TY - JOUR
T1 - Oxidation-induced persistent activation of protein kinase C in hippocampal homogenates
AU - Palumbo, Elizabeth J.
AU - David Sweatt, J.
AU - Chen, Shu Jen
AU - Klann, Eric
N1 - Funding Information:
This laboratory has previously shown that persistent PKC activation is associated with the maintenance phase of LTP (15). Several mechanisms for this persistent activation have been postulated: membrane insertion of PKC (16), persistently elevated levels of a second messenger (17,18), proteolytic cleavage of PKC (6,15,19), or a protein kinase cascade (20). Another possible mechanism for the persistent activation of PKC is oxidative modification (21). In this study, we demonstrate that mild oxidation of hippocampal homogenates with Hz02 results in the * This work was supported by funds from the McKnight and Klingenstein Foundations (J.D.S.), an NM National Research Service Award (E.K.) and NIH grant MH48186 (J.D.S.).
PY - 1992/9/30
Y1 - 1992/9/30
N2 - 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.
AB - 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.
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U2 - 10.1016/0006-291X(92)90463-U
DO - 10.1016/0006-291X(92)90463-U
M3 - Article
C2 - 1417820
AN - SCOPUS:0026758133
SN - 0006-291X
VL - 187
SP - 1439
EP - 1445
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -