Oxidation-induced persistent activation of protein kinase C in hippocampal homogenates.
Incubation of purified protein kinase C with H2O2 results in the generation of a persistently activated form of the enzyme which is no longer dependent on Ca2+ or lipid cofactors. This oxidative activation of purified protein kinase C requires added Fe2+ in the incubation medium. Treatment of the soluble fraction of hippocampal homogenates with H2O2 also leads to persistent activation of protein kinase C; however, oxidative activation of protein kinase C under these conditions does not require the addition of Fe2+. The persistently activated form of protein kinase C appears as a novel peak of activity on DE52 anion exchange columns, suggesting a modification of the charge character of the enzyme. Thus, oxidative modification of protein kinase C can result in its persistent activation, and this mechanism may constitute a pathway for physiological activation of the enzyme in the hippocampus.
Palumbo
E J
EJ
Division of Neuroscience, Baylor College of Medicine, Houston, TX 77030.
Sweatt
J D
JD
Chen
S J
SJ
Klann
E
E
D000818:Animals; D004789:Enzyme Activation / Q000187:drug effects; D005296:Ferrous Compounds / Q000378:metabolism; D006624:Hippocampus / Q000201:enzymology*; D006861:Hydrogen Peroxide / Q000494:pharmacology; D009473:Neuronal Plasticity; D010084:Oxidation-Reduction; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats
D005296:Ferrous Compounds; D006861:Hydrogen Peroxide; D011493:Protein Kinase C