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- W2041003411 abstract "Incubation of the acutely dissected rat hippocampal slices in calcium-containing media resulted in spontaneous activation-translocation of classical PKC isoforms and their subsequent (especially gamma-type) proteolytic degradation. These changes were blocked by calpain inhibitor MDL 28 170 in 100 microM concentration. Rat hippocampal slices were metabolically prelabelled with 32Pi and stimulated with NMDA/glycine, depolarization or phorbol dibutyrate (PDBu) treatment. The basal phosphorylation of specific PKC substrates (MARCKS, neuromodulin and neurogranin) was significantly reduced in non-stimulated slices by MDL pretreatment. In contrast, only the slices where calpain activity was inhibited responded to further NMDA or phorbol dibutyrate stimulation by a substantial increase of PKC-dependent protein phosphorylation. It is concluded that the PKC phosphorylation system is severely affected by non-specific activation and a subsequent, calpain-dependent proteolysis in the acutely prepared hippocampal slices. Calpain inhibition by 100 microM MDL partially prevented these changes and increased stimulus-dependent phosphorylation of PKC-specific protein substrates." @default.
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- W2041003411 date "1998-01-01" @default.
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- W2041003411 title "Phosphorylation of protein kinase C substrate proteins in rat hippocampal slices--effect of calpain inhibition." @default.
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