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Slc38a3  -  solute carrier family 38, member 3

Rattus norvegicus

Synonyms: N-system amino acid transporter 1, Na(+)-coupled neutral amino acid transporter 3, Nat1, Sn1, Snat3, ...
 
 
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Disease relevance of Slc38a3

 

High impact information on Slc38a3

  • However, SN1 remains sorted to the basolateral membranes [1].
  • During CMA, SN1 expression increases five- to six-fold and appears also in cortical tubule cells in parallel with the increased expression and activity of phosphate-activated glutaminase, a mitochondrial enzyme involved in ammoniagenesis [1].
  • The glutamine transporter SNAT3 (SN1) has recently been identified as one of the major mediators of glutamine efflux from astrocytes [5].
  • The acidosis-induced increase in Na(+)-dependent glutamine uptake was eliminated by histidine, confirming transport by system N. SN1 protein was detected only in BLMV and BBMV from acidotic rats [2].
  • We studied the expression of the system N1 (SN1) amino acid transporter in the kidney during chronic ammonium chloride acidosis in rats [2].
 

Biological context of Slc38a3

 

Anatomical context of Slc38a3

  • When compared to the expression of glutamine transporter mRNAs in cultured astrocytes it appeared likely that glutamine efflux was mediated by SN1, LAT2, ASCT2 and an additional, yet unidentified, transporter that mediates about 40% of the basal efflux [8].
  • The system N transporter SN1 mediates efflux as well as influx of glutamine in glial cells [Chaudhry et al. (1999), Cell, 99, 769-780] [9].
  • A dedication of SN1 to neurotransmitter recycling is further supported by the lack of SN1 immunoreactivity in oligodendrocytes (cells rich in glutamine but without perisynaptic processes) [9].
  • System N(m) activity mediates most trans-sarcolemmal glutamine movement, and although two System N (SN) isoforms have been identified (SN1/sodium-coupled neutral amino acid transporter or System N and A transporters [SNAT]-3; and SN2/SNAT5), their expression in skeletal muscle remains controversial [10].
 

Associations of Slc38a3 with chemical compounds

  • SN1, a Na(+)- and H(+)-dependent glutamine transporter has previously been identified molecularly, and its mRNA has been detected in tubule cells in the medulla of the kidney [1].
  • This is in accord with the SN2 nature of the weak carcinogen methylmethanesulphonate compared with the SN1 nature of the reactive methylating agent derived from either one of the N-methyl-N-nitroso compounds [11].
  • O6-methylguanine (O6-mG) is widely considered to be the critical toxic lesion induced by methylating agents, including AMMN, NMUR, and MNU, which form DNA adducts through SN1 reactions [12].
  • In several regions, SN1 immunoreactivity is higher in association with GABAergic than glutamatergic synapses, in agreement with observations that exogenous glutamine increases output of transmitter glutamate but not GABA [9].
  • More potent carcinogens, that react predominantly with an Ingold's SN1 mechanism, mainly alkylate the amino group of lysine and the guanido group of arginine [13].
 

Analytical, diagnostic and therapeutic context of Slc38a3

  • Light and electron microscopic immunocytochemistry shows that glutamatergic, GABAergic and, surprisingly, purely glycinergic boutons are ensheathed by astrocytic SN1 laden processes, indicating a role of glutamine in the production of all three rapid transmitters [9].

References

  1. Induction and targeting of the glutamine transporter SN1 to the basolateral membranes of cortical kidney tubule cells during chronic metabolic acidosis suggest a role in pH regulation. Solbu, T.T., Boulland, J.L., Zahid, W., Lyamouri Bredahl, M.K., Amiry-Moghaddam, M., Storm-Mathisen, J., Roberg, B.A., Chaudhry, F.A. J. Am. Soc. Nephrol. (2005) [Pubmed]
  2. Regulation of expression of the SN1 transporter during renal adaptation to chronic metabolic acidosis in rats. Karinch, A.M., Lin, C.M., Wolfgang, C.L., Pan, M., Souba, W.W. Am. J. Physiol. Renal Physiol. (2002) [Pubmed]
  3. Examination of alpha-carbonyl derivatives of nitrosodimethylamine and ethylnitrosomethylamine as putative proximate carcinogens. Elespuru, R.K., Saavedra, J.E., Kovatch, R.M., Lijinsky, W. Carcinogenesis (1993) [Pubmed]
  4. Suppression of glial glutamine release to the extracellular fluid studied in vivo by NMR and microdialysis in hyperammonemic rat brain. Kanamori, K., Ross, B.D. J. Neurochem. (2005) [Pubmed]
  5. Astroglial glutamine transport by system N is upregulated by glutamate. Bröer, A., Deitmer, J.W., Bröer, S. Glia (2004) [Pubmed]
  6. Primary 13C and beta-secondary 2H KIEs for trans-sialidase. A snapshot of nucleophilic participation during catalysis. Yang, J., Schenkman, S., Horenstein, B.A. Biochemistry (2000) [Pubmed]
  7. Protein modification of glutamine transporters in SV40-transformed hepatocytes and immunodetection of proteins associated with hepatic system N transport activity. Tamarappoo, B.K., Singh, H.P., Kilberg, M.S. J. Nutr. (1994) [Pubmed]
  8. Glutamine efflux from astrocytes is mediated by multiple pathways. Deitmer, J.W., Bröer, A., Bröer, S. J. Neurochem. (2003) [Pubmed]
  9. Cell-specific expression of the glutamine transporter SN1 suggests differences in dependence on the glutamine cycle. Boulland, J.L., Osen, K.K., Levy, L.M., Danbolt, N.C., Edwards, R.H., Storm-Mathisen, J., Chaudhry, F.A. Eur. J. Neurosci. (2002) [Pubmed]
  10. Type I diabetes affects skeletal muscle glutamine uptake in a fiber-specific manner. Onan, M.C., Fisher, J.S., Ju, J.S., Fuchs, B.C., Bode, B.P. Exp. Biol. Med. (Maywood) (2005) [Pubmed]
  11. DNA and protein adducts as indicators of in vivo methylation by nitrosatable drugs. Farmer, P.B., Shuker, E.G., Bird, I. Carcinogenesis (1986) [Pubmed]
  12. Genotoxic methylating agents modulate extracellular signal regulated kinase activity through MEK-dependent, glutathione-, and DNA methylation-independent mechanisms in lung epithelial cells. Wichmann, A.E., Thomson, N.M., Peterson, L.A., Wattenberg, E.V. Chem. Res. Toxicol. (2003) [Pubmed]
  13. Specific targets of alkylating agents in nuclear proteins of cultured hepatocytes. Boffa, L.C., Bolognesi, C., Mariani, M.R. Mutat. Res. (1987) [Pubmed]
 
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