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The Journal of Neurophysiology Vol. 85 No. 2 February 2001, pp. 816-827
Copyright ©2001 by the American Physiological Society
1D, CaV1.3)
Voltage-Dependent Calcium Currents
1Department of Pharmacology, University College London, London WC1E 6BT, United Kingdom; 2Merck Research Laboratories, La Jolla, California 92307; 3Abteilung Pharmakologie und Toxikologie, Universität Ulm and Institut für Pharmakologie, Freie Universität, D-14195 Berlin, Germany; and 4Merck, Sharp and Dohme, Neuroscience Research Centre, Harlow CM20 2QR, United Kingdom
Bell, D. C.,
A.
J. Butcher,
N. S. Berrow,
K. M. Page,
P. F. Brust,
A. Nesterova,
K. A. Stauderman,
G. R. Seabrook,
B. Nürnberg, and
A. C. Dolphin.
Biophysical Properties, Pharmacology, and Modulation of
Human, Neuronal L-Type (1D, CaV1.3)
Voltage-Dependent Calcium Currents. J. Neurophysiol. 85: 816-827, 2001. Voltage-dependent calcium channels
(VDCCs) are multimeric complexes composed of a pore-forming
1 subunit together with several accessory
subunits, including 2
, 
, and, in some
cases, 
subunits. A family of VDCCs known as the L-type channels are
formed specifically from 1S (skeletal muscle),
1C (in heart and brain),
1D (mainly in brain, heart, and endocrine
tissue), and 1F (retina). Neuroendocrine L-type currents have a significant role in the control of
neurosecretion and can be inhibited by GTP-binding (G-) proteins.
However, the subunit composition of the VDCCs underlying these
G-protein-regulated neuroendocrine L-type currents is unknown. To
investigate the biophysical and pharmacological properties and role of
G-protein modulation of 1D calcium channels,
we have examined calcium channel currents formed by the human neuronal
L-type 1D subunit, co-expressed with
2-1 and 3a, stably
expressed in a human embryonic kidney (HEK) 293 cell line, using whole
cell and perforated patch-clamp techniques. The
1D-expressing cell line exhibited L-type
currents with typical characteristics. The currents were high-voltage
activated (peak at +20 mV in 20 mM Ba2+) and
showed little inactivation in external Ba2+,
while displaying rapid inactivation kinetics in external
Ca2+. The L-type currents were inhibited by the
1,4 dihydropyridine (DHP) antagonists nifedipine and nicardipine and
were enhanced by the DHP agonist BayK S-(
)8644. However,
1D L-type currents were not modulated by
activation of a number of G-protein pathways. Activation of endogenous
somatostatin receptor subtype 2 (sst2) by somatostatin-14 or activation
of transiently transfected rat D2 dopamine receptors
(rD2long) by quinpirole had no effect. Direct activation of G-proteins by the nonhydrolyzable GTP analogue, guanosine
5'-0-(3-thiotriphospate) also had no effect on the
1D currents. In contrast, in the same system,
N-type currents, formed from transiently transfected
1B/2-1/3,
showed strong G-protein-mediated inhibition. Furthermore, the I-II
loop from the 1D clone, expressed as a
glutathione-S-transferase (GST) fusion protein, did not bind G, unlike the 1B I-II loop fusion
protein. These data show that the biophysical and pharmacological
properties of recombinant human 1D L-type
currents are similar to 1C currents, and
these currents are also resistant to modulation by
Gi/o-linked G-protein-coupled receptors.
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