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Brain Res Mol Brain Res. 1999 Jun 18;70(1):101-15.

Characterization of multiple forms of the human glycine transporter type-2.

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  • 1Discovery Research, Gliatech, 23420 Commerce Park Rd., Cleveland, OH 44122, USA.


The human glycine transporter type 2 (hGlyT2) was cloned from a spinal cord cDNA library using PCR-based methodologies. The isolated sequence exhibits 89% homology with the previously isolated rat GlyT2 cDNA (Liu et al., J. Biol. Chem. 268 (1993) 22802-22808) at the nucleotide level, and 93% amino acid sequence identity. The greatest divergence between the human and rat sequences is found at the amino-terminus, where only 74% amino acid identity exists in residues 1-190. Expression of the intact hGlyT2 transporter sequence in COS-7 cells resulted in a 10-fold increase in high-affinity uptake relative to control cells transfected with vector alone. An artificially truncated form of the transporter, missing the NH2-terminal 153 amino acids, was also capable of mediating glycine uptake. However, an identified variant lacking the first 234 amino acids was non-functional. An hGlyT2 transporter containing a 14-residue deletion in the intracellular loop between transmembrane domains 6 and 7 was also identified and expressed, but failed to mediate glycine uptake. Like rat GlyT2, the high-affinity uptake mediated by hGlyT2 was found to be insensitive to the GlyT1 inhibitor sarcosine.

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