Trehalose transporter 1, a facilitated and high-capacity trehalose transporter, allows exogenous trehalose uptake into cells
Trehalose is potentially a useful cryo- or anhydroprotectant molecule for cells and biomolecules such as proteins and nucleotides. A major obstacle to application is that cellular membranes are impermeable to trehalose. In this study, we isolated and characterized the functions of a facilitated treh...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2007-07, Vol.104 (28), p.11585-11590 |
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| creator | Kikawada, Takahiro Saito, Ayako Kanamori, Yasushi Nakahara, Yuichi Iwata, Ken-ichi Tanaka, Daisuke Watanabe, Masahiko Okuda, Takashi |
| description | Trehalose is potentially a useful cryo- or anhydroprotectant molecule for cells and biomolecules such as proteins and nucleotides. A major obstacle to application is that cellular membranes are impermeable to trehalose. In this study, we isolated and characterized the functions of a facilitated trehalose transporter [trehalose transporter 1 (TRET1)] from an anhydrobiotic insect, Polypedilum vanderplanki. Tret1 cDNA encodes a 504-aa protein with 12 predicted transmembrane structures. Tret1 expression was induced by either desiccation or salinity stress. Expression was predominant in the fat body and occurred concomitantly with the accumulation of trehalose, indicating that TRET1 is involved in transporting trehalose synthesized in the fat body into the hemolymph. Functional expression of TRET1 in Xenopus oocytes showed that transport activity was stereochemically specific for trehalose and independent of extracellular pH (between 4.0 and 9.0) and electrochemical membrane potential. These results indicate that TRET1 is a trehalose-specific facilitated transporter and that the direction of transport is reversible depending on the concentration gradient of trehalose. The extraordinarily high values for apparent Km (>=100 mM) and Vmax (>=500 pmol/min per oocyte) for trehalose both indicate that TRET1 is a high-capacity transporter of trehalose. Furthermore, TRET1 was found to function in mammalian cells, suggesting that it confers trehalose permeability on cells, including those of vertebrates as well as insects. These characteristic features imply that TRET1 in combination with trehalose has high potential for basic and practical applications in vivo. |
| doi_str_mv | 10.1073/pnas.0702538104 |
| format | Article |
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A major obstacle to application is that cellular membranes are impermeable to trehalose. In this study, we isolated and characterized the functions of a facilitated trehalose transporter [trehalose transporter 1 (TRET1)] from an anhydrobiotic insect, Polypedilum vanderplanki. Tret1 cDNA encodes a 504-aa protein with 12 predicted transmembrane structures. Tret1 expression was induced by either desiccation or salinity stress. Expression was predominant in the fat body and occurred concomitantly with the accumulation of trehalose, indicating that TRET1 is involved in transporting trehalose synthesized in the fat body into the hemolymph. Functional expression of TRET1 in Xenopus oocytes showed that transport activity was stereochemically specific for trehalose and independent of extracellular pH (between 4.0 and 9.0) and electrochemical membrane potential. These results indicate that TRET1 is a trehalose-specific facilitated transporter and that the direction of transport is reversible depending on the concentration gradient of trehalose. The extraordinarily high values for apparent Km (>=100 mM) and Vmax (>=500 pmol/min per oocyte) for trehalose both indicate that TRET1 is a high-capacity transporter of trehalose. Furthermore, TRET1 was found to function in mammalian cells, suggesting that it confers trehalose permeability on cells, including those of vertebrates as well as insects. These characteristic features imply that TRET1 in combination with trehalose has high potential for basic and practical applications in vivo.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0702538104</identifier><identifier>PMID: 17606922</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>amino acid sequences ; Animals ; Biological Sciences ; Biological Transport, Active - physiology ; Carrier Proteins - physiology ; Cell Line, Tumor ; Cell Membrane Permeability - physiology ; Cell membranes ; Cells ; Chironomidae - chemistry ; Chironomidae - metabolism ; Chironomidae - physiology ; CHO Cells ; Complementary DNA ; Complementary RNA ; Cricetinae ; Cricetulus ; dehydration (animal physiology) ; Fat body ; Frogs ; Gene expression ; gene expression regulation ; Humans ; Larvae ; Membrane potential ; Mice ; Molecular Sequence Data ; Molecules ; NIH 3T3 Cells ; nucleotide sequences ; Oocytes ; physiological transport ; Polypedilum ; Polypedilum vanderplanki ; Proteins ; RNA ; salinity ; salt stress ; Studies ; Sugars ; transporters ; trehalose ; Trehalose - metabolism ; trehalose transporter 1 ; Xenopus</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2007-07, Vol.104 (28), p.11585-11590</ispartof><rights>Copyright 2007 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Jul 10, 2007</rights><rights>2007 by The National Academy of Sciences of the USA 2007</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c554t-f6d617b508a4a7f1e0cb47ef1410dfa7895cd8b564d408c6d21bad0338cfcb243</citedby><cites>FETCH-LOGICAL-c554t-f6d617b508a4a7f1e0cb47ef1410dfa7895cd8b564d408c6d21bad0338cfcb243</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/104/28.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/25436162$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/25436162$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17606922$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kikawada, Takahiro</creatorcontrib><creatorcontrib>Saito, Ayako</creatorcontrib><creatorcontrib>Kanamori, Yasushi</creatorcontrib><creatorcontrib>Nakahara, Yuichi</creatorcontrib><creatorcontrib>Iwata, Ken-ichi</creatorcontrib><creatorcontrib>Tanaka, Daisuke</creatorcontrib><creatorcontrib>Watanabe, Masahiko</creatorcontrib><creatorcontrib>Okuda, Takashi</creatorcontrib><title>Trehalose transporter 1, a facilitated and high-capacity trehalose transporter, allows exogenous trehalose uptake into cells</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Trehalose is potentially a useful cryo- or anhydroprotectant molecule for cells and biomolecules such as proteins and nucleotides. A major obstacle to application is that cellular membranes are impermeable to trehalose. In this study, we isolated and characterized the functions of a facilitated trehalose transporter [trehalose transporter 1 (TRET1)] from an anhydrobiotic insect, Polypedilum vanderplanki. Tret1 cDNA encodes a 504-aa protein with 12 predicted transmembrane structures. Tret1 expression was induced by either desiccation or salinity stress. Expression was predominant in the fat body and occurred concomitantly with the accumulation of trehalose, indicating that TRET1 is involved in transporting trehalose synthesized in the fat body into the hemolymph. Functional expression of TRET1 in Xenopus oocytes showed that transport activity was stereochemically specific for trehalose and independent of extracellular pH (between 4.0 and 9.0) and electrochemical membrane potential. These results indicate that TRET1 is a trehalose-specific facilitated transporter and that the direction of transport is reversible depending on the concentration gradient of trehalose. The extraordinarily high values for apparent Km (>=100 mM) and Vmax (>=500 pmol/min per oocyte) for trehalose both indicate that TRET1 is a high-capacity transporter of trehalose. Furthermore, TRET1 was found to function in mammalian cells, suggesting that it confers trehalose permeability on cells, including those of vertebrates as well as insects. These characteristic features imply that TRET1 in combination with trehalose has high potential for basic and practical applications in vivo.</description><subject>amino acid sequences</subject><subject>Animals</subject><subject>Biological Sciences</subject><subject>Biological Transport, Active - physiology</subject><subject>Carrier Proteins - physiology</subject><subject>Cell Line, Tumor</subject><subject>Cell Membrane Permeability - physiology</subject><subject>Cell membranes</subject><subject>Cells</subject><subject>Chironomidae - chemistry</subject><subject>Chironomidae - metabolism</subject><subject>Chironomidae - physiology</subject><subject>CHO Cells</subject><subject>Complementary DNA</subject><subject>Complementary RNA</subject><subject>Cricetinae</subject><subject>Cricetulus</subject><subject>dehydration (animal physiology)</subject><subject>Fat body</subject><subject>Frogs</subject><subject>Gene expression</subject><subject>gene expression regulation</subject><subject>Humans</subject><subject>Larvae</subject><subject>Membrane potential</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Molecules</subject><subject>NIH 3T3 Cells</subject><subject>nucleotide sequences</subject><subject>Oocytes</subject><subject>physiological transport</subject><subject>Polypedilum</subject><subject>Polypedilum vanderplanki</subject><subject>Proteins</subject><subject>RNA</subject><subject>salinity</subject><subject>salt stress</subject><subject>Studies</subject><subject>Sugars</subject><subject>transporters</subject><subject>trehalose</subject><subject>Trehalose - metabolism</subject><subject>trehalose transporter 1</subject><subject>Xenopus</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9rFDEcxQex2LV69qQGD0LBab_J5NdcBClqCwUPtueQySS7s85OpklGW_CPN8Mu3SpCT4F8P-_l-_KK4hWGEwyiOh0HHU9AAGGVxECfFAsMNS45reFpsQAgopSU0MPieYxrAKiZhGfFIRYceE3Iovh9FexK9z5alIIe4uhDsgHhD0gjp03Xd0kn2yI9tGjVLVel0WO-TncZ_48wy_re_4rI3vqlHfwUH3DTmPQPi7oheWRs38cXxYHTfbQvd-dRcf3l89XZeXn57evF2afL0jBGU-l4y7FoGEhNtXDYgmmosA5TDK3TQtbMtLJhnLYUpOEtwY1uoaqkcaYhtDoqPm59x6nZ2NbYIa_cqzF0Gx3ulNed-nsydCu19D8VroHVRGSD9zuD4G8mG5PadHGOoAebMyqRK5A1hkdBArxiNZAMvvsHXPspDPkXMoMrTIDWGTrdQib4GIN19ytjUHP_au5f7fvPijcPk-75XeEZON4Bs3JvRxWRCmMmmXJT3yd7mzKLHmEz8nqLrGPy4Z4hjFYc8_m5t9u5017pZeiiuv4-BwTItVHOqz_2hdpu</recordid><startdate>20070710</startdate><enddate>20070710</enddate><creator>Kikawada, Takahiro</creator><creator>Saito, Ayako</creator><creator>Kanamori, Yasushi</creator><creator>Nakahara, Yuichi</creator><creator>Iwata, Ken-ichi</creator><creator>Tanaka, Daisuke</creator><creator>Watanabe, Masahiko</creator><creator>Okuda, Takashi</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20070710</creationdate><title>Trehalose transporter 1, a facilitated and high-capacity trehalose transporter, allows exogenous trehalose uptake into cells</title><author>Kikawada, Takahiro ; 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A major obstacle to application is that cellular membranes are impermeable to trehalose. In this study, we isolated and characterized the functions of a facilitated trehalose transporter [trehalose transporter 1 (TRET1)] from an anhydrobiotic insect, Polypedilum vanderplanki. Tret1 cDNA encodes a 504-aa protein with 12 predicted transmembrane structures. Tret1 expression was induced by either desiccation or salinity stress. Expression was predominant in the fat body and occurred concomitantly with the accumulation of trehalose, indicating that TRET1 is involved in transporting trehalose synthesized in the fat body into the hemolymph. Functional expression of TRET1 in Xenopus oocytes showed that transport activity was stereochemically specific for trehalose and independent of extracellular pH (between 4.0 and 9.0) and electrochemical membrane potential. These results indicate that TRET1 is a trehalose-specific facilitated transporter and that the direction of transport is reversible depending on the concentration gradient of trehalose. The extraordinarily high values for apparent Km (>=100 mM) and Vmax (>=500 pmol/min per oocyte) for trehalose both indicate that TRET1 is a high-capacity transporter of trehalose. Furthermore, TRET1 was found to function in mammalian cells, suggesting that it confers trehalose permeability on cells, including those of vertebrates as well as insects. These characteristic features imply that TRET1 in combination with trehalose has high potential for basic and practical applications in vivo.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>17606922</pmid><doi>10.1073/pnas.0702538104</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | amino acid sequences Animals Biological Sciences Biological Transport, Active - physiology Carrier Proteins - physiology Cell Line, Tumor Cell Membrane Permeability - physiology Cell membranes Cells Chironomidae - chemistry Chironomidae - metabolism Chironomidae - physiology CHO Cells Complementary DNA Complementary RNA Cricetinae Cricetulus dehydration (animal physiology) Fat body Frogs Gene expression gene expression regulation Humans Larvae Membrane potential Mice Molecular Sequence Data Molecules NIH 3T3 Cells nucleotide sequences Oocytes physiological transport Polypedilum Polypedilum vanderplanki Proteins RNA salinity salt stress Studies Sugars transporters trehalose Trehalose - metabolism trehalose transporter 1 Xenopus |
| title | Trehalose transporter 1, a facilitated and high-capacity trehalose transporter, allows exogenous trehalose uptake into cells |
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