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Effects of protein kinase C and phosphoprotein phosphatase modulators on Ehrlich cell plasma membrane redox system activity.

Abstract
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.
AuthorsA del Castillo-Olivares, A Esteban del Valle, J Márquez, I Núñez de Castro, M A Medina
JournalBiochimica et biophysica acta (Biochim Biophys Acta) Vol. 1313 Issue 2 Pg. 157-60 (Aug 28 1996) ISSN: 0006-3002 [Print] Netherlands
PMID8781563 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Enzyme Inhibitors
  • Ethers, Cyclic
  • Okadaic Acid
  • Cyclosporine
  • NADH, NADPH Oxidoreductases
  • ferricyanide reductase
  • Protein Kinase C
  • Phosphoprotein Phosphatases
  • Tetradecanoylphorbol Acetate
Topics
  • Animals
  • Carcinoma, Ehrlich Tumor
  • Cell Membrane (metabolism)
  • Cyclosporine (pharmacology)
  • Enzyme Inhibitors (pharmacology)
  • Ethers, Cyclic (pharmacology)
  • NADH, NADPH Oxidoreductases (metabolism)
  • Okadaic Acid
  • Oxidation-Reduction
  • Phosphoprotein Phosphatases (antagonists & inhibitors, metabolism)
  • Protein Kinase C (antagonists & inhibitors, physiology)
  • Tetradecanoylphorbol Acetate (pharmacology)
  • Tumor Cells, Cultured

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