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Molecular Pharmacology

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Research ArticleArticle

Regulation of N-Methyl-d-Aspartate Receptor Function by Constitutively Active Protein Kinase C

Zhi-Gang Xiong, Ramin Raouf, Wei-Yang Lu, Lu-Yang Wang, Beverley A. Orser, Ellen M. Dudek, Michael D. Browning and John F. MacDonald
Molecular Pharmacology December 1998, 54 (6) 1055-1063; DOI: https://doi.org/10.1124/mol.54.6.1055
Zhi-Gang Xiong
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Ramin Raouf
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Wei-Yang Lu
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Lu-Yang Wang
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Beverley A. Orser
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Ellen M. Dudek
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Michael D. Browning
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John F. MacDonald
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Abstract

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.

Footnotes

    • Received April 30, 1998.
    • Accepted August 14, 1998.
  • Send reprint requests to: Dr. John F. MacDonald, Department of Physiology and Pharmacology, Medical Sciences Building, 1 King’s College Circle, University of Toronto, Toronto, Ontario, M5S 1A8. E-mail: j.macdonald{at}utoronto.ca

  • This work was supported by grants to J.F.M. from the Medical Research Council of Canada and by grants to M.D.B. from the National Institutes of Health (AA09675, AA03527, MH44212, and AG04418). Z.-G.X. is a Fellow of the Medical Research Council, and W.-Y.L. is a Fellow of the Networks of Centers of Excellence. Z.-G.X., R.R., and W.-Y.L. contributed equally to this work.

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Molecular Pharmacology: 54 (6)
Molecular Pharmacology
Vol. 54, Issue 6
1 Dec 1998
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Research ArticleArticle

Regulation of N-Methyl-d-Aspartate Receptor Function by Constitutively Active Protein Kinase C

Zhi-Gang Xiong, Ramin Raouf, Wei-Yang Lu, Lu-Yang Wang, Beverley A. Orser, Ellen M. Dudek, Michael D. Browning and John F. MacDonald
Molecular Pharmacology December 1, 1998, 54 (6) 1055-1063; DOI: https://doi.org/10.1124/mol.54.6.1055

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Research ArticleArticle

Regulation of N-Methyl-d-Aspartate Receptor Function by Constitutively Active Protein Kinase C

Zhi-Gang Xiong, Ramin Raouf, Wei-Yang Lu, Lu-Yang Wang, Beverley A. Orser, Ellen M. Dudek, Michael D. Browning and John F. MacDonald
Molecular Pharmacology December 1, 1998, 54 (6) 1055-1063; DOI: https://doi.org/10.1124/mol.54.6.1055
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