| Popis: |
In previous studies, we isolated and identified a μ-calpain/PKCα complex from rabbit skeletal muscle. Here, we have used specific purification procedures in order to study the interactions between μ-calpain and PKC in mouse hippocampus, a brain structure implicated in memory processes. We observed that μ-calpain and conventional PKCs (α, βII and γ) are co-eluted after anion exchange chromatography. In contrast to our previous results obtained on skeletal muscle, μ-calpain and PKC isoenzymes were dissociated after gel filtration chromatography. Furthermore, μ-calpain induced the proteolytic conversion of PKCα, βII, and γ into PKMα, βII, and γ with a preferential hydrolysis of PKCγ, a specific isoenzyme of the nervous system. Although the μ-calpain/PKC interactions in the hippocampus are quite different from skeletal muscle, our results however, point out the functional importance of these inter-relations. Moreover, as PKCγ has been involved in the biochemical events underlying learning and memory, the preferential relationship between μ-calpain and PKCγ promotes the importance of the role that μ-calpain could play in the cellular mechanisms of memory formation. |
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