Activation of Ca2+/calmodulin-dependent protein kinase I in cultured rat hippocampal neurons

Akiyoshi Uezu, Kohji Fukunaga, Jiro Kasahara, Eishichi Miyamoto

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)


We have focused on activation mechanisms of calcium/calmodulin-dependent protein kinase (CaM) kinase I in the hippocampal neurons and compared them with that of CaM kinase IV. Increased activation of CaM kinase I occurred by stimulation with glutamate and depolarization in cultured rat hippocampal neurons. Similar to CaM kinases II and IV, CaM kinase I was essentially activated by stimulation with the NMDA receptor. Although both CaM kinases I and IV seem to be activated by CaM kinase kinase, the activation of CaM kinase I was persistent during stimulation with glutamate in contrast to a transient activation of CaM kinase IV. In addition, CaM kinase I was activated in a lower concentration of glutamate than that of CaM kinase IV. Depolarization-induced activation of CaM kinase I was also evident in the cultured neurons and was largely blocked by nifedipine. In the experiment with 32P-labeled cells, phosphorylation of CaM kinase I was stimulated by glutamate treatment and depolarization. The glutamate- and depolarization-induced phosphorylation was inhibited by the NMDA receptor antagonist and nifedipine, respectively. These results suggest that, although CaM kinases I and IV are activated by the NMDA receptor and depolarization stimulation, these kinase activities are differently regulated in the hippocampal neurons.

Original languageEnglish
Pages (from-to)585-593
Number of pages9
JournalJournal of Neurochemistry
Issue number3
Publication statusPublished - 2002 Aug 12
Externally publishedYes


  • CaM kinase I
  • CaM kinase IV
  • Depolarization
  • Glutamate
  • Hippocampal neurons

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience


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