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.
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Alanine uptake may be mediated by either Slc1a4/SLC1A4 or Slc38a2/SLC38A2.
“Alanine uptake may be mediated by either Slc1a4/SLC1A4 (encoding the transporter ASCT1; Appendix Figure 11B,D) (329) or Slc38a2/SLC38A2 (encoding the transporter SNAT2; Appendix Figure 11C-D) (415).”
From Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men (2018) · cites this paper as [415]
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“This toxicity was blocked by MeAIB, a paradigm analog inhibitor of system A transporters (Mackenzie and Erickson, 2004), suggesting that the toxicity was mediated by excessive L-Gln uptake.”
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- Authors
- Mackenzie, B., & Erickson, J. D.
- Affiliations
- Brigham and Women's Hospital (US)
- Louisiana State University (US)
- Corresponding author
- Mackenzie, Bryan
- Erickson, Jeffrey D.
- Venue
- Pfl�gers Archiv European Journal of Physiology
- Published
- 2004-02-01
- Volume
- 447
- Issue
- 5
- Pages
- 784-795
- ISSN
- 0031-6768 (ISSN-L)
- 1432-2013
- OpenAlex
- W1999946965
- Cited by
- 515
- References
- 1
- Citations by year
- 2026: 9 · 2025: 14 · 2024: 19 · 2023: 13 · 2022: 14 · 2021: 14 · 2020: 25 · 2019: 17 · 2018: 18 · 2017: 26 · 2016: 29 · 2015: 21 · 2014: 26 · 2013: 33 · 2012: 26
- FWCI
- 14.53
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Pflügers Archiv - European Journal of Physiology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant nutrient uptake and metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Keywords
- system A, system N, SNAT1, SNAT2, SNAT3, glutamine transport, pH sensitivity, ammonia detoxification, gluconeogenesis, transporter regulation
- MeSH terms
- Amino Acid Sequence, Animals, Biological Transport, Multigene Family, Humans, Molecular Sequence Data, Sodium, Amino Acids, Neutral, Amino Acid Transport System A
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