Dataset Information


Pharmacological characterization of a high-affinity p-tyramine transporter in rat brain synaptosomes.

ABSTRACT: p-Tyramine is an archetypal member of the endogenous family of monoamines known as trace amines, and is one of the endogenous agonists for trace amine-associated receptor (TAAR)1. While much work has focused on the function of TAAR1, very little is known about the regulation of the endogenous agonists. We have previously reported that p-tyramine readily crosses lipid bilayers and that its release from synaptosomes is non-exocytotic. Such release, however, showed characteristics of modification by one or more transporters. Here we provide the first characterization of such a transporter. Using frontal cortical and striatal synaptosomes we show that p-tyramine passage across synaptosome membranes is not modified by selective inhibition of either the dopamine, noradrenaline or 5-HT transporters. In contrast, inhibition of uptake-2 transporters significantly slowed p-tyramine re-uptake. Using inhibitors of varying selectivity, we identify Organic Cation Transporter 2 (OCT2; SLC22A2) as mediating high affinity uptake of p-tyramine at physiologically relevant concentrations. Further, we confirm the presence of OCT2 protein in synaptosomes. These results provide the first identification of a high affinity neuronal transporter for p-tyramine, and also confirm the recently described localization of OCT2 in pre-synaptic terminals.


PROVIDER: S-EPMC5128819 | BioStudies | 2016-01-01T00:00:00Z

REPOSITORIES: biostudies

Similar Datasets

2009-01-01 | S-EPMC2677188 | BioStudies
2006-01-01 | S-EPMC2014643 | BioStudies
2013-01-01 | S-EPMC3594682 | BioStudies
2011-01-01 | S-EPMC3205048 | BioStudies
2017-01-01 | S-EPMC6328375 | BioStudies
2005-01-01 | S-EPMC1190334 | BioStudies
2014-01-01 | S-EPMC4224135 | BioStudies
2014-01-01 | S-EPMC4120670 | BioStudies
2017-01-01 | S-EPMC6580852 | BioStudies
2010-01-01 | S-EPMC2814896 | BioStudies