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1 Acta Neurobiologiae Experimentalis

1 1998

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Phosphorylation of Protein Kinase C substrate proteins in rat hippocampal slices - effect of calpain inhibition

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Domanska-Janik K. , Zablocka B. , Zalewska T. , Zajac H.

1998

tom 58

nr 4

247-252

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 g- type) proteolytic degradation. These changes were blocked by calpain inhibitor MDL 28 170 in 100 mM 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 mM MDL partially prevented these changes and increased stimulus-dependent phosphorylation of PKC-specific protein substrates.