Phorbol binding and enzymatic activity of protein kinase C from C3H 10T1/2 cells and relation to contact inhibition.
Protein kinase C (PKC) from membrane and cytosol fractions of fast growing as well as confluent contact-inhibited cells was assayed by two methods: PDBu binding and histone phosphorylation. In cytosol and membrane fractions of fast growing cells and in the cytosol fraction of confluent cells a reasonable agreement between the two methods was found. In membranes of confluent cells good PDBu binding was not accompanied with histone phosphorylation. Also in contact-inhibited cells, serum-stimulated hydrolysis of phosphatidylinositol bisphosphate (PIP2) was found to be reduced.
Miłoszewska
J
J
Department of Tumor Biology, M. Skłodowska-Curie Institute of Oncology, Warsaw.
Janik
P
P
Szaniawska
B
B
D000818:Animals; D002478:Cells, Cultured; D003260:Contact Inhibition; D005347:Fibroblasts / Q000201:enzymology; D007295:Inositol Phosphates / Q000378:metabolism*; D051379:Mice; D008809:Mice, Inbred C3H; D015240:Phorbol 12,13-Dibutyrate / Q000378:metabolism; D010703:Phorbol Esters / Q000378:metabolism*; D011493:Protein Kinase C / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000378:metabolism
D007295:Inositol Phosphates; D010703:Phorbol Esters; D015240:Phorbol 12,13-Dibutyrate; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate