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Publication : Cloning and characterization of a brain-specific cationic amino acid transporter.

First Author  Hosokawa H Year  1997
Journal  J Biol Chem Volume  272
Issue  13 Pages  8717-22
PubMed ID  9079705 Mgi Jnum  J:39296
Mgi Id  MGI:86679 Doi  10.1074/jbc.272.13.8717
Citation  Hosokawa H, et al. (1997) Cloning and characterization of a brain-specific cationic amino acid transporter. J Biol Chem 272(13):8717-22
abstractText  rCAT3 (rat cationic amino acid transporter 3), a cDNA that encodes a novel member of the murine CAT family was isolated. The protein encoded by rCAT3 contained 619 amino acids, 53-58% of which were identical with those of the murine CAT family proteins previously described (mouse CAT1, CAT2a, CAT2b, and rat CAT1). Transient expression of rCAT3 and L-[14C]arginine incorporation experiments in COS7 cells verified a high affinity system y+ transporter activity of rCAT3. First, rCAT3-mediated L-[14C]arginine incorporation was time-dependent and saturable with half-saturation constant (Km) values of 103 +/- 12 &mgr;M (mean +/- S.E., n = 3). Second, the incorporation was specific for cationic amino acids as evidenced from the inhibition by L-arginine, L-lysine, and L-ornithine. Third, neither sodium nor chloride ions in the extracellular medium were required for the activity. Fourth, the incorporation was inhibited by high potassium-induced membrane depolarization. On Northern blot using RNAs from various rat tissues, the expression of rCAT3 mRNA was restricted to the brain. These results indicated a role of rCAT3 in the system y+ transporter activity in the nervous tissue.
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