Differential uptake mechanisms of fluorescent substrates into stem-cell-derived serotonergic neurons

The actions of the neurotransmitters serotonin, dopamine, and norepinephrine are partly terminated by diffusion and in part by their uptake into neurons via the selective, high-affinity transporters for serotonin (SERT), dopamine (DAT), and norepinephrine (NET), respectively. There is also growing e...

Full description

Saved in:
Bibliographic Details
Main Authors: Matthäus, Friederike (Author) , Schloss, Patrick (Author) , Lau, Thorsten (Author)
Format: Article (Journal) Editorial
Language:English
Published: October 26, 2015
In: ACS chemical neuroscience
Year: 2015, Volume: 6, Issue: 12, Pages: 1906-1912
ISSN:1948-7193
DOI:10.1021/acschemneuro.5b00219
Online Access:Verlag, Volltext: http://dx.doi.org/10.1021/acschemneuro.5b00219
Get full text
Author Notes:Friederike Matthaeus, Patrick Schloss, and Thorsten Lau
Description
Summary:The actions of the neurotransmitters serotonin, dopamine, and norepinephrine are partly terminated by diffusion and in part by their uptake into neurons via the selective, high-affinity transporters for serotonin (SERT), dopamine (DAT), and norepinephrine (NET), respectively. There is also growing evidence that all three monoamines are taken up into neurons by low-affinity, high-capacity organic cation transporters (OCT) and the plasma membrane monoamine transporter (PMAT). Pharmacological characterization of these low-affinity recombinant transporter proteins in heterologous expression systems has revealed that they are not antagonized by classical inhibitors of SERT, DAT, or NET but that decynium-22 (D22) antagonizes OCT3 and PMAT, whereas corticosterone and progesterone selectively inhibit OCT3. Here, we show that SERT, PMAT, and OCT3, but not OCT1 and OCT2, are coexpressed in murine stem cell-derived serotonergic neurons. Using selective antagonists, we provide evidence that uptake of the fluorescent substrates FFN511, ASP+, and 5-HT into stem cell-derived serotonergic neurons is mediated differentially by these transporters and also involves an as yet unknown transport mechanism.
Item Description:Gesehen am 17.10.2017
Physical Description:Online Resource
ISSN:1948-7193
DOI:10.1021/acschemneuro.5b00219