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XB-ART-10807
Neurosci Lett. June 30, 2000; 287 (3): 231-5.

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 DK , Goto A , Chairoungdua A , Cha SH , Inatomi J , Shiokawa Y , Yamaguchi K , Saito I , Endou H , Kanai Y .


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 K(m) value of 22.8 microM. 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.

PubMed ID: 10863037
Article link: Neurosci Lett.

Genes referenced: pycard slc3a2 sts
Antibodies referenced:

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