Modulation of cytosolic protein kinase C activity by ferricyanide: priming event seems transmembrane redox signalling: A study on transformed C3H/10T1/2 cells in culture

• Published in: FEBS letters 1986-05, Vol.200 (2), p.265-270
• Main Authors: Malviya, A.N., Anglard, P.
• Format: Article
• Language: English
• Subjects: Animals; antiport; Antiporters; Biological and medical sciences; Carrier Proteins - analysis; Cell Membrane - metabolism; Cell physiology; Cells, Cultured; Cytosol - enzymology; Edetic Acid - pharmacology; Ferricyanides - pharmacology; Fundamental and applied biological sciences. Psychology; Hydrogen-Ion Concentration; Molecular and cellular biology; Ouabain - pharmacology; Oxidation-Reduction; Potassium - metabolism; protein kinase C; Protein Kinase C - metabolism; Protein kinase CTumor promotionTransformed cellTransmembrane signalingFerricyanideNa +/H + antiporter; Protons; Responses to growth factors, tumor promotors, other factors; sodium; Sodium - metabolism; transformed cells
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(86)81149-8

Transformed 3T3/10T1/2 cultured cells incubated with ferricyanide caused a decrease of 2 mM EDTA extractable cytosolic protein kinase C activity in 2 min, whereas 5 or 20 min ferricyanide treatment reverted the enzyme activity to that observed without ferricyanide. The ferricyanide effect in 2 min was abolished by amiloride and sustained by ouabain. Thus, deactivation-activation of cytosolic protein kinase C is attributed to an unknown signal generation during H + accumulation coupled with the Na +/H + exchange phase. In this mechanism the priming event concerns the transmembrane redox process shedding H + into the cell interior while impermeant ferricyanide acts as a unique electron acceptor.