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...
Gespeichert in:
| Hauptverfasser: | , , |
|---|---|
| Dokumenttyp: | Article (Journal) Editorial |
| Sprache: | Englisch |
| Veröffentlicht: |
October 26, 2015
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| In: |
ACS chemical neuroscience
Year: 2015, Jahrgang: 6, Heft: 12, Pages: 1906-1912 |
| ISSN: | 1948-7193 |
| DOI: | 10.1021/acschemneuro.5b00219 |
| Online-Zugang: | Verlag, Volltext: http://dx.doi.org/10.1021/acschemneuro.5b00219
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| Verfasserangaben: | Friederike Matthaeus, Patrick Schloss, and Thorsten Lau |
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| 520 | |a 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. | ||
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| 700 | 1 | |a Lau, Thorsten |e VerfasserIn |0 (DE-588)1141706628 |0 (DE-627)1000693643 |0 (DE-576)494472766 |4 aut | |
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