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      Amino acid transport across mammalian intestinal and renal epithelia.

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      Physiological reviews
      American Physiological Society

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          Abstract

          The transport of amino acids in kidney and intestine is critical for the supply of amino acids to all tissues and the homeostasis of plasma amino acid levels. This is illustrated by a number of inherited disorders affecting amino acid transport in epithelial cells, such as cystinuria, lysinuric protein intolerance, Hartnup disorder, iminoglycinuria, dicarboxylic aminoaciduria, and some other less well-described disturbances of amino acid transport. The identification of most epithelial amino acid transporters over the past 15 years allows the definition of these disorders at the molecular level and provides a clear picture of the functional cooperation between transporters in the apical and basolateral membranes of mammalian epithelial cells. Transport of amino acids across the apical membrane not only makes use of sodium-dependent symporters, but also uses the proton-motive force and the gradient of other amino acids to efficiently absorb amino acids from the lumen. In the basolateral membrane, antiporters cooperate with facilitators to release amino acids without depleting cells of valuable nutrients. With very few exceptions, individual amino acids are transported by more than one transporter, providing backup capacity for absorption in the case of mutational inactivation of a transport system.

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          Author and article information

          Journal
          Physiol Rev
          Physiological reviews
          American Physiological Society
          0031-9333
          0031-9333
          Jan 2008
          : 88
          : 1
          Affiliations
          [1 ] School of Biochemistry and Molecular Biology, Australian National University, Canberra, Australian Capital Territory, Australia. stefan.broeer@anu.edu.au
          Article
          88/1/249
          10.1152/physrev.00018.2006
          18195088
          56237e1e-4fe9-413f-812f-45f1092d463d
          History

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