Role of the System L permease LAT1 in amino acid and iodothyronine transport in placenta

James W. A. Ritchie, Peter M. Taylor

    Research output: Contribution to journalArticle

    74 Citations (Scopus)

    Abstract

    The fete-placental unit relies on a maternal supply of indispensable amino acids and iodothyronines for early development and normal growth. We examined the role of the System L transporter in placental uptake of these substances, using the human placental choriocarcinoma cell line BeWo as a model experimental system. BeWo cells express both heavy (4F2hc) and light (LAT1, LAT2) chains of the System L holotransporter, Saturable transport of both L-[H-3]tryptophan and [I-125]tri-iodo-L-thyronine in BeWo cells includes components sensitive to inhibition by the System-L-specific substrate 2-endoamino-bicycloheptane-2-carboxylic acid; kinetic properties of these components indicate that the 4F2hc-LAT1 transporter isoform is likely to predominate for the carriage of both substances at physiologically relevant concentrations. Both 4F2hc and LAT1 proteins are also expressed in human placental membranes and LAT1 at least is localized largely to the syncytiotrophoblast layer of the term human placenta. The 4F2hc-LAT1 transporter might therefore serve a vital role in supplying the developing fetus and the placenta with both thyroid hormones and indispensable amino acids from the maternal circulation.
    Original languageEnglish
    Pages (from-to)719-725
    Number of pages7
    JournalBiochemical Journal
    Volume356
    Issue number3
    Publication statusPublished - 15 Jun 2001

    Keywords

    • BeWo cells
    • Membrane transport
    • System L
    • Tri-iodothyronine
    • Tryptophan

    Cite this

    Ritchie, James W. A. ; Taylor, Peter M. . / Role of the System L permease LAT1 in amino acid and iodothyronine transport in placenta. In: Biochemical Journal. 2001 ; Vol. 356, No. 3. pp. 719-725.
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    abstract = "The fete-placental unit relies on a maternal supply of indispensable amino acids and iodothyronines for early development and normal growth. We examined the role of the System L transporter in placental uptake of these substances, using the human placental choriocarcinoma cell line BeWo as a model experimental system. BeWo cells express both heavy (4F2hc) and light (LAT1, LAT2) chains of the System L holotransporter, Saturable transport of both L-[H-3]tryptophan and [I-125]tri-iodo-L-thyronine in BeWo cells includes components sensitive to inhibition by the System-L-specific substrate 2-endoamino-bicycloheptane-2-carboxylic acid; kinetic properties of these components indicate that the 4F2hc-LAT1 transporter isoform is likely to predominate for the carriage of both substances at physiologically relevant concentrations. Both 4F2hc and LAT1 proteins are also expressed in human placental membranes and LAT1 at least is localized largely to the syncytiotrophoblast layer of the term human placenta. The 4F2hc-LAT1 transporter might therefore serve a vital role in supplying the developing fetus and the placenta with both thyroid hormones and indispensable amino acids from the maternal circulation.",
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    Role of the System L permease LAT1 in amino acid and iodothyronine transport in placenta. / Ritchie, James W. A. ; Taylor, Peter M. .

    In: Biochemical Journal, Vol. 356, No. 3, 15.06.2001, p. 719-725.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - Role of the System L permease LAT1 in amino acid and iodothyronine transport in placenta

    AU - Ritchie, James W. A.

    AU - Taylor, Peter M.

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    N2 - The fete-placental unit relies on a maternal supply of indispensable amino acids and iodothyronines for early development and normal growth. We examined the role of the System L transporter in placental uptake of these substances, using the human placental choriocarcinoma cell line BeWo as a model experimental system. BeWo cells express both heavy (4F2hc) and light (LAT1, LAT2) chains of the System L holotransporter, Saturable transport of both L-[H-3]tryptophan and [I-125]tri-iodo-L-thyronine in BeWo cells includes components sensitive to inhibition by the System-L-specific substrate 2-endoamino-bicycloheptane-2-carboxylic acid; kinetic properties of these components indicate that the 4F2hc-LAT1 transporter isoform is likely to predominate for the carriage of both substances at physiologically relevant concentrations. Both 4F2hc and LAT1 proteins are also expressed in human placental membranes and LAT1 at least is localized largely to the syncytiotrophoblast layer of the term human placenta. The 4F2hc-LAT1 transporter might therefore serve a vital role in supplying the developing fetus and the placenta with both thyroid hormones and indispensable amino acids from the maternal circulation.

    AB - The fete-placental unit relies on a maternal supply of indispensable amino acids and iodothyronines for early development and normal growth. We examined the role of the System L transporter in placental uptake of these substances, using the human placental choriocarcinoma cell line BeWo as a model experimental system. BeWo cells express both heavy (4F2hc) and light (LAT1, LAT2) chains of the System L holotransporter, Saturable transport of both L-[H-3]tryptophan and [I-125]tri-iodo-L-thyronine in BeWo cells includes components sensitive to inhibition by the System-L-specific substrate 2-endoamino-bicycloheptane-2-carboxylic acid; kinetic properties of these components indicate that the 4F2hc-LAT1 transporter isoform is likely to predominate for the carriage of both substances at physiologically relevant concentrations. Both 4F2hc and LAT1 proteins are also expressed in human placental membranes and LAT1 at least is localized largely to the syncytiotrophoblast layer of the term human placenta. The 4F2hc-LAT1 transporter might therefore serve a vital role in supplying the developing fetus and the placenta with both thyroid hormones and indispensable amino acids from the maternal circulation.

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    JO - Biochemical Journal

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