4.4 Article

Cloning and characterization of a human brain Na+-independent transporter for small neutral amino acids that transports D-serine with high affinity

Journal

NEUROSCIENCE LETTERS
Volume 287, Issue 3, Pages 231-235

Publisher

ELSEVIER SCI IRELAND LTD
DOI: 10.1016/S0304-3940(00)01169-1

Keywords

amino acid transporter; system asc; 4F2 heavy chain; D-serine; N-methyl-D-aspartate receptor; human chromosome 19; human

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We isolated a cDNA for the human homologue of system asc transporter Asc-1 from human brain. The encoded protein designated as hAsc-1 (human Asc-1) exhibited 91 % sequence identity to mouse Asc-1. Consistent with mouse Asc-1, hAsc-1 required 4F2 heavy chain for its functional expression in Xenopus oocytes. hAsc-1 exhibited the properties of amino acid transport system asc which transports small neutral amino acids in a Na+-independent manner. hAsc-1 transported D-serine at high affinity with a K-m value of 22.8 mu M. In brain, 2.0 kb mRNA was highly expressed. hAsc-1 gene was mapped to human chromosome 19, region q12-q13.1. 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. (C) 2000 Elsevier Science Ireland Ltd. All rights reserved.

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