Oxidation-induced persistent activation of protein kinase C in hippocampal homogenates

Elizabeth J. Palumbo, J. David Sweatt, Shu Jen Chen, Eric Klann

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1439-1445
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume187
Issue number3
DOIs
StatePublished - Sep 30 1992

Fingerprint

Protein Kinase C
Chemical activation
Oxidation
Enzymes
Enzyme Activation
Anions
Hippocampus
Lipids

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Oxidation-induced persistent activation of protein kinase C in hippocampal homogenates. / Palumbo, Elizabeth J.; David Sweatt, J.; Chen, Shu Jen; Klann, Eric.

In: Biochemical and Biophysical Research Communications, Vol. 187, No. 3, 30.09.1992, p. 1439-1445.

Research output: Contribution to journalArticle

Palumbo, Elizabeth J. ; David Sweatt, J. ; Chen, Shu Jen ; Klann, Eric. / Oxidation-induced persistent activation of protein kinase C in hippocampal homogenates. In: Biochemical and Biophysical Research Communications. 1992 ; Vol. 187, No. 3. pp. 1439-1445.
@article{195974ee0acb46be92da7ad21c090d82,
title = "Oxidation-induced persistent activation of protein kinase C in hippocampal homogenates",
abstract = "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.",
author = "Palumbo, {Elizabeth J.} and {David Sweatt}, J. and Chen, {Shu Jen} and Eric Klann",
year = "1992",
month = "9",
day = "30",
doi = "10.1016/0006-291X(92)90463-U",
language = "English (US)",
volume = "187",
pages = "1439--1445",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "3",

}

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

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.

UR - http://www.scopus.com/inward/record.url?scp=0026758133&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026758133&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(92)90463-U

DO - 10.1016/0006-291X(92)90463-U

M3 - Article

C2 - 1417820

AN - SCOPUS:0026758133

VL - 187

SP - 1439

EP - 1445

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -