Phosphatidic acid activation of protein kinase C in LA-N-1 neuroblastoma cells

• Published in: Neuroscience letters Vol. 201; no. 3; pp. 199 - 202
• Main Authors: Lang, Dominique, Malviya, Anant N., Hubsch, Alphonse, Kanfer, Julian N., Freysz, Louis
• Format: Journal Article
• Language: English
• Published: Shannon Elsevier Ireland Ltd 15.12.1995; Elsevier
• Subjects: Binding, Competitive; Biological and medical sciences; Calcium - metabolism; Cell physiology; Cells, Cultured; Dose-Response Relationship, Drug; Fundamental and applied biological sciences. Psychology; Humans; Molecular and cellular biology; Neuroblastoma - metabolism; Neuroblastoma cells; Phorbol ester; Phosphatidic acid; Phosphatidic Acids - pharmacology; Phospholipases; Protein kinase C; Protein Kinase C - drug effects; Signal transduction; Time Factors; Protein kinase C; Phospholipases; Phorbol ester; Neuroblastoma cells; Phosphatidic acid; Signal transduction; Enzyme; Hydrolases; Esterases; Phosphoric diester hydrolases; Neuroblastoma; Phospholipase D
• ISSN: 0304-3940; 1872-7972
• DOI: 10.1016/0304-3940(95)12178-1

Phosphatidic acid (PA), a hydrolytic product of phospholipase D activity, stimulated cytosolic protein kinase C (PKC) activity when LA-N-1 neuroblastoma cells in culture were treated with PA, without translocating the enzyme to the membrane. Treatment of cells with 12- O-tetradecanoylphorbol-13-acetate (TPA) translocated and activated PKC in a dogmatic manner. Partially purified PKC activity derived from LA-N-1 neuroblastoma cells was stimulated by PA alone or in the presence of phosphatidylserine or TPA, without affecting [ 3H]phorbol dibutyrate binding, indicating that the site of action of PA was different from the phorbol ester or diacylglycerol binding site. These results suggest an unorthodox pattern of PKC stimulation mediated by PA which appears to be yet another mode of PA signal transduction.