Sodium-coupled neutral amino acid (System N/A) transporters of the SLC38 gene family
- PMID: 12845534
- DOI: 10.1007/s00424-003-1117-9
Sodium-coupled neutral amino acid (System N/A) transporters of the SLC38 gene family
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.
Similar articles
-
Functional Consequences of Low Activity of Transport System A for Neutral Amino Acids in Human Bone Marrow Mesenchymal Stem Cells.Int J Mol Sci. 2020 Mar 10;21(5):1899. doi: 10.3390/ijms21051899. Int J Mol Sci. 2020. PMID: 32164327 Free PMC article.
-
The role of the neutral amino acid transporter SNAT2 in cell volume regulation.Acta Physiol (Oxf). 2006 May-Jun;187(1-2):273-83. doi: 10.1111/j.1748-1716.2006.01552.x. Acta Physiol (Oxf). 2006. PMID: 16734764 Review.
-
The SLC38 family of sodium-amino acid co-transporters.Pflugers Arch. 2014 Jan;466(1):155-72. doi: 10.1007/s00424-013-1393-y. Epub 2013 Nov 6. Pflugers Arch. 2014. PMID: 24193407 Review.
-
Transport of L-glutamine, L-alanine, L-arginine and L-histidine by the neuron-specific Slc38a8 (SNAT8) in CNS.J Mol Biol. 2015 Mar 27;427(6 Pt B):1495-1512. doi: 10.1016/j.jmb.2014.10.016. Epub 2014 Oct 30. J Mol Biol. 2015. PMID: 25451601
-
SNAT4 isoform of system A amino acid transporter is expressed in human placenta.Am J Physiol Cell Physiol. 2006 Jan;290(1):C305-12. doi: 10.1152/ajpcell.00258.2005. Epub 2005 Sep 7. Am J Physiol Cell Physiol. 2006. PMID: 16148032
Cited by
-
Glutamine transporters as effective targets in digestive system malignant tumor treatment.Oncol Res. 2024 Sep 18;32(10):1661-1671. doi: 10.32604/or.2024.048287. eCollection 2024. Oncol Res. 2024. PMID: 39308523 Free PMC article. Review.
-
The sodium-bicarbonate cotransporter NBCe1 supports glutamine efflux via SNAT3 (SLC38A3) co-expressed in Xenopus oocytes.Pflugers Arch. 2008 Feb;455(5):885-93. doi: 10.1007/s00424-007-0351-y. Epub 2007 Oct 2. Pflugers Arch. 2008. PMID: 17909850
-
Functional Consequences of Low Activity of Transport System A for Neutral Amino Acids in Human Bone Marrow Mesenchymal Stem Cells.Int J Mol Sci. 2020 Mar 10;21(5):1899. doi: 10.3390/ijms21051899. Int J Mol Sci. 2020. PMID: 32164327 Free PMC article.
-
SNAT2 amino acid transporter is regulated by amino acids of the SLC6 gamma-aminobutyric acid transporter subfamily in neocortical neurons and may play no role in delivering glutamine for glutamatergic transmission.J Biol Chem. 2009 Apr 24;284(17):11224-36. doi: 10.1074/jbc.M806470200. Epub 2009 Feb 24. J Biol Chem. 2009. PMID: 19240036 Free PMC article.
-
Expression and function of system N glutamine transporters (SN1/SN2 or SNAT3/SNAT5) in retinal ganglion cells.Invest Ophthalmol Vis Sci. 2008 Nov;49(11):5151-60. doi: 10.1167/iovs.08-2245. Epub 2008 Aug 8. Invest Ophthalmol Vis Sci. 2008. PMID: 18689705 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases