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Gene Review

Slc26a1  -  solute carrier family 26 (anion exchanger)...

Rattus norvegicus

Synonyms: Canalicular sulfate transporter, SAT-1, Sat1, Solute carrier family 26 member 1, Sulfate anion transporter 1, ...
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Disease relevance of Slc26a1


High impact information on Slc26a1

  • In particular, System A transporter (SAT1) is a highly efficient glutamine transporter, whereas SAT2 exhibits broad specificity for neutral amino acids with a preference for alanine [2].
  • However, whereas SAT1 is present in axonal growth cones and can be detected at later developmental stages at the sites of synaptic contacts, SAT2 does not appear to be significantly expressed in these compartments [2].
  • The cloned cDNA sulfate anion transporter-1 (sat-1) expresses saturable Na(+)-independent sulfate uptake (Km approximately 0.14 mM) that can be inhibited by 4,4'-diisothiocyano-2,2'-disulfonic acid stilbene (DIDS, IC50 = 28 microM) and oxalate, but not by succinate or cholate [3].
  • We have cloned a single cDNA encoding the canalicular sulfate transporter of rat liver using Xenopus laevis oocytes as a functional expression system [3].
  • The cloned sat-1 cDNA has a total length of 3726 base pairs (bp) with an open reading frame encompassing 2109 bp, a 5'-untranslated region of 367 bp, and a 3'-untranslated region of 1250 bp [3].

Biological context of Slc26a1

  • Another group was maximally activated during the time of active membrane fusion (GlcT and SAT-1) [4].
  • We find that SAT1/ATA1 was present in the developing rat brain at all gestational ages examined including prenatal days 17 and 19 and postnatal days 2, 10, 14, and adult [5].

Anatomical context of Slc26a1


Associations of Slc26a1 with chemical compounds

  • Under such conditions, SAT-1 and other late acting glycosyltransferases were over 90% latent, while both GlcT and GalT-2 were just as active as in the detergent-containing assay; they were still inhibited by EDTA [7].
  • These results provide strong evidence that GlcT and GalT-2 face the cytoplasmic side of the Golgi apparatus, whereas SAT-1 and the other late acting enzymes face the luminal side [7].

Analytical, diagnostic and therapeutic context of Slc26a1

  • Reverse transcriptase PCR failed to detect the presence of SAT1 or amino acid transporter 3 (ATA3) in either untreated or TGF-beta 1-treated SMCs [8].
  • In this study, we have examined the developmental expression pattern of SAT1/ATA1 protein in rat brain by immunohistochemistry [5].


  1. Sulfate homeostasis, NaSi-1 cotransporter, and SAT-1 exchanger expression in chronic renal failure in rats. Fernandes, I., Laouari, D., Tutt, P., Hampson, G., Friedlander, G., Silve, C. Kidney Int. (2001) [Pubmed]
  2. Localization and functional relevance of system a neutral amino acid transporters in cultured hippocampal neurons. Armano, S., Coco, S., Bacci, A., Pravettoni, E., Schenk, U., Verderio, C., Varoqui, H., Erickson, J.D., Matteoli, M. J. Biol. Chem. (2002) [Pubmed]
  3. Functional expression cloning of the canalicular sulfate transport system of rat hepatocytes. Bissig, M., Hagenbuch, B., Stieger, B., Koller, T., Meier, P.J. J. Biol. Chem. (1994) [Pubmed]
  4. Glycosphingolipids during skeletal muscle cell differentiation: comparison of normal and fusion-defective myoblasts. Cambron, L.D., Leskawa, K.C. Mol. Cell. Biochem. (1994) [Pubmed]
  5. Ontogeny of the neutral amino acid transporter SAT1/ATA1 in rat brain. Weiss, M.D., Derazi, S., Rossignol, C., Varoqui, H., Erickson, J.D., Kilberg, M.S., Anderson, K.J. Brain Res. Dev. Brain Res. (2003) [Pubmed]
  6. A dileucine motif targets the sulfate anion transporter sat-1 to the basolateral membrane in renal cell lines. Regeer, R.R., Markovich, D. Am. J. Physiol., Cell Physiol. (2004) [Pubmed]
  7. Topography of glycosyltransferases involved in the initial glycosylations of gangliosides. Trinchera, M., Fabbri, M., Ghidoni, R. J. Biol. Chem. (1991) [Pubmed]
  8. Transforming growth factor-beta 1 stimulates vascular smooth muscle cell L-proline transport by inducing system A amino acid transporter 2 (SAT2) gene expression. Ensenat, D., Hassan, S., Reyna, S.V., Schafer, A.I., Durante, W. Biochem. J. (2001) [Pubmed]
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