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Gene Review

SLC7A3  -  solute carrier family 7 (cationic amino...

Homo sapiens

Synonyms: ATRC3, CAT-3, CAT3, Cationic amino acid transporter 3, Cationic amino acid transporter y+, ...
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Disease relevance of SLC7A3

  • In Xenopus laevis oocytes and human U373MG glioblastoma cells, hCAT-3-mediated L-arginine transport was significantly reduced upon treatment with compounds that activate classical PKC [1].
  • On the other hand, the Cat3 transcript is up-regulated by dehydration and osmotic stress only in ABA-deficient mutant leaves, implying that ABA may act as a repressor for Cat3 expression in response to dehydration and high osmoticum [2].

High impact information on SLC7A3

  • In the CAT family, three genes encode for four different isoforms [CAT-1, CAT-2A, CAT-2(B) and CAT-3]; these are approximately 70-kDa proteins with multiple transmembrane segments (12-14), and despite their structural similarity, they differ in tissue distribution, kinetics, and regulatory properties [3].
  • This circadian rhythm in Cat3 gene expression and the resulting high levels of mRNA which accumulate late in the light period suggest that the catalase 3 (CAT-3) isozyme is being synthesized for accumulation in the dark period [4].
  • This, together with the high level of Cat3 mRNA and CAT-3 protein accumulation in dark-grown maize shoots, suggests that the activity of the CAT-3 isozyme might be associated with a metabolic process important in shoot cells in the dark [4].
  • In oocyte injection assays, CAT3 cRNA exhibited a saturable, sodium ion-independent transport activity with high affinity for L-arginine and L-lysine (Km = 40-60 and 115-165 microM, respectively) [5].
  • The presence of L-arginine in the incubation medium stimulated the efflux rate of L-arginine, indicating that CAT3 is subject to trans-stimulation [5].

Biological context of SLC7A3

  • Oocytes expressing hCAT-3 displayed less negative membrane potentials and larger voltage-dependent currents than native or water-injected oocytes did [6].
  • The Cat3 gene of maize exhibits a transcriptionally regulated circadian rhythm [7].
  • The results suggest that the molecular basis for Cat3 null phenotype in IDS28 may be a deletion in the 5' end of the Cat3 gene [8].
  • Two of the Cat2 introns are located in the same position as the two Cat3 introns [9].

Anatomical context of SLC7A3

  • Transport studies in Xenopus laevis oocytes revealed that hCAT-3 is selective for cationic L-amino acids and exhibits a maximal transport activity similar to other CAT proteins [10].
  • We have cloned a cDNA containing the complete coding region of human CAT-3. hCAT-3 is glycosylated and localized to the plasma membrane [10].
  • Human CAT-3 expression is not restricted to the brain, in fact, by far the highest expression was found in thymus [10].
  • In contrast to its highly localized expression during the primitive streak stage and in the adult stage, CAT3 expression was detected more widely in 13.5 day post-coitum mouse embryos [5].
  • The induction of the Cat3 circadian expression in etiolated leaves is probably regulated by a very low fluence phytochrome response; the involvement of a blue light/UV-A and a UV-B photoreceptor is also possible [7].

Associations of SLC7A3 with chemical compounds

  • This is in contrast to rat and murine CAT-3 proteins that have been reported to display a very low activity and to be inhibited by neutral and anionic L-amino acids as well as D-arginine (Hosokawa, H., et al. (1997) J. Biol. Chem. 272, 8717-8722; Ito, K., and Groudine, M. (1997) J. Biol. Chem. 272, 26780-26786) [10].
  • In young leaves, only Cat1 and Cat3 transcripts increase in response to wounding, but JA does not play a role [11].

Other interactions of SLC7A3


Analytical, diagnostic and therapeutic context of SLC7A3

  • On the Northern blot of adult rat tissues, the expression of CAT3 is restricted to the brain [12].
  • In the present study, cellular localization of CAT3 mRNA and protein in the adult rat brain sections was examined by in situ hybridization with cRNA and immunostaining with a CAT3-specific antiserum, respectively [12].


  1. Activation of classical protein kinase C reduces the expression of human cationic amino acid transporter 3 (hCAT-3) in the plasma membrane. Rotmann, A., Vékony, N., Gassner, D., Niegisch, G., Strand, D., Martiné, U., Closs, E.I. Biochem. J. (2006) [Pubmed]
  2. Catalase transcript accumulation in response to dehydration and osmotic stress in leaves of maize viviparous mutants. Guan, L.M., Scandalios, J.G. Redox Rep. (2000) [Pubmed]
  3. Transporters for cationic amino acids in animal cells: discovery, structure, and function. Devés, R., Boyd, C.A. Physiol. Rev. (1998) [Pubmed]
  4. Expression of the maize Cat3 catalase gene is under the influence of a circadian rhythm. Redinbaugh, M.G., Sabre, M., Scandalios, J.G. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  5. A new member of the cationic amino acid transporter family is preferentially expressed in adult mouse brain. Ito, K., Groudine, M. J. Biol. Chem. (1997) [Pubmed]
  6. Monovalent cation conductance in Xenopus laevis oocytes expressing hCAT-3. Gilles, W., Vulcu, S.D., Liewald, J.F., Habermeier, A., Vékony, N., Closs, E.I., Rupp, J., Nawrath, H. Biochim. Biophys. Acta (2005) [Pubmed]
  7. Response of the maize catalases to light. Polidoros, A.N., Scandalios, J.G. Free Radic. Biol. Med. (1997) [Pubmed]
  8. Molecular characterization of a catalase null allele at the Cat3 locus in maize. Wadsworth, G.J., Scandalios, J.G. Genetics (1990) [Pubmed]
  9. Isolation, characterization and expression of the maize Cat2 catalase gene. Guan, L., Polidoros, A.N., Scandalios, J.G. Plant Mol. Biol. (1996) [Pubmed]
  10. Human cationic amino acid transporter hCAT-3 is preferentially expressed in peripheral tissues. Vékony, N., Wolf, S., Boissel, J.P., Gnauert, K., Closs, E.I. Biochemistry (2001) [Pubmed]
  11. Hydrogen-peroxide-mediated catalase gene expression in response to wounding. Guan, L.M., Scandalios, J.G. Free Radic. Biol. Med. (2000) [Pubmed]
  12. Neuron-specific expression of cationic amino acid transporter 3 in the adult rat brain. Hosokawa, H., Ninomiya, H., Sawamura, T., Sugimoto, Y., Ichikawa, A., Fujiwara, K., Masaki, T. Brain Res. (1999) [Pubmed]
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