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1 Institute of Applied Physiology, University Hospital Hamburg-Eppendorf, University of Hamburg, Martinistr. 52, D-20246 Hamburg, Germany
2 Center for Molecular Neurobiology, ZMNH, University of Hamburg, Falkenried 94, D-20251 Hamburg, Germany
Ether-à-go-go-related gene (erg) channels form one subfamily of the ether-à-go-go (EAG) K+ channels and all three erg channels (erg1–3) are expressed in the brain. In the present study we characterize a fast erg current in neurones in primary culture derived from the median part of rat embryonic rhombencephala (E15–16). The relatively uniform erg current was regularly found in large multipolar serotonergic neurones, and occurred also in other less well characterized neurones. The erg current was blocked by the antiarrhythmic substance E-4031. Single-cell RT-PCR revealed the expression of erg1a, erg1b, erg2 and erg3 mRNA in different combinations in large multipolar neurones. These cells also contained neuronal tryptophan hydroxylase, a key enzyme for serotonin production. To characterize the molecular properties of the channels mediating the native erg current, we compared the voltage and time dependence of activation and deactivation of the neuronal erg current to erg1a, erg1b, erg2 and erg3 currents heterologously expressed in CHO cells. The biophysical properties of the neuronal erg current were well within the range displayed by the different heterologously expressed erg currents. Activation and deactivation kinetics of the neuronal erg current were fast and resembled those of erg3 currents. Our data suggest that the erg channels in rat embryonic rhombencephalon neurones are heteromultimers formed by different erg channel subunits.
(Received 24 December 2004;
accepted after revision 26 January 2005;
first published online 27 January 2005)
Corresponding author J. R. Schwarz: Institute of Applied Physiology, University Hospital Hamburg-Eppendorf, Martinistr. 52, D-20246 Hamburg, Germany. Email: schwarz{at}uke.uni-hamburg.de
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