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Journal of Neuroscience, Vol 16, 36-45, Copyright © 1996 by Society for Neuroscience
Metabotropic glutamate receptor modulation of voltage-gated Ca2+ channels involves multiple receptor subtypes in cortical neurons
S Choi and DM Lovinger
Department of Molecular Physiology and Biophysics, Vanderbilt University Medical School, Nashville, Tennessee 37232, USA.
Metabotropic glutamate receptor (mGluR) modulation of voltage-gated Ca2+
channels was examined in isolated deep layer frontoparietal cortical
neurons under conditions designed to isolate calcium- independent
modulatory pathways. Trans-1-aminocyclopentane-1,3- dicarboxylate (t-ACPD),
a nonspecific mGluR agonist, produced rapid and reversible inhibition of
Ca2+ channels. This effect was mimicked by agonists for group I and group
II, but not group III, mGluRs. Effects of group I and II agonists often
were observed in the same neurons, but separate subgroups of neurons were
unresponsive to the group I agonist quisqualate or the group II agonist
2-(2,3-dicarboxycyclopropyl) glycine (DCG-IV). Inhibition by quisqualate
and DCG-IV was nonocclusive in neurons responding to both agonists. These
agonists thus appear to act on different mGluRs. The mGluR antagonist
alpha-methyl-4- carboxylphenylglycine attenuated inhibition by t-ACPD,
quisqualate, and DCG-IV. Inhibition by quisqualate and DCG-IV was
voltage-dependent. Although the effects of both agonists were greatly
reduced by N- ethylmaleimide (NEM), inhibition by DCG-IV was more sensitive
to NEM than inhibition by quisqualate. t-ACPD-induced inhibition was
reduced by omega-conotoxin GVIA (omega-CgTx) and omega-agatoxin IVA (omega-
AgTx) but was affected little by nifedipine. Inhibition by DCG-IV and
quisqualate also was reduced by omega-CgTx. We conclude that multiple mGluR
subtypes inhibit Ca2+ channels in cortical neurons and that N- and possibly
P-type channels are inhibited. Modulation is via a rapid- onset,
voltage-dependent mechanism that likely involves a pertussis toxin
(PTX)-sensitive G-protein. Type I mGluRs may work via additional
PTX-insensitive pathways.
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