Activation of Ca2+/calmodulin-dependent protein kinase II and protein kinase C by glutamate in cultured rat hippocampal neurons

K. Fukunaga, T. R. Soderling, E. Miyamoto

Research output: Contribution to journalArticlepeer-review

176 Citations (Scopus)

Abstract

In cultured rat hippocampal neurons, glutamate elevated the Ca2+- independent activity of Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) through autophosphorylation when the neurons were incubated in Mg2+-free buffer, and this response was blocked by specific antagonists of the N-methyl-D-aspartate (NMDA) receptor. In addition, glutamate stimulated the transient translocation of protein kinase C (PKC) from the cytosol to the membrane fraction. This effect was not blocked by NMDA receptor antagonists but was partially blocked by DL-2-amino-3-phosphonopropionate. Quisqualate or trans-1-amoinocyclopentane-trans1,3-dicarboxylate produced a similar effect on the translocation of PKC. In the experiments with 32P-labeled cells, the phosphorylation of microtuble-associated protein 2 and synapsin I, as well as autophosphorylation of CaM kinase II, were found to be stimulated by exposure to glutamate. These results suggest that glutamate can activate CaM kinase II through the ionotropic NMDA receptor, which in turn increases the phosphorylation of microtuble-associated protein 2 and synapsin I. PKC was activated through the metabotropic glutamate receptor in the hippocampal neurons.

Original languageEnglish
Pages (from-to)22527-22533
Number of pages7
JournalJournal of Biological Chemistry
Volume267
Issue number31
Publication statusPublished - 1992
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Activation of Ca<sup>2+</sup>/calmodulin-dependent protein kinase II and protein kinase C by glutamate in cultured rat hippocampal neurons'. Together they form a unique fingerprint.

Cite this