Cyclic AMP-stimulated protein kinase activity in rabbit peripheral myelin

Vivian Zabrenetzky, Vivien Krygier-Brévart, Peter S. Spencer

Research output: Contribution to journalArticle

Abstract

Cyclic AMP-sensitive protein kinase activity has been found in suspensions of purified rabbit peripheral myelin. The enzyme phosphorylated the P0, "Y", X, P1, and P2 myelin proteins. Kinase activity, which was maximal at physiological pH, 2.5 mM Mg2+, and 2 νM cAMP, was stimulated three-fold over basal levels by cyclic AMP. Addition of calcium or EGTA had no effect on the enzyme activity in the presence or absence of cyclic AMP. Cyclic GMP also did not stimulated endogenous or exogenous protein phosphorylation. Theophylline, an inhibitor of 3′,5′-cyclic nucleotide phosphodiesterase activity, increased protein kinase activity in the presence of cyclic AMP. These data show that PNS myelin proteins can be phosphorylated in situ by a protein kinase system whose activity is stimulated selectively by cyclic AMP.

Original languageEnglish (US)
Pages (from-to)121-132
Number of pages12
JournalNeurochemical Research
Volume9
Issue number1
DOIs
StatePublished - Jan 1 1984

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

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