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Keywords {🔍}

human, article, xct, acid, amino, transport, activity, system, transporter, access, privacy, cookies, content, marta, information, publish, search, chain, fhc, oocytes, data, log, journal, research, pflügers, heavy, bassi, gasol, manzoni, pineda, slca, related, open, discover, author, springer, essential, function, optional, personal, parties, policy, find, track, archiv, identification, characterisation, coexpresses, cite, maria,

Topics {✒️}

month download article/chapter amino acid transporters 4f2 heavy chain tissue-expression studies showed human cystine transporter marta pineda surface antigen 4f2 cultured cell lines full article pdf privacy choices/manage cookies expressed xct protein human slc7a11 mrna related subjects seventh human member human orthologue thereof check access facultat de biologia instant access heavy chain european economic area mirko riboni oocyte plasma membrane regulating redox homeostasis universitat de barcelona centro especial ramón conditions privacy policy transport characteristics accepting optional cookies human xct antonio zorzano xenopus oocytes article bassi journal finder publish article log marta manzoni rafael martín maria bassi article cite mouse xct oocytes privacy policy personal data books a activity optional cookies human 4f2hc manage preferences subscription content similar content data protection

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WebPage:
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         headline:Identification and characterisation of human xCT that co-expresses, with 4F2 heavy chain, the amino acid transport activity system xc –
         description: We have identified a new human complementary deoxyribonucleic acid (cDNA), for the xc – amino acid transporter (HGMW-approved name SLC7A11; also known as human xCT), that, when co-expressed with the heavy chain of surface antigen 4F2 (4F2hc, also termed CD98), but not with rBAT, (related to the bo,+ amino acid transporter), induces system xc – transport activity in Xenopus oocytes. Human xCT is the seventh human member of the family of amino acid transporters that are subunits of 4F2hc or rBAT and, inview of its amino acid sequence identity (89%) with mouse xCT, is most probably the human orthologue thereof. The amino acid transport activity induced by the co-expression of human 4F2hc and xCT in Xenopus oocytes was sodium independent and specific for L-cystine, L-glutamate and L-aspartate. This activity also functioned in an exchange mode (e.g. cystine/glutamate) with a substrate stoichiometry of 1:1. Expression of human xCT alone in oocytes did not induce amino acid transport activity and the expressed xCT protein was localised intracellularly. When human xCT was co-expressed with 4F2hc, the former localised to the oocyte plasma membrane. Tissue-expression studies showed that human SLC7A11 mRNA is expressed mainly in the brain, but also in pancreas and in cultured cell lines. The transport characteristics of human xCT and the distribution of its tissue expression strongly suggest that it corresponds to the human amino acid transporter system xc –.
         datePublished:
         dateModified:
         pageStart:286
         pageEnd:296
         sameAs:https://doi.org/10.1007/s004240100537
         keywords:
            Human xCT amino acid transporter 4F2 light chain System xc– Oocytes
            Human Physiology
            Molecular Medicine
            Neurosciences
            Cell Biology
            Receptors
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      headline:Identification and characterisation of human xCT that co-expresses, with 4F2 heavy chain, the amino acid transport activity system xc –
      description: We have identified a new human complementary deoxyribonucleic acid (cDNA), for the xc – amino acid transporter (HGMW-approved name SLC7A11; also known as human xCT), that, when co-expressed with the heavy chain of surface antigen 4F2 (4F2hc, also termed CD98), but not with rBAT, (related to the bo,+ amino acid transporter), induces system xc – transport activity in Xenopus oocytes. Human xCT is the seventh human member of the family of amino acid transporters that are subunits of 4F2hc or rBAT and, inview of its amino acid sequence identity (89%) with mouse xCT, is most probably the human orthologue thereof. The amino acid transport activity induced by the co-expression of human 4F2hc and xCT in Xenopus oocytes was sodium independent and specific for L-cystine, L-glutamate and L-aspartate. This activity also functioned in an exchange mode (e.g. cystine/glutamate) with a substrate stoichiometry of 1:1. Expression of human xCT alone in oocytes did not induce amino acid transport activity and the expressed xCT protein was localised intracellularly. When human xCT was co-expressed with 4F2hc, the former localised to the oocyte plasma membrane. Tissue-expression studies showed that human SLC7A11 mRNA is expressed mainly in the brain, but also in pancreas and in cultured cell lines. The transport characteristics of human xCT and the distribution of its tissue expression strongly suggest that it corresponds to the human amino acid transporter system xc –.
      datePublished:
      dateModified:
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      pageEnd:296
      sameAs:https://doi.org/10.1007/s004240100537
      keywords:
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         Human Physiology
         Molecular Medicine
         Neurosciences
         Cell Biology
         Receptors
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      author:
            name:Maria Bassi
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                  name:Telethon Institute of Genetics and Medicine (TIGEM), San Raffaele Biomedical Science Park, 20312 Milan, Italy
                  address:
                     name:Telethon Institute of Genetics and Medicine (TIGEM), San Raffaele Biomedical Science Park, 20312 Milan, Italy,
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Emma Gasol
            affiliation:
                  name:Departament de Bioquímica i Biologia Molecular, Facultat de Biologia, Universitat de Barcelona, Avda. Diagonal 645, 08028 Barcelona, Spain
                  address:
                     name:Departament de Bioquímica i Biologia Molecular, Facultat de Biologia, Universitat de Barcelona, Avda. Diagonal 645, 08028 Barcelona, Spain,
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                     name:Telethon Institute of Genetics and Medicine (TIGEM), San Raffaele Biomedical Science Park, 20312 Milan, Italy,
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            name:Marta Pineda
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                  address:
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                     name:Telethon Institute of Genetics and Medicine (TIGEM), San Raffaele Biomedical Science Park, 20312 Milan, Italy,
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                     name:Departamento de Investigación, Centro Especial Ramón y Cajal, Ctra. de Colmenar Km 9, 28034 Madrid, Spain,
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            address:
               name:Departament de Bioquímica i Biologia Molecular, Facultat de Biologia, Universitat de Barcelona, Avda. Diagonal 645, 08028 Barcelona, Spain,
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               name:Telethon Institute of Genetics and Medicine (TIGEM), San Raffaele Biomedical Science Park, 20312 Milan, Italy,
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