Abstract
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 Km value of 22.8 μM. 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 Km 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.
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