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Gene Review

SLC7A10  -  solute carrier family 7 (neutral amino...

Homo sapiens

Synonyms: ASC1, Asc-1, Asc-type amino acid transporter 1, HASC-1, Solute carrier family 7 member 10, ...
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Disease relevance of SLC7A10


High impact information on SLC7A10

  • TxB2 comprised 2 to 6% of 20-carbon fatty acid cyclooxygenase products biosynthesized from endogenous arachidonic acid in calcium ionophore A23187-stimulated Calu-6 and A549/Asc-1 cells and 16 to 25% of these products in Calu-3 and A549 cells [2].
  • In contrast, harmaline functioned as a competitive inhibitor of L-lysine uptake by system asc1 (apparent Ki = 2.6 mM) [3].
  • This site does not however bind Na+, the asc1 transporter exhibiting normal L-alanine and L-lysine influx kinetics in the total absence of extracellular cations [3].
  • The plant disease resistance gene Asc-1 prevents disruption of sphingolipid metabolism during AAL-toxin-induced programmed cell death [4].
  • Immunohistochemical staining of tissue from a normal human tongue and from a patient with SCC of the tongue revealed that mAb ASC-1 stained the surface of epithelial cells that were in contact with the basement membrane, as well as those cells located two to three layers above the basement membrane [5].

Chemical compound and disease context of SLC7A10

  • BACKGROUND: The human amino acid transporter asc-1 (SLC7A10) exhibits substrate selectivity for small neutral amino acids, including cysteine, is expressed in kidney, is located close to the cystinuria B gene and presents sequence variants (e.g., E112D) in some cystinuria patients [1].

Biological context of SLC7A10


Anatomical context of SLC7A10


Associations of SLC7A10 with chemical compounds

  • Consensus DNA sequences from human, mouse and/or rat were used to design oligonucleotide primers for equine homologues of exons 16, 17 and 20-23 of potassium chloride co-transporter (SLC12A4) and exons 10, 11 and 3, 4, respectively, for two amino acid transporters (SLC7A10 and SLC7A9) [10].
  • Asc-1 mediates a substantial efflux of alanine in a facilitated diffusion mode of transport [1].
  • The facilitated diffusion mode of transport and the expression in distal nephron suggest a role for asc-1 in osmotic adaptation [1].
  • 1. Because of the high-affinity transport with the K(m) value close to the physiological concentration of D-serine, together with the high levels of expression in brain, hAsc-1 is proposed to play significant roles in the D-serine mobilization in brain [7].
  • Here we report a strong induction of attachment of alpha 3 beta 1 integrin expressing human breast carcinoma cell line MDA MB 231 to matrix proteins by two alpha 3 integrin subunit function-blocking monoclonal antibodies (P1B5 and ASC-1) [11].

Other interactions of SLC7A10


Analytical, diagnostic and therapeutic context of SLC7A10

  • One of these mAbs, ASC-1, bound to the surface of SCC cells as determined by flow cytometry [5].


  1. The amino acid transporter asc-1 is not involved in cystinuria. Pineda, M., Font, M., Bassi, M.T., Manzoni, M., Borsani, G., Marigo, V., Fernández, E., Río, R.M., Purroy, J., Zorzano, A., Nunes, V., Palacín, M. Kidney Int. (2004) [Pubmed]
  2. Evidence for thromboxane biosynthesis in established cell lines derived from human lung adenocarcinomas. Hubbard, W.C., Alley, M.C., McLemore, T.L., Boyd, M.R. Cancer Res. (1988) [Pubmed]
  3. Topographical similarities between harmaline inhibition sites on Na+-dependent amino acid transport system ASC in human erythrocytes and Na+-independent system asc in horse erythrocytes. Young, J.D., Mason, D.K., Fincham, D.A. J. Biol. Chem. (1988) [Pubmed]
  4. The plant disease resistance gene Asc-1 prevents disruption of sphingolipid metabolism during AAL-toxin-induced programmed cell death. Spassieva, S.D., Markham, J.E., Hille, J. Plant J. (2002) [Pubmed]
  5. A novel recognition site on laminin for the alpha 3 beta 1 integrin. Pattaramalai, S., Skubitz, K.M., Skubitz, A.P. Exp. Cell Res. (1996) [Pubmed]
  6. Is the SLC7A10 gene on chromosome 19 a candidate locus for cystinuria? Leclerc, D., Wu, Q., Ellis, J.R., Goodyer, P., Rozen, R. Mol. Genet. Metab. (2001) [Pubmed]
  7. Cloning and characterization of a human brain Na(+)-independent transporter for small neutral amino acids that transports D-serine with high affinity. Nakauchi, J., Matsuo, H., Kim, D.K., Goto, A., Chairoungdua, A., Cha, S.H., Inatomi, J., Shiokawa, Y., Yamaguchi, K., Saito, I., Endou, H., Kanai, Y. Neurosci. Lett. (2000) [Pubmed]
  8. Transforming growth factor-beta(1) induces apoptosis via connective tissue growth factor in human aortic smooth muscle cells. Hishikawa, K., Nakaki, T., Fujii, T. Eur. J. Pharmacol. (1999) [Pubmed]
  9. Inhibition of transport system b0,+ in blastocysts by inorganic and organic cations yields insight into the structure of its amino acid receptor site. Van Winkle, L.J., Campione, A.L., Gorman, J.M. Biochim. Biophys. Acta (1990) [Pubmed]
  10. Mapping of equine potassium chloride co-transporter (SLC12A4) and amino acid transporter (SLC7A10) and preliminary studies on associations between SNPs from SLC12A4, SLC7A10 and SLC7A9 and osmotic fragility of erythrocytes. Hanzawa, K., Lear, T.L., Piumi, F., Bailey, E. Anim. Genet. (2002) [Pubmed]
  11. Negative cooperativity between alpha 3 beta 1 and alpha 2 beta 1 integrins in human mammary carcinoma MDA MB 231 cells. Lichtner, R.B., Howlett, A.R., Lerch, M., Xuan, J.A., Brink, J., Langton-Webster, B., Schneider, M.R. Exp. Cell Res. (1998) [Pubmed]
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