Cyclic AMP-stimulated protein kinase activity in rabbit peripheral myelin

Vivian Zabrenetzky, Vivien Krygier-Brévart, Peter 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 1984
Externally publishedYes

Fingerprint

Myelin Sheath
Cyclic AMP
Protein Kinases
Rabbits
Myelin P2 Protein
Myelin Proteins
Phosphorylation
Egtazic Acid
Cyclic Nucleotides
Cyclic GMP
Phosphoric Diester Hydrolases
Enzyme activity
Enzymes
Theophylline
Suspensions
Phosphotransferases
Calcium
Proteins

ASJC Scopus subject areas

  • Neuroscience(all)
  • Biochemistry

Cite this

Cyclic AMP-stimulated protein kinase activity in rabbit peripheral myelin. / Zabrenetzky, Vivian; Krygier-Brévart, Vivien; Spencer, Peter.

In: Neurochemical Research, Vol. 9, No. 1, 01.1984, p. 121-132.

Research output: Contribution to journalArticle

Zabrenetzky, Vivian ; Krygier-Brévart, Vivien ; Spencer, Peter. / Cyclic AMP-stimulated protein kinase activity in rabbit peripheral myelin. In: Neurochemical Research. 1984 ; Vol. 9, No. 1. pp. 121-132.
@article{dc59b5dba52943fb95f27c8e51bc7c70,
title = "Cyclic AMP-stimulated protein kinase activity in rabbit peripheral myelin",
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.",
author = "Vivian Zabrenetzky and Vivien Krygier-Br{\'e}vart and Peter Spencer",
year = "1984",
month = "1",
doi = "10.1007/BF00967664",
language = "English (US)",
volume = "9",
pages = "121--132",
journal = "Neurochemical Research",
issn = "0364-3190",
publisher = "Springer New York",
number = "1",

}

TY - JOUR

T1 - Cyclic AMP-stimulated protein kinase activity in rabbit peripheral myelin

AU - Zabrenetzky, Vivian

AU - Krygier-Brévart, Vivien

AU - Spencer, Peter

PY - 1984/1

Y1 - 1984/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0021345750&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021345750&partnerID=8YFLogxK

U2 - 10.1007/BF00967664

DO - 10.1007/BF00967664

M3 - Article

C2 - 6325973

AN - SCOPUS:0021345750

VL - 9

SP - 121

EP - 132

JO - Neurochemical Research

JF - Neurochemical Research

SN - 0364-3190

IS - 1

ER -