes - metabolism ; Organic Anion Transporters, Sodium-Dependent - chemistry ; Organic Anion Transporters, Sodium-Dependent - genetics ; Organic Anion Transporters, Sodium-Dependent - metabolism ; POLYMERASE CHAIN REACTION ; PROTEINS ; Proximal tubules ; RATS ; SLC10 ; SLC10A5 ; SULFATES ; Symporters - chemistry ; Symporters - genetics ; Symporters - metabolism ; TUBULES ; Xenopus laevis</subject><ispartof>Biochemical and biophysical research communications, 2007-09, Vol.361 (1), p.26-32</ispartof><rights>2007 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c413t-fe58dfd2d109ad9a6e0ef88cad67a203f2d10bb499da9eb6f67f828e48cfa47a3</citedby><cites>FETCH-LOGICAL-c413t-fe58dfd2d109ad9a6e0ef88cad67a203f2d10bb499da9eb6f67f828e48cfa47a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17632081$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/20991526$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Fernandes, Carla F.</creatorcontrib><creatorcontrib>Godoy, José R.</creatorcontrib><creatorcontrib>Döring, Barbara</creatorcontrib><creatorcontrib>Cavalcanti, Marcia C.O.</creatorcontrib><creatorcontrib>Bergmann, Martin</creatorcontrib><creatorcontrib>Petzinger, Ernst</creatorcontrib><creatorcontrib>Geyer, Joachim</creatorcontrib><title>The novel putative bile acid transporter SLC10A5 is highly expressed in liver and kidney</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Here we report the identification, cloning, and characterization of SLC10A5, which is a new member of Solute Carrier Family 10 (SLC10), also known as the “sodium/bile acid cotransporter family”. Expression of SLC10A5/Slc10a5 was examined by quantitative real-time PCR and revealed its highest expression levels in liver and kidney in humans, rat and mouse. In rat liver and kidney, Slc10a5 expression was localized by
in situ hybridization to hepatocytes and proximal tubules, respectively. A SLC10A5-FLAG fusion protein was expressed in HEK293 cells and showed an apparent molecular weight of 42
kDa after immunoprecipitation. When expressed in
Xenopus laevis oocytes, the SLC10A5-FLAG protein was detected in the oocyte’s plasma membrane but showed no transport activity for taurocholate, cholate, estrone-3-sulfate, or dehydroepiandrosterone sulfate. 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Godoy, José R. ; Döring, Barbara ; Cavalcanti, Marcia C.O. ; Bergmann, Martin ; Petzinger, Ernst ; Geyer, Joachim</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c413t-fe58dfd2d109ad9a6e0ef88cad67a203f2d10bb499da9eb6f67f828e48cfa47a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Bile acid transport</topic><topic>BILE ACIDS</topic><topic>CARRIERS</topic><topic>Cloning, Molecular</topic><topic>ESTRONE</topic><topic>Gene Expression</topic><topic>Humans</topic><topic>HYDROXYANDROSTENONE</topic><topic>IN-SITU HYBRIDIZATION</topic><topic>Kidney - metabolism</topic><topic>LIVER</topic><topic>Liver - metabolism</topic><topic>LIVER CELLS</topic><topic>MICE</topic><topic>Molecular Sequence Data</topic><topic>NTCP</topic><topic>OOCYTES</topic><topic>Oocytes - metabolism</topic><topic>Organic Anion Transporters, Sodium-Dependent - chemistry</topic><topic>Organic Anion Transporters, Sodium-Dependent - genetics</topic><topic>Organic Anion Transporters, Sodium-Dependent - metabolism</topic><topic>POLYMERASE CHAIN REACTION</topic><topic>PROTEINS</topic><topic>Proximal tubules</topic><topic>RATS</topic><topic>SLC10</topic><topic>SLC10A5</topic><topic>SULFATES</topic><topic>Symporters - chemistry</topic><topic>Symporters - genetics</topic><topic>Symporters - metabolism</topic><topic>TUBULES</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fernandes, Carla F.</creatorcontrib><creatorcontrib>Godoy, José R.</creatorcontrib><creatorcontrib>Döring, Barbara</creatorcontrib><creatorcontrib>Cavalcanti, Marcia C.O.</creatorcontrib><creatorcontrib>Bergmann, Martin</creatorcontrib><creatorcontrib>Petzinger, Ernst</creatorcontrib><creatorcontrib>Geyer, Joachim</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fernandes, Carla F.</au><au>Godoy, José R.</au><au>Döring, Barbara</au><au>Cavalcanti, Marcia C.O.</au><au>Bergmann, Martin</au><au>Petzinger, Ernst</au><au>Geyer, Joachim</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The novel putative bile acid transporter SLC10A5 is highly expressed in liver and kidney</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2007-09-14</date><risdate>2007</risdate><volume>361</volume><issue>1</issue><spage>26</spage><epage>32</epage><pages>26-32</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Here we report the identification, cloning, and characterization of SLC10A5, which is a new member of Solute Carrier Family 10 (SLC10), also known as the “sodium/bile acid cotransporter family”. Expression of SLC10A5/Slc10a5 was examined by quantitative real-time PCR and revealed its highest expression levels in liver and kidney in humans, rat and mouse. In rat liver and kidney, Slc10a5 expression was localized by
in situ hybridization to hepatocytes and proximal tubules, respectively. A SLC10A5-FLAG fusion protein was expressed in HEK293 cells and showed an apparent molecular weight of 42
kDa after immunoprecipitation. When expressed in
Xenopus laevis oocytes, the SLC10A5-FLAG protein was detected in the oocyte’s plasma membrane but showed no transport activity for taurocholate, cholate, estrone-3-sulfate, or dehydroepiandrosterone sulfate. As bile acid carriers are the most related carriers to SLC10A5 though, we strongly suppose that SLC10A5 is an orphan carrier with yet non-identified substrates.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17632081</pmid><doi>10.1016/j.bbrc.2007.06.160</doi><tpages>7</tpages></addata></record> |
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source | ScienceDirect Freedom Collection |
subjects | 60 APPLIED LIFE SCIENCES Amino Acid Sequence Animals Bile acid transport BILE ACIDS CARRIERS Cloning, Molecular ESTRONE Gene Expression Humans HYDROXYANDROSTENONE IN-SITU HYBRIDIZATION Kidney - metabolism LIVER Liver - metabolism LIVER CELLS MICE Molecular Sequence Data NTCP OOCYTES Oocytes - metabolism Organic Anion Transporters, Sodium-Dependent - chemistry Organic Anion Transporters, Sodium-Dependent - genetics Organic Anion Transporters, Sodium-Dependent - metabolism POLYMERASE CHAIN REACTION PROTEINS Proximal tubules RATS SLC10 SLC10A5 SULFATES Symporters - chemistry Symporters - genetics Symporters - metabolism TUBULES Xenopus laevis |
title | The novel putative bile acid transporter SLC10A5 is highly expressed in liver and kidney |
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