Pflügers Archiv

, Volume 447, Issue 5, pp 784–795

Sodium-coupled neutral amino acid (System N/A) transporters of the SLC38 gene family

The ABC of Solute carriers Guest Editor: Matthias A. Hediger

DOI: 10.1007/s00424-003-1117-9

Cite this article as:
Mackenzie, B. & Erickson, J.D. Pflugers Arch - Eur J Physiol (2004) 447: 784. doi:10.1007/s00424-003-1117-9

Abstract

The sodium-coupled neutral amino acid transporters (SNAT) of the SLC38 gene family resemble the classically-described System A and System N transport activities in terms of their functional properties and patterns of regulation. Transport of small, aliphatic amino acids by System A subtypes (SNAT1, SNAT2, and SNAT4) is rheogenic and pH sensitive. The System N subtypes SNAT3 and SNAT5 also countertransport H+, which may be key to their operation in reverse, and have narrower substrate profiles than do the System A subtypes. Glutamine emerges as a favored substrate throughout the family, except for SNAT4. The SLC38 transporters undoubtedly play many physiological roles including the transfer of glutamine from astrocyte to neuron in the CNS, ammonia detoxification and gluconeogenesis in the liver, and the renal response to acidosis. Probing their regulation has revealed additional roles, and recent work has considered SLC38 transporters as therapeutic targets in neoplasia.

Keywords

Glutamine transport Amino acid transport Glutamate-glutamine cycle Adaptive regulation SNAT6 Gluconeogenesis Ammonia detoxification 

Copyright information

© Springer-Verlag  2004

Authors and Affiliations

  1. 1.Membrane Biology Program and Renal DivisionBrigham and Women's Hospital and Harvard Medical SchoolBostonUSA
  2. 2.Neuroscience Center and Department of PharmacologyLouisiana State University Health Sciences CenterNew OrleansUSA

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