2. Academic Validation
  3. Cloning and characterization of a human brain Na(+)-independent transporter for small neutral amino acids that transports D-serine with high affinity

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

  • Neurosci Lett. 2000 Jun 30;287(3):231-5. doi: 10.1016/s0304-3940(00)01169-1.
J Nakauchi 1,  H Matsuo,  D K Kim,  A Goto,  A Chairoungdua,  S H Cha,  J Inatomi,  Y Shiokawa,  K Yamaguchi,  I Saito,  H Endou,  Y Kanai
Affiliations

Affiliation

  • 1 Department of Neurosurgery, Kyorin University School of Medicine, Tokyo, Japan.
PMID: 10863037 DOI: 10.1016/s0304-3940(00)01169-1
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.

Figures