Oligomeric structure of a renal cystine transporter: implications in cystinuria
Homologous proteins (NBAT) which mediate sodium-independent transport of neutral as well as basic amino acids and cystine when expressed in Xenopus oocytes were recently cloned from mammalian kidneys. Mutations in human NBAT have been implicated in cystinuria. Here, we show that rat kidney and jejun...
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Veröffentlicht in: | FEBS letters 1995-07, Vol.368 (2), p.389-392 |
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description | Homologous proteins (NBAT) which mediate sodium-independent transport of neutral as well as basic amino acids and cystine when expressed in
Xenopus oocytes were recently cloned from mammalian kidneys. Mutations in human NBAT have been implicated in cystinuria. Here, we show that rat kidney and jejunal brush border membrane NBAT (85 kDa) is found in association with a 50 kDa protein. The association involves one or more interprotein disulfide bonds. Rabbit kidney brush border membranes and membranes of NBAT cRNA-injected
Xenopus oocytes also contain such heterodimers. Our data suggest that the heterodimer is the minimal functional unit of NBAT-mediated amino acid transport and that the NBAT-associated 50 kDa protein could play a role in cystinuria. |
doi_str_mv | 10.1016/0014-5793(95)00685-3 |
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Xenopus oocytes were recently cloned from mammalian kidneys. Mutations in human NBAT have been implicated in cystinuria. Here, we show that rat kidney and jejunal brush border membrane NBAT (85 kDa) is found in association with a 50 kDa protein. The association involves one or more interprotein disulfide bonds. Rabbit kidney brush border membranes and membranes of NBAT cRNA-injected
Xenopus oocytes also contain such heterodimers. Our data suggest that the heterodimer is the minimal functional unit of NBAT-mediated amino acid transport and that the NBAT-associated 50 kDa protein could play a role in cystinuria.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(95)00685-3</identifier><identifier>PMID: 7628645</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>2-mercaptoethanol ; Amino acid transport ; Amino Acid Transport Systems, Basic ; Amino Acid Transport Systems, Neutral ; Animals ; BBM ; Biological Transport, Active ; Blotting, Western ; brush border membrane ; Carrier Proteins - analysis ; Carrier Proteins - chemistry ; Carrier Proteins - metabolism ; Cross-Linking Reagents ; Cystine - metabolism ; Cystinuria ; Cystinuria - metabolism ; Dimethyl Suberimidate ; dimethylsuberimidate ; DMS ; Humans ; IgG ; immunoglobulin ; Jejunum - chemistry ; Kidney ; Kidney - chemistry ; Kidney - metabolism ; membrane-spanning domain ; Microvilli - chemistry ; Molecular Weight ; MSD ; MSH ; N-ethylmaleimide ; NBAT ; NEM ; neutral and basic amino acid transporter ; Oocyte ; Oocytes ; Protein Conformation ; Rabbits ; Rats ; RNA, Complementary ; SDS-PAGE ; sodium dodecylsulfate/polyacrylamide gel electrophoresis ; Xenopus laevis</subject><ispartof>FEBS letters, 1995-07, Vol.368 (2), p.389-392</ispartof><rights>1995</rights><rights>FEBS Letters 368 (1995) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4973-156fca79522529f7c5e6d57c2c726c79b167d55f3525592c0cbb0dced56c9b543</citedby><cites>FETCH-LOGICAL-c4973-156fca79522529f7c5e6d57c2c726c79b167d55f3525592c0cbb0dced56c9b543</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(95)00685-3$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7628645$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Yan</creatorcontrib><creatorcontrib>Tate, Suresh S.</creatorcontrib><title>Oligomeric structure of a renal cystine transporter: implications in cystinuria</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Homologous proteins (NBAT) which mediate sodium-independent transport of neutral as well as basic amino acids and cystine when expressed in
Xenopus oocytes were recently cloned from mammalian kidneys. Mutations in human NBAT have been implicated in cystinuria. Here, we show that rat kidney and jejunal brush border membrane NBAT (85 kDa) is found in association with a 50 kDa protein. The association involves one or more interprotein disulfide bonds. Rabbit kidney brush border membranes and membranes of NBAT cRNA-injected
Xenopus oocytes also contain such heterodimers. Our data suggest that the heterodimer is the minimal functional unit of NBAT-mediated amino acid transport and that the NBAT-associated 50 kDa protein could play a role in cystinuria.</description><subject>2-mercaptoethanol</subject><subject>Amino acid transport</subject><subject>Amino Acid Transport Systems, Basic</subject><subject>Amino Acid Transport Systems, Neutral</subject><subject>Animals</subject><subject>BBM</subject><subject>Biological Transport, Active</subject><subject>Blotting, Western</subject><subject>brush border membrane</subject><subject>Carrier Proteins - analysis</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - metabolism</subject><subject>Cross-Linking Reagents</subject><subject>Cystine - metabolism</subject><subject>Cystinuria</subject><subject>Cystinuria - metabolism</subject><subject>Dimethyl Suberimidate</subject><subject>dimethylsuberimidate</subject><subject>DMS</subject><subject>Humans</subject><subject>IgG</subject><subject>immunoglobulin</subject><subject>Jejunum - chemistry</subject><subject>Kidney</subject><subject>Kidney - chemistry</subject><subject>Kidney - metabolism</subject><subject>membrane-spanning domain</subject><subject>Microvilli - chemistry</subject><subject>Molecular Weight</subject><subject>MSD</subject><subject>MSH</subject><subject>N-ethylmaleimide</subject><subject>NBAT</subject><subject>NEM</subject><subject>neutral and basic amino acid transporter</subject><subject>Oocyte</subject><subject>Oocytes</subject><subject>Protein Conformation</subject><subject>Rabbits</subject><subject>Rats</subject><subject>RNA, Complementary</subject><subject>SDS-PAGE</subject><subject>sodium dodecylsulfate/polyacrylamide gel electrophoresis</subject><subject>Xenopus laevis</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1P3DAQhq2qCLbQf1CknKr2kGI7GX9wQKKIbZGQ9kLPljOZVK7ysdgJ1f57EnbFkfY0mnnfeWf0MPZJ8G-CC3XBuShz0Lb4YuEr58pAXrxjK2F0kRelMu_Z6tVywj6k9IfPvRH2mB1rJY0qYcU2mzb8HjqKAbM0xgnHKVI2NJnPIvW-zXCXxtBTNkbfp-0QR4qXWei2bUA_hqFPWegPpikGf8aOGt8m-niop-zX-vbh5md-v_lxd3N9n2Np5_8EqAa9tiAlSNtoBFI1aJSopUJtK6F0DdAUIAGsRI5VxWukGhTaCsrilH3e527j8DhRGl0XElLb-p6GKTmtS2mEUf80CmWUMaaYjeXeiHFIKVLjtjF0Pu6c4G4B7haabqHpLLgX4G5ZOz_kT1VH9evSgfCsr_f639DS7r8y3fr2u1yEZW7hZbocutoH0Yz1KVB0CQP1M5MQCUdXD-HtT58Bc_2jFQ</recordid><startdate>19950717</startdate><enddate>19950717</enddate><creator>Wang, Yan</creator><creator>Tate, Suresh S.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7TM</scope><scope>7X8</scope></search><sort><creationdate>19950717</creationdate><title>Oligomeric structure of a renal cystine transporter: implications in cystinuria</title><author>Wang, Yan ; Tate, Suresh S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4973-156fca79522529f7c5e6d57c2c726c79b167d55f3525592c0cbb0dced56c9b543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>2-mercaptoethanol</topic><topic>Amino acid transport</topic><topic>Amino Acid Transport Systems, Basic</topic><topic>Amino Acid Transport Systems, Neutral</topic><topic>Animals</topic><topic>BBM</topic><topic>Biological Transport, Active</topic><topic>Blotting, Western</topic><topic>brush border membrane</topic><topic>Carrier Proteins - analysis</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - metabolism</topic><topic>Cross-Linking Reagents</topic><topic>Cystine - metabolism</topic><topic>Cystinuria</topic><topic>Cystinuria - metabolism</topic><topic>Dimethyl Suberimidate</topic><topic>dimethylsuberimidate</topic><topic>DMS</topic><topic>Humans</topic><topic>IgG</topic><topic>immunoglobulin</topic><topic>Jejunum - chemistry</topic><topic>Kidney</topic><topic>Kidney - chemistry</topic><topic>Kidney - metabolism</topic><topic>membrane-spanning domain</topic><topic>Microvilli - chemistry</topic><topic>Molecular Weight</topic><topic>MSD</topic><topic>MSH</topic><topic>N-ethylmaleimide</topic><topic>NBAT</topic><topic>NEM</topic><topic>neutral and basic amino acid transporter</topic><topic>Oocyte</topic><topic>Oocytes</topic><topic>Protein Conformation</topic><topic>Rabbits</topic><topic>Rats</topic><topic>RNA, Complementary</topic><topic>SDS-PAGE</topic><topic>sodium dodecylsulfate/polyacrylamide gel electrophoresis</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Yan</creatorcontrib><creatorcontrib>Tate, Suresh S.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Yan</au><au>Tate, Suresh S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Oligomeric structure of a renal cystine transporter: implications in cystinuria</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1995-07-17</date><risdate>1995</risdate><volume>368</volume><issue>2</issue><spage>389</spage><epage>392</epage><pages>389-392</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Homologous proteins (NBAT) which mediate sodium-independent transport of neutral as well as basic amino acids and cystine when expressed in
Xenopus oocytes were recently cloned from mammalian kidneys. Mutations in human NBAT have been implicated in cystinuria. Here, we show that rat kidney and jejunal brush border membrane NBAT (85 kDa) is found in association with a 50 kDa protein. The association involves one or more interprotein disulfide bonds. Rabbit kidney brush border membranes and membranes of NBAT cRNA-injected
Xenopus oocytes also contain such heterodimers. Our data suggest that the heterodimer is the minimal functional unit of NBAT-mediated amino acid transport and that the NBAT-associated 50 kDa protein could play a role in cystinuria.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>7628645</pmid><doi>10.1016/0014-5793(95)00685-3</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; Elsevier ScienceDirect Journals Complete; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
subjects | 2-mercaptoethanol Amino acid transport Amino Acid Transport Systems, Basic Amino Acid Transport Systems, Neutral Animals BBM Biological Transport, Active Blotting, Western brush border membrane Carrier Proteins - analysis Carrier Proteins - chemistry Carrier Proteins - metabolism Cross-Linking Reagents Cystine - metabolism Cystinuria Cystinuria - metabolism Dimethyl Suberimidate dimethylsuberimidate DMS Humans IgG immunoglobulin Jejunum - chemistry Kidney Kidney - chemistry Kidney - metabolism membrane-spanning domain Microvilli - chemistry Molecular Weight MSD MSH N-ethylmaleimide NBAT NEM neutral and basic amino acid transporter Oocyte Oocytes Protein Conformation Rabbits Rats RNA, Complementary SDS-PAGE sodium dodecylsulfate/polyacrylamide gel electrophoresis Xenopus laevis |
title | Oligomeric structure of a renal cystine transporter: implications in cystinuria |
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