Physiological evidence that d -aspartate activates a current distinct from ionotropic glutamate receptor currents in Aplysia californica neurons
Author(s) -
Stephen L. Carlson,
Lynne A. Fieber
Publication year - 2011
Publication title -
journal of neurophysiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.302
H-Index - 245
eISSN - 1522-1598
pISSN - 0022-3077
DOI - 10.1152/jn.00403.2011
Subject(s) - aplysia , ionotropic effect , glutamate receptor , excitatory postsynaptic potential , nmda receptor , receptor , neuroscience , biophysics , chemistry , voltage clamp , patch clamp , ion channel , neurotransmission , biology , electrophysiology , microbiology and biotechnology , biochemistry
D-Aspartate (D-Asp) activates an excitatory current in neurons of Aplysia californica. Although D-Asp is presumed to activate a subset of L-glutamate (L-Glu) channels, the identities of putative d-Asp receptors and channels are unclear. Whole cell voltage- and current-clamp studies using primary cultures of Aplysia buccal S cluster (BSC) neurons were executed to characterize D-Asp-activated ion channels. Both D-Asp and L-Glu evoked currents with similar current-voltage relationships, amplitudes, and relatively slow time courses of activation and inactivation when agonists were pressure applied. D-Asp-induced currents, however, were faster and desensitized longer, requiring 40 s to return to full amplitude. Of cells exposed to both agonists, 25% had D-Asp- but not L-Glu-induced currents, suggesting a receptor for D-Asp that was independent of l-Glu receptors. D-Asp channels were permeable to Na(+) and K(+), but not Ca²⁺, and were vulnerable to voltage-dependent Mg²⁺ block similarly to vertebrate NMDA receptor (NMDAR) channels. d-Asp may activate both NMDARs and non-l-Glu receptors in the nervous system of Aplysia.
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