okadaic-acid and Carcinoma--Ehrlich-Tumor

Diacyl glycerols and phorbol esters, which activate protein kinases C, stimulated Ehrlich ascites tumor cell ferricyanide reductase activity. On the contrary, selective inhibition of active protein kinases C with bis-indolyl maleimide did not change the rate of ferricyanide reduction by Ehrlich cells. Selective inhibitors of phosphoprotein phosphatases, okadaic acid and cyclosporin A, also stimulated plasma membrane redox system. Taking all these data together, protein kinases or phosphoprotein phosphatases seemed to be involved in the multiple and complex regulation of Ehrlich cell plasma membrane redox system.

Topics: Animals; Carcinoma, Ehrlich Tumor; Cell Membrane; Cyclosporine; Enzyme Inhibitors; Ethers, Cyclic; NADH, NADPH Oxidoreductases; Okadaic Acid; Oxidation-Reduction; Phosphoprotein Phosphatases; Protein Kinase C; Tetradecanoylphorbol Acetate; Tumor Cells, Cultured