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Vol. 54, Issue 6, 1055-1063, December 1998
Departments of
Physiology and Pharmacology (Z.-G.X., R.R., W.-Y.L.,
L.-Y.W., B.A.O., J.F.M.) and
Department of Anesthesia (B.A.O.),
University of Toronto, Toronto, Ontario, Canada, M5S 1A8, and
Department of Pharmacology, Program in Neuroscience, University of
Colorado Health Science Center, University of Colorado, Denver,
Colorado 80262 (E.M.D.)
The ability of the constitutively active fragment of protein kinase C
(PKM) to modulate N-methyl-D-aspartate
(NMDA)-activated currents in cultured mouse hippocampal neurons and
acutely isolated CA1 hippocampal neurons from postnatal rats was
studied using patch-clamp techniques. The responses of two
heterodimeric combinations of recombinant NMDA receptors (NR1a/NR2A and
NR1a/NR2B) expressed in human embryonic kidney 293 cells were also
examined. Intracellular applications of PKM potentiated NMDA-evoked
currents in cultured and isolated CA1 hippocampal neurons. This
potentiation was observed in the absence or presence of extracellular
Ca2+ and was prevented by the coapplication of the
inhibitory peptide protein kinase inhibitor(19-36). Furthermore, the
PKM-induced potentiation was not a consequence of a reduction in the
sensitivity of the currents to voltage-dependent blockade by
extracellular Mg2+. We also found different sensitivities
of the responses of recombinant NMDA receptors to the intracellular
application of PKM. Some potentiation was observed with the NR1a/NR2A
subunits, but none was observed with the NR1a/NR2B combination.
Applications of PKM to inside-out patches taken from cultured neurons
increased the probability of channel opening without changing
single-channel current amplitudes or channel open times. Thus, the
activation of protein kinase C is associated with potentiation of NMDA
receptor function in hippocampal neurons largely through an increase in
the probability of channel opening.
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