Protein kinase C inactivation by Fenton's-reaction at discrete CU++ binding sites.
The consequence of direct exposure to HO. radical (chemically generated by Fenton's reaction) of partially purified rat liver PKC has been evaluated in this work. PKC inhibited Fenton-dependent HO. generation, probably due to the binding of copper ions to the enzyme. PKC activity was inhibited by H2O2. Copper ions were able to increase the H2O2-mediated damage to the enzyme, but only beyond a concentration threshold. The possible interactions between PKC and Fenton's reagents, in particular copper ions, is discussed.
Institute of General Pathology, University of Genoa, Italy.
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Traverso
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Ricciarelli
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Domenicotti
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Menini
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Pronzato
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Cottalasso
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UM
Marinari
D000818:Animals; D001665:Binding Sites; D003300:Copper / Q000378:metabolism* / Q000494:pharmacology; D006861:Hydrogen Peroxide / Q000494:pharmacology*; D017665:Hydroxyl Radical / Q000494:pharmacology; D015151:Immunoblotting; D007501:Iron / Q000494:pharmacology*; D007502:Iron Chelating Agents / Q000494:pharmacology; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D004369:Pentetic Acid / Q000494:pharmacology; D011493:Protein Kinase C / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000302:isolation & purification; D051381:Rats; D017208:Rats, Wistar
C045076:Fenton's reagent; D007502:Iron Chelating Agents; D017665:Hydroxyl Radical; D003300:Copper; D004369:Pentetic Acid; D006861:Hydrogen Peroxide; D007501:Iron; D011493:Protein Kinase C