Addition of phosphatidylcholine-phospholipase C induces cellular redistribution and phosphorylation of protein kinase C zeta in C 6 glial cells.
Phosphatidylcholine breakdown has been shown to play a critical role in signal transduction involving generation of a number of second messengers [Exton, J.H., Biochim. Biophys. Acta, 1212 (1994) 26-42]. In the present report we demonstrate by immunofluorescence that short-treatment of C 6 glial cells with phosphatidylcholine-hydrolyzing phospholipase C (PC-PLC), changes the intracellular localization of protein kinase C (PKC) zeta from the cytoplasm to a perinuclear region. Western blot analysis also showed a redistribution of PKC zeta after incubation of cells with PC-PLC. To test whether these changes were accompanied by an activation of the enzyme, we measured the extent of phosphorylation of PKC zeta by immunoprecipitation from 32P-labelled cells. Short-treatment with PC-PLC resulted in enhanced phosphorylation of the higher Mr PKC zeta in C 6 glial cells.
Galve-Roperh
I
I
Departamento de Bioquímica y Biología Molecular I, Facultad de Químicas, Universidad Complutense, Madrid, Spain.
Malpartida
J M
JM
Haro
A
A
Diaz-Laviada
I
I
D000818:Animals; D009457:Neuroglia / Q000187:drug effects* / Q000378:metabolism; D010713:Phosphatidylcholines / Q000494:pharmacology*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D010738:Type C Phospholipases / Q000494:pharmacology*
D010713:Phosphatidylcholines; D011493:Protein Kinase C; D010738:Type C Phospholipases