Characterization of the Rat Neutral and Basic Amino Acid Transporter Utilizing Anti-Peptide Antibodies
High-titer, site-specific antibodies have been produced against the rat kidney broad-spectrum, sodium-independent neutral and basic amino acid transporter (NBAA-Tr) whose cDNA we cloned earlier. These antibodies have allowed us to characterize the transporter protein in normal rat tissues and in var...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1993-05, Vol.90 (9), p.4022-4026 |
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| creator | Mosckovitz, Rachel Yan, Ning Heimer, Edward Felix, Arthur Tate, Suresh S. Udenfriend, Sidney |
| description | High-titer, site-specific antibodies have been produced against the rat kidney broad-spectrum, sodium-independent neutral and basic amino acid transporter (NBAA-Tr) whose cDNA we cloned earlier. These antibodies have allowed us to characterize the transporter protein in normal rat tissues and in various cellular and in vitro expression systems. Western analysis detected 84- to 87-kDa glycosylated species enriched in rat renal and jejunal epithelial cell brush border membranes. In vitro translation of NBAA-Tr complementary RNA in the rabbit reticulocyte lysate system yielded a 78-kDa protein, a molecular mass that was predicted by the amino acid sequence deduced from the cloned cDNA. Translation in the presence of rough microsomal membranes yielded a glycosylated 89-kDa species. Glycosylated 87- to 89-kDa species were also expressed in Xenopus oocytes microinjected with NBAA-Tr complementary RNA and in COS-7 cells transfected with NBAA-Tr cDNA. Localization of NBAA-Tr in renal and intestinal brush border membranes is consistent with its proposed role in transepithelial transport of amino acids. |
| doi_str_mv | 10.1073/pnas.90.9.4022 |
| format | Article |
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These antibodies have allowed us to characterize the transporter protein in normal rat tissues and in various cellular and in vitro expression systems. Western analysis detected 84- to 87-kDa glycosylated species enriched in rat renal and jejunal epithelial cell brush border membranes. In vitro translation of NBAA-Tr complementary RNA in the rabbit reticulocyte lysate system yielded a 78-kDa protein, a molecular mass that was predicted by the amino acid sequence deduced from the cloned cDNA. Translation in the presence of rough microsomal membranes yielded a glycosylated 89-kDa species. Glycosylated 87- to 89-kDa species were also expressed in Xenopus oocytes microinjected with NBAA-Tr complementary RNA and in COS-7 cells transfected with NBAA-Tr cDNA. Localization of NBAA-Tr in renal and intestinal brush border membranes is consistent with its proposed role in transepithelial transport of amino acids.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.90.9.4022</identifier><identifier>PMID: 8483918</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Amino Acid Sequence ; Amino Acid Transport Systems, Basic ; Amino Acid Transport Systems, Neutral ; Amino acids ; Amino Acids - metabolism ; Animals ; Antibodies ; Biochemistry ; Biological and medical sciences ; Biological Transport ; Blotting, Western ; Carrier Proteins - genetics ; Carrier Proteins - isolation & purification ; Carrier Proteins - metabolism ; Cell Line ; Cell physiology ; Cercopithecus aethiops ; characterization ; Complementary DNA ; Complementary RNA ; COS cells ; Fundamental and applied biological sciences. Psychology ; Immunoprecipitation ; Jejunum - metabolism ; Kidney - metabolism ; Kidneys ; Membrane and intracellular transports ; Microvilli ; Microvilli - metabolism ; Molecular and cellular biology ; Molecular Sequence Data ; Molecular Weight ; neutral and basic amino acid transporter ; Oocytes ; Oocytes - metabolism ; Peptides - chemical synthesis ; Peptides - immunology ; Protein Biosynthesis ; Proteins ; Rabbits ; Rats ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Reticulocytes - metabolism ; Rodents ; Transfection ; use ; Xenopus</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1993-05, Vol.90 (9), p.4022-4026</ispartof><rights>Copyright 1993 The National Academy of Sciences of the United States of America</rights><rights>1993 INIST-CNRS</rights><rights>Copyright National Academy of Sciences May 1, 1993</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4592-a4da96a00a07ff3f8200953081a92d7f11dbb00c20583f7fb3f9ca471c19f3633</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/90/9.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2361884$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2361884$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4773708$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8483918$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mosckovitz, Rachel</creatorcontrib><creatorcontrib>Yan, Ning</creatorcontrib><creatorcontrib>Heimer, Edward</creatorcontrib><creatorcontrib>Felix, Arthur</creatorcontrib><creatorcontrib>Tate, Suresh S.</creatorcontrib><creatorcontrib>Udenfriend, Sidney</creatorcontrib><title>Characterization of the Rat Neutral and Basic Amino Acid Transporter Utilizing Anti-Peptide Antibodies</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>High-titer, site-specific antibodies have been produced against the rat kidney broad-spectrum, sodium-independent neutral and basic amino acid transporter (NBAA-Tr) whose cDNA we cloned earlier. These antibodies have allowed us to characterize the transporter protein in normal rat tissues and in various cellular and in vitro expression systems. Western analysis detected 84- to 87-kDa glycosylated species enriched in rat renal and jejunal epithelial cell brush border membranes. In vitro translation of NBAA-Tr complementary RNA in the rabbit reticulocyte lysate system yielded a 78-kDa protein, a molecular mass that was predicted by the amino acid sequence deduced from the cloned cDNA. Translation in the presence of rough microsomal membranes yielded a glycosylated 89-kDa species. Glycosylated 87- to 89-kDa species were also expressed in Xenopus oocytes microinjected with NBAA-Tr complementary RNA and in COS-7 cells transfected with NBAA-Tr cDNA. Localization of NBAA-Tr in renal and intestinal brush border membranes is consistent with its proposed role in transepithelial transport of amino acids.</description><subject>Amino Acid Sequence</subject><subject>Amino Acid Transport Systems, Basic</subject><subject>Amino Acid Transport Systems, Neutral</subject><subject>Amino acids</subject><subject>Amino Acids - metabolism</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biological Transport</subject><subject>Blotting, Western</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Line</subject><subject>Cell physiology</subject><subject>Cercopithecus aethiops</subject><subject>characterization</subject><subject>Complementary DNA</subject><subject>Complementary RNA</subject><subject>COS cells</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Immunoprecipitation</subject><subject>Jejunum - metabolism</subject><subject>Kidney - metabolism</subject><subject>Kidneys</subject><subject>Membrane and intracellular transports</subject><subject>Microvilli</subject><subject>Microvilli - metabolism</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>neutral and basic amino acid transporter</subject><subject>Oocytes</subject><subject>Oocytes - metabolism</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - immunology</subject><subject>Protein Biosynthesis</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>Rats</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Reticulocytes - metabolism</subject><subject>Rodents</subject><subject>Transfection</subject><subject>use</subject><subject>Xenopus</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kduLEzEYxYMo61p99UlhEPFt6pfLTBLwpRZvsKjI7nNIM8k2ZZp0k4zo_vXObGupIj6FcH7nux2EnmKYY-D09S7oPJcwl3MGhNxD5xgkrlsm4T46ByC8Foywh-hRzhsAkI2AM3QmmKASi3PklmudtCk2-VtdfAxVdFVZ2-qbLtVnO5Sk-0qHrnqrszfVYutDrBbGd9Vl0iHvYhqt1VXxvb_14bpahOLrr3ZXfGfvPqvYeZsfowdO99k-ObwzdPX-3eXyY33x5cOn5eKiNqyRpNas07LVABq4c9QJMk1MQWAtSccdxt1qBWAINII67lbUSaMZxwZLR1tKZ-jNvu5uWG1tZ2yYFlC75Lc6_VRRe_WnEvxaXcfvirWMitH-6mBP8Wawuaitz8b2vQ42DlnxhmMq7vr8H8RtgxsqJ_DFX-AmDimMN1AEMGlZO4Y4Q_M9ZFLMOVl3HBiDmlJWU8pKgpJqSnk0PD9d84gfYh31lwddZ6N7N0ZlfD5ijHPK4XTdqfxv9dhGuaHvi_1RTvr9Exz1Z3t9k0tMR4DQFgvB6C831tE3</recordid><startdate>19930501</startdate><enddate>19930501</enddate><creator>Mosckovitz, Rachel</creator><creator>Yan, Ning</creator><creator>Heimer, Edward</creator><creator>Felix, Arthur</creator><creator>Tate, Suresh S.</creator><creator>Udenfriend, Sidney</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><scope>IQODW</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>M7Z</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19930501</creationdate><title>Characterization of the Rat Neutral and Basic Amino Acid Transporter Utilizing Anti-Peptide Antibodies</title><author>Mosckovitz, Rachel ; Yan, Ning ; Heimer, Edward ; Felix, Arthur ; Tate, Suresh S. ; Udenfriend, Sidney</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4592-a4da96a00a07ff3f8200953081a92d7f11dbb00c20583f7fb3f9ca471c19f3633</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acid Transport Systems, Basic</topic><topic>Amino Acid Transport Systems, Neutral</topic><topic>Amino acids</topic><topic>Amino Acids - metabolism</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biological Transport</topic><topic>Blotting, Western</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Line</topic><topic>Cell physiology</topic><topic>Cercopithecus aethiops</topic><topic>characterization</topic><topic>Complementary DNA</topic><topic>Complementary RNA</topic><topic>COS cells</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Immunoprecipitation</topic><topic>Jejunum - metabolism</topic><topic>Kidney - metabolism</topic><topic>Kidneys</topic><topic>Membrane and intracellular transports</topic><topic>Microvilli</topic><topic>Microvilli - metabolism</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>neutral and basic amino acid transporter</topic><topic>Oocytes</topic><topic>Oocytes - metabolism</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - immunology</topic><topic>Protein Biosynthesis</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>Rats</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Reticulocytes - metabolism</topic><topic>Rodents</topic><topic>Transfection</topic><topic>use</topic><topic>Xenopus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mosckovitz, Rachel</creatorcontrib><creatorcontrib>Yan, Ning</creatorcontrib><creatorcontrib>Heimer, Edward</creatorcontrib><creatorcontrib>Felix, Arthur</creatorcontrib><creatorcontrib>Tate, Suresh S.</creatorcontrib><creatorcontrib>Udenfriend, Sidney</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Biochemistry Abstracts 1</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mosckovitz, Rachel</au><au>Yan, Ning</au><au>Heimer, Edward</au><au>Felix, Arthur</au><au>Tate, Suresh S.</au><au>Udenfriend, Sidney</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of the Rat Neutral and Basic Amino Acid Transporter Utilizing Anti-Peptide Antibodies</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1993-05-01</date><risdate>1993</risdate><volume>90</volume><issue>9</issue><spage>4022</spage><epage>4026</epage><pages>4022-4026</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>High-titer, site-specific antibodies have been produced against the rat kidney broad-spectrum, sodium-independent neutral and basic amino acid transporter (NBAA-Tr) whose cDNA we cloned earlier. These antibodies have allowed us to characterize the transporter protein in normal rat tissues and in various cellular and in vitro expression systems. Western analysis detected 84- to 87-kDa glycosylated species enriched in rat renal and jejunal epithelial cell brush border membranes. In vitro translation of NBAA-Tr complementary RNA in the rabbit reticulocyte lysate system yielded a 78-kDa protein, a molecular mass that was predicted by the amino acid sequence deduced from the cloned cDNA. Translation in the presence of rough microsomal membranes yielded a glycosylated 89-kDa species. Glycosylated 87- to 89-kDa species were also expressed in Xenopus oocytes microinjected with NBAA-Tr complementary RNA and in COS-7 cells transfected with NBAA-Tr cDNA. Localization of NBAA-Tr in renal and intestinal brush border membranes is consistent with its proposed role in transepithelial transport of amino acids.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>8483918</pmid><doi>10.1073/pnas.90.9.4022</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1993-05, Vol.90 (9), p.4022-4026 |
| issn | 0027-8424 1091-6490 |
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| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Amino Acid Transport Systems, Basic Amino Acid Transport Systems, Neutral Amino acids Amino Acids - metabolism Animals Antibodies Biochemistry Biological and medical sciences Biological Transport Blotting, Western Carrier Proteins - genetics Carrier Proteins - isolation & purification Carrier Proteins - metabolism Cell Line Cell physiology Cercopithecus aethiops characterization Complementary DNA Complementary RNA COS cells Fundamental and applied biological sciences. Psychology Immunoprecipitation Jejunum - metabolism Kidney - metabolism Kidneys Membrane and intracellular transports Microvilli Microvilli - metabolism Molecular and cellular biology Molecular Sequence Data Molecular Weight neutral and basic amino acid transporter Oocytes Oocytes - metabolism Peptides - chemical synthesis Peptides - immunology Protein Biosynthesis Proteins Rabbits Rats Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Reticulocytes - metabolism Rodents Transfection use Xenopus |
| title | Characterization of the Rat Neutral and Basic Amino Acid Transporter Utilizing Anti-Peptide Antibodies |
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