Compounds > 6-ketoprostaglandin-f1-alpha

6-ketoprostaglandin-f1-alpha and staurosporine-aglycone

6-ketoprostaglandin-f1-alpha has been researched along with staurosporine-aglycone* in 1 studies

Other Studies

1 other study(ies) available for 6-ketoprostaglandin-f1-alpha and staurosporine-aglycone

Article	Year
Effects of the protein kinase inhibitors, staurosporine and K-252a, on PGI2 production by rat liver cells (the C-9 cell line). Prostaglandins, 1990, Volume: 40, Issue:3 Staurosporine and K-252a, known inhibitors of several protein kinases, stimulated PGI2 production (measured as 6-keto-PGF1 alpha) in rat liver cells (the C-9 cell line). Preincubation of the rat liver cells with staurosporine or K-252a enhanced the PGI2 production stimulated by 12-O-tetradecanoylphorbol-13-acetate (TPA), platelet activating factor (PAF) and the Ca2(+)-ionophore A-23187, but not the PGI2 synthesis stimulated by exogenous arachidonic acid. These results suggest that phosphorylation of some proteins or certain amino acids on a protein can regulate arachidonic acid metabolism probably in the pathway leading to deesterification of phospholipids. Topics: 6-Ketoprostaglandin F1 alpha; Alkaloids; Animals; Calcimycin; Carbazoles; Cell Line; Drug Synergism; Epoprostenol; Indole Alkaloids; Liver; Platelet Activating Factor; Protein Kinase C; Radioimmunoassay; Rats; Staurosporine; Tetradecanoylphorbol Acetate	1990

Article

Year

Effects of the protein kinase inhibitors, staurosporine and K-252a, on PGI2 production by rat liver cells (the C-9 cell line).

Prostaglandins, 1990, Volume: 40, Issue:3

Staurosporine and K-252a, known inhibitors of several protein kinases, stimulated PGI2 production (measured as 6-keto-PGF1 alpha) in rat liver cells (the C-9 cell line). Preincubation of the rat liver cells with staurosporine or K-252a enhanced the PGI2 production stimulated by 12-O-tetradecanoylphorbol-13-acetate (TPA), platelet activating factor (PAF) and the Ca2(+)-ionophore A-23187, but not the PGI2 synthesis stimulated by exogenous arachidonic acid. These results suggest that phosphorylation of some proteins or certain amino acids on a protein can regulate arachidonic acid metabolism probably in the pathway leading to deesterification of phospholipids.

Topics: 6-Ketoprostaglandin F1 alpha; Alkaloids; Animals; Calcimycin; Carbazoles; Cell Line; Drug Synergism; Epoprostenol; Indole Alkaloids; Liver; Platelet Activating Factor; Protein Kinase C; Radioimmunoassay; Rats; Staurosporine; Tetradecanoylphorbol Acetate

1990