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Amino acid transporter B0AT1 (slc6a19) and ancillary protein: impact on function

  • Ion channels, receptors and transporters
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Abstract

Amino acids play an important role in the metabolism of all organisms. Their epithelial re-absorption is due to specific transport proteins, such as B0AT1, a Na+-coupled neutral amino acid symporter belonging to the solute carrier 6 family. Here, a recently cloned fish orthologue, from the intestine of Salmo salar, was electrophysiologically characterized with the two-electrode voltage clamp technique, in Xenopus laevis oocytes heterologously expressing the transporter. Substrate specificity, apparent affinities and the ionic dependence of the transport mechanism were determined in the presence of specific collectrin. Results demonstrated that like the human, but differently from sea bass (Dicentrarchus labrax) orthologue, salmon B0AT1 needs to be associated with partner proteins to be correctly expressed at the oocyte plasma membrane. Cloning of sea bass collectrin and comparison of membrane expression and functionality of the B0AT1 orthologue transporters allowed a deeper investigation on the role of their interactions. The parameters acquired by electrophysiological and immunolocalization experiments in the mammalian and fish transporters contributed to highlight the dynamic of relations and impacts on transport function of the ancillary proteins. The comparative characterization of the physiological parameters of amino acid transporters with auxiliary proteins can help the comprehension of the regulatory mechanism of essential nutrient absorption.

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Acknowledgments

This work has been funded under the seventh EU Framework Programme by the ARRAINA project No. 288925: Advanced Research Initiatives for Nutrition & Aquaculture. The views expressed in this work are the sole responsibility of the authors and do not necessary reflect the views of the European Commission.

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    Authors and Affiliations

    1. Department of Biotechnology and Life Science, University of Insubria, Via J.H. Dunant 3, 21100, Varese, Italy

      Eleonora Margheritis, Francesca Guia Imperiali, Raffaella Cinquetti, Alessandra Vollero, Genciana Terova, Simona Rimoldi, Rossana Girardello & Elena Bossi

    2. Interuniversity Center “The Protein Factory”, Politecnico di Milano, ICRM-CNR Milano and Università dell’Insubria, Via Mancinelli 7, I-20131, Milan, Italy

      Genciana Terova & Elena Bossi

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    1. Eleonora Margheritis
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    2. Francesca Guia Imperiali
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    3. Raffaella Cinquetti
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    4. Alessandra Vollero
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    8. Elena Bossi
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    Correspondence to Elena Bossi.

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    All procedures performed in the studies involving animals were in accordance with the ethical standards of the institution or practice at which the studies were conducted. The experiments were carried out according to the institutional and national ethical guidelines (permission no. 05/12 and no. 1011/2015).

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    Eleonora Margheritis and Francesca Guia Imperiali contributed equally to this work.

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    Margheritis, E., Imperiali, F.G., Cinquetti, R. et al. Amino acid transporter B0AT1 (slc6a19) and ancillary protein: impact on function. Pflugers Arch - Eur J Physiol 468, 1363–1374 (2016). https://doi.org/10.1007/s00424-016-1842-5

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