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
Hauptverfasser: Wang, Yan, Tate, Suresh S.
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Tate, Suresh S.
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.
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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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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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