ABCG transporters and disease

Authors

  • Owen M. Woodward,

    1.  Department of Physiology, Johns Hopkins University, School of Medicine, Baltimore, MD, USA
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  • Anna Köttgen,

    1.  Renal Division, University Medical Centre Freiburg, Freiburg, Germany
    2.  Department of Epidemiology, Johns Hopkins Bloomberg School of Public Health, Baltimore, MD, USA
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  • Michael Köttgen

    1.  Renal Division, University Medical Centre Freiburg, Freiburg, Germany
    2.  Department of Nephrology, Johns Hopkins University, School of Medicine, Baltimore, MD, USA
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M. Köttgen, Renal Division, University Medical Centre Freiburg, Freiburg, Germany
Fax: +49 (0)761 27063240
Tel: +49 (0)761 27032990
E-mail: michael.koettgen@uniklinik-freiburg.de

Abstract

ATP-binding cassette (ABC) transporters form a large family of transmembrane proteins that facilitate the transport of specific substrates across membranes in an ATP-dependent manner. Transported substrates include lipids, lipopolysaccharides, amino acids, peptides, proteins, inorganic ions, sugars and xenobiotics. Despite this broad array of substrates, the physiological substrate of many ABC transporters has remained elusive. ABC transporters are divided into seven subfamilies, A–G, based on sequence similarity and domain organization. Here we review the role of members of the ABCG subfamily in human disease and how the identification of disease genes helped to determine physiological substrates for specific ABC transporters. We focus on the recent discovery of mutations in ABCG2 causing hyperuricemia and gout, which has led to the identification of urate as a physiological substrate for ABCG2.

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