Rat cerebellar slices were incubated in absence and presence of N-methyl-D-aspartate and then used to prepare a purified nuclear fraction. The purity of the nuclear fraction was assessed by electron microscopy and measurements of Na+, K(+)-ATPase activity. The presence of protein kinase C in nuclear fractions was measured by [3H]phorbol dibutyrate binding. Treatment of cerebellar slices with N-methyl-D-aspartate caused a significant, two-fold increase in the density of nuclear [3H]phorbol dibutyrate binding sites, indicating the translocation of protein kinase C to the nuclear fraction. The effect of N-methyl-D-aspartate was prevented by the presence of the N-methyl-D-aspartate receptor antagonist (+)5-methyl-10,11-dihydro-5H-dibenzocyclohepten-5,10-imine maleate (MK-801). These results suggest a possible role for protein kinase C in mediating N-methyl-D-aspartate-induced nuclear events.
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