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Multiple Forms and Distribution of Calcium/Calmodulin‐Stimulated Protein Kinase II in Brain
Author(s) -
Rostas John A. P.,
Dunkley Peter R.
Publication year - 1992
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1992.tb08428.x
Subject(s) - long term potentiation , calmodulin , protein kinase c , neuroscience , neurotransmission , synaptic plasticity , protein kinase a , biology , chemistry , enzyme , biochemistry , microbiology and biotechnology , receptor
In recent years, the enzyme Ca 2+ /calmodulin‐stimulated protein kinase II 1 (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).