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Biophysical Journal 74: 230-241 (1998)
© 1998 the Biophysical Society
Biophys J, January 1998, p. 230-241, Vol. 74, No. 1
Departments of Medicine (Cardiology) and Physiology, University of Wisconsin, Madison, Wisconsin 53792 USA
We have established stably transfected HEK 293 cell lines
expressing high levels of functional human ether-a go-go-related gene
(HERG) channels. We used these cells to study biochemical characteristics of HERG protein, and to study electrophysiological and
pharmacological properties of HERG channel current at 35°C. HERG-transfected cells expressed an mRNA band at 4.0 kb. Western blot
analysis showed two protein bands (155 and 135 kDa) slightly larger
than the predicted molecular mass (127 kDa). Treatment with
N-glycosidase F converted both bands to smaller
molecular mass, suggesting that both are glycosylated, but at different levels. HERG current activated at voltages positive to 
50 mV, maximum
current was reached with depolarizing steps to 10 mV, and the current
amplitude declined at more positive voltages, similar to HERG channel
current expressed in other heterologous systems. Current density at
35°C, compared with 23°C, was increased by more than twofold to a
maximum of 53.4 ± 6.5 pA/pF. Activation, inactivation, recovery
from inactivation, and deactivation kinetics were rapid at 35°C, and
more closely resemble values reported for the rapidly activating
delayed rectifier K+ current
(IKr) at physiological temperatures. HERG
channels were highly selective for K+. When we used an
action potential clamp technique, HERG current activation began shortly
after the upstroke of the action potential waveform. HERG current
increased during repolarization to reach a maximum amplitude during
phases 2 and 3 of the cardiac action potential. HERG contributed
current throughout the return of the membrane to the resting potential,
and deactivation of HERG current could participate in phase 4 depolarization. HERG current was blocked by low concentrations of
E-4031 (IC50 7.7 nM), a value close to that reported for
IKr in native cardiac myocytes. Our data
support the postulate that HERG encodes a major constituent of
IKr and suggest that at physiological
temperatures HERG contributes current throughout most of the action
potential and into the postrepolarization period.
Biophys J, January 1998, p. 230-241, Vol. 74, No. 1
© 1998 by the Biophysical Society 0006-3495/98/01/230/12 $2.00
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