Identification and Functional Characterization of Rat Riboflavin Transporter 2
We have newly identified rat riboflavin transporter 2 (rRFT2) and its human orthologue (hRFT2), and carried out detailed functional characterization of rRFT2. The mRNA of rRFT2 was highly expressed in jejunum and ileum. When transiently expressed in human embryonic kidney (HEK) 293 cells, rRFT2 coul...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 2009-04, Vol.145 (4), p.437-443 |
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| container_title | Journal of biochemistry (Tokyo) |
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| creator | Yamamoto, Syunsuke Inoue, Katsuhisa Ohta, Kin-ya Fukatsu, Rui Maeda, Jun-ya Yoshida, Yukihiro Yuasa, Hiroaki |
| description | We have newly identified rat riboflavin transporter 2 (rRFT2) and its human orthologue (hRFT2), and carried out detailed functional characterization of rRFT2. The mRNA of rRFT2 was highly expressed in jejunum and ileum. When transiently expressed in human embryonic kidney (HEK) 293 cells, rRFT2 could transport riboflavin efficiently. Riboflavin transport mediated by rRFT2 was Na⁺-independent but moderately pH-sensitive, being more efficient in acidic conditions than in neutral and basic conditions. Kinetic analysis indicated that rRFT2-mediated riboflavin transport was saturable with a Michaelis constant (Km) of 0.21 μM. Furthermore, it was specifically and strongly inhibited by lumiflavin, flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), and to a lesser extent by amiloride. Such ability to transport riboflavin in a specific manner, together with its high expression in the small intestine, indicates that RFT2 may play a role in the intestinal absorption of riboflavin. |
| doi_str_mv | 10.1093/jb/mvn181 |
| format | Article |
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The mRNA of rRFT2 was highly expressed in jejunum and ileum. When transiently expressed in human embryonic kidney (HEK) 293 cells, rRFT2 could transport riboflavin efficiently. Riboflavin transport mediated by rRFT2 was Na⁺-independent but moderately pH-sensitive, being more efficient in acidic conditions than in neutral and basic conditions. Kinetic analysis indicated that rRFT2-mediated riboflavin transport was saturable with a Michaelis constant (Km) of 0.21 μM. Furthermore, it was specifically and strongly inhibited by lumiflavin, flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), and to a lesser extent by amiloride. Such ability to transport riboflavin in a specific manner, together with its high expression in the small intestine, indicates that RFT2 may play a role in the intestinal absorption of riboflavin.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/jb/mvn181</identifier><identifier>PMID: 19122205</identifier><language>eng</language><publisher>England: Japanese Biochemical Society</publisher><subject>absorption ; Amino Acid Sequence ; Animals ; Cell Line ; Gene Expression Profiling ; Gene Expression Regulation ; Green Fluorescent Proteins - metabolism ; Humans ; intestine ; Membrane Transport Proteins - chemistry ; Membrane Transport Proteins - genetics ; Membrane Transport Proteins - metabolism ; Molecular Sequence Data ; Rats ; Recombinant Fusion Proteins - metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; RFT2 ; riboflavin ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; Substrate Specificity ; transporter</subject><ispartof>Journal of biochemistry (Tokyo), 2009-04, Vol.145 (4), p.437-443</ispartof><rights>The Authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved 2009</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c490t-900a855e4d934878b3c78d28a5a761d93463e3117f07a7d3e8670d5904c107653</citedby><cites>FETCH-LOGICAL-c490t-900a855e4d934878b3c78d28a5a761d93463e3117f07a7d3e8670d5904c107653</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1578,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19122205$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yamamoto, Syunsuke</creatorcontrib><creatorcontrib>Inoue, Katsuhisa</creatorcontrib><creatorcontrib>Ohta, Kin-ya</creatorcontrib><creatorcontrib>Fukatsu, Rui</creatorcontrib><creatorcontrib>Maeda, Jun-ya</creatorcontrib><creatorcontrib>Yoshida, Yukihiro</creatorcontrib><creatorcontrib>Yuasa, Hiroaki</creatorcontrib><title>Identification and Functional Characterization of Rat Riboflavin Transporter 2</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>We have newly identified rat riboflavin transporter 2 (rRFT2) and its human orthologue (hRFT2), and carried out detailed functional characterization of rRFT2. The mRNA of rRFT2 was highly expressed in jejunum and ileum. When transiently expressed in human embryonic kidney (HEK) 293 cells, rRFT2 could transport riboflavin efficiently. Riboflavin transport mediated by rRFT2 was Na⁺-independent but moderately pH-sensitive, being more efficient in acidic conditions than in neutral and basic conditions. Kinetic analysis indicated that rRFT2-mediated riboflavin transport was saturable with a Michaelis constant (Km) of 0.21 μM. Furthermore, it was specifically and strongly inhibited by lumiflavin, flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), and to a lesser extent by amiloride. Such ability to transport riboflavin in a specific manner, together with its high expression in the small intestine, indicates that RFT2 may play a role in the intestinal absorption of riboflavin.</description><subject>absorption</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Cell Line</subject><subject>Gene Expression Profiling</subject><subject>Gene Expression Regulation</subject><subject>Green Fluorescent Proteins - metabolism</subject><subject>Humans</subject><subject>intestine</subject><subject>Membrane Transport Proteins - chemistry</subject><subject>Membrane Transport Proteins - genetics</subject><subject>Membrane Transport Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Rats</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RFT2</subject><subject>riboflavin</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>Substrate Specificity</subject><subject>transporter</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90E1P3DAQBmALFcEWOPQPtDkgpB4CM3YcJ0e0goK0AonPFRdrkjjgbTZe7ARBfz1ZZdXeerLGfvTK8zL2DeEYIRcni-Jk-dZihltsgkqmMU8lfmETAI5xzpP5LvsawmI9ciF22C7myDkHOWFXl5VpO1vbkjrr2ojaKjrv23I9UBNNX8hT2Rlv_4zvro5uqItubOHqht5sG915asPK-QFFfJ9t19QEc7A599j9-dnd9CKeXf-6nJ7O4jLJoYtzAMqkNEmViyRTWSFKlVU8I0kqxfVlKoxAVDUoUpUwWaqgkjkkJYJKpdhjR2PuyrvX3oROL20oTdNQa1wfdKoQU8zEAH-OsPQuBG9qvfJ2Sf5DI-h1eXpR6LG8wX7fhPbF0lT_5KatARyOwPWr_-bEI7OhM-9_Ifnfw7-Ekvpi_qTh8YEnjzDXs8H_GH1NTtOzt0Hf33JAAcMOQvJcfAJrp44h</recordid><startdate>20090401</startdate><enddate>20090401</enddate><creator>Yamamoto, Syunsuke</creator><creator>Inoue, Katsuhisa</creator><creator>Ohta, Kin-ya</creator><creator>Fukatsu, Rui</creator><creator>Maeda, Jun-ya</creator><creator>Yoshida, Yukihiro</creator><creator>Yuasa, Hiroaki</creator><general>Japanese Biochemical Society</general><general>Oxford University Press</general><scope>FBQ</scope><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>20090401</creationdate><title>Identification and Functional Characterization of Rat Riboflavin Transporter 2</title><author>Yamamoto, Syunsuke ; Inoue, Katsuhisa ; Ohta, Kin-ya ; Fukatsu, Rui ; Maeda, Jun-ya ; Yoshida, Yukihiro ; Yuasa, Hiroaki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c490t-900a855e4d934878b3c78d28a5a761d93463e3117f07a7d3e8670d5904c107653</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>absorption</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Cell Line</topic><topic>Gene Expression Profiling</topic><topic>Gene Expression Regulation</topic><topic>Green Fluorescent Proteins - metabolism</topic><topic>Humans</topic><topic>intestine</topic><topic>Membrane Transport Proteins - chemistry</topic><topic>Membrane Transport Proteins - genetics</topic><topic>Membrane Transport Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Rats</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RFT2</topic><topic>riboflavin</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>Substrate Specificity</topic><topic>transporter</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yamamoto, Syunsuke</creatorcontrib><creatorcontrib>Inoue, Katsuhisa</creatorcontrib><creatorcontrib>Ohta, Kin-ya</creatorcontrib><creatorcontrib>Fukatsu, Rui</creatorcontrib><creatorcontrib>Maeda, Jun-ya</creatorcontrib><creatorcontrib>Yoshida, Yukihiro</creatorcontrib><creatorcontrib>Yuasa, Hiroaki</creatorcontrib><collection>AGRIS</collection><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>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yamamoto, Syunsuke</au><au>Inoue, Katsuhisa</au><au>Ohta, Kin-ya</au><au>Fukatsu, Rui</au><au>Maeda, Jun-ya</au><au>Yoshida, Yukihiro</au><au>Yuasa, Hiroaki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and Functional Characterization of Rat Riboflavin Transporter 2</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>2009-04-01</date><risdate>2009</risdate><volume>145</volume><issue>4</issue><spage>437</spage><epage>443</epage><pages>437-443</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><abstract>We have newly identified rat riboflavin transporter 2 (rRFT2) and its human orthologue (hRFT2), and carried out detailed functional characterization of rRFT2. The mRNA of rRFT2 was highly expressed in jejunum and ileum. When transiently expressed in human embryonic kidney (HEK) 293 cells, rRFT2 could transport riboflavin efficiently. Riboflavin transport mediated by rRFT2 was Na⁺-independent but moderately pH-sensitive, being more efficient in acidic conditions than in neutral and basic conditions. Kinetic analysis indicated that rRFT2-mediated riboflavin transport was saturable with a Michaelis constant (Km) of 0.21 μM. Furthermore, it was specifically and strongly inhibited by lumiflavin, flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), and to a lesser extent by amiloride. Such ability to transport riboflavin in a specific manner, together with its high expression in the small intestine, indicates that RFT2 may play a role in the intestinal absorption of riboflavin.</abstract><cop>England</cop><pub>Japanese Biochemical Society</pub><pmid>19122205</pmid><doi>10.1093/jb/mvn181</doi><tpages>7</tpages></addata></record> |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Alma/SFX Local Collection |
| subjects | absorption Amino Acid Sequence Animals Cell Line Gene Expression Profiling Gene Expression Regulation Green Fluorescent Proteins - metabolism Humans intestine Membrane Transport Proteins - chemistry Membrane Transport Proteins - genetics Membrane Transport Proteins - metabolism Molecular Sequence Data Rats Recombinant Fusion Proteins - metabolism Reverse Transcriptase Polymerase Chain Reaction RFT2 riboflavin RNA, Messenger - genetics RNA, Messenger - metabolism Substrate Specificity transporter |
| title | Identification and Functional Characterization of Rat Riboflavin Transporter 2 |
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