Multiple Forms and Distribution of Calcium/Calmodulin-Stimulated Protein Kinase II in Brain

Authors

  • John A. P. Rostas,

    Corresponding author
    1. The Neuroscience Group, Faculty of Medicine, University of Newcastle, New South Wales, Australia
      Address correspondence and reprint requests to Dr. J. A. P. Rostas at The Neuroscience Group, Faculty of Medicine, University of Newcastle, University Drive, Callaghan, New South Wales, Australia 2308.
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  • Peter R. Dunkley

    1. The Neuroscience Group, Faculty of Medicine, University of Newcastle, New South Wales, Australia
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Address correspondence and reprint requests to Dr. J. A. P. Rostas at The Neuroscience Group, Faculty of Medicine, University of Newcastle, University Drive, Callaghan, New South Wales, Australia 2308.

Abstract

In recent years, the enzyme Ca2+/calmodulin-stimulated protein kinase II1 (CaM-PK II) as attracted a great deal of interest. CaM-PK II is the most abundant calmodulin-stimulated protein kinase in brain, where it is particularly enriched in neurons (Ouimet et al., 1984; Erondu and Kennedy, 1985; Lin et al., 1987; Scholz et al., 1988). Neuronal CaM-PK II has been suggested to be involved in several phenomena associated with synaptic plasticity (Lisman and Goldring, 1988; Kelly, 1992), including long-term potentiation (Malinow et al., 1988; Malenka et al.,1989), neurotransmission (Nichols et al., 1990; Siekevitz, 1991), and learning (for review, see Rostas, 1991). This enzyme has also been postulated to be selectively vulnerable in several pathological condition, including epilepsy/kindling (Bronstein et al.,1990; Wu et al., 1990), cerebral ischemia (Taft et al., 1988), and organophosphorus toxicity (Abou-Donia and Lapadula, 1990).

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