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 language | English (US) |
|---|---|
| Pages (from-to) | 121-132 |
| Number of pages | 12 |
| Journal | Neurochemical Research |
| Volume | 9 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 1984 |
| Externally published | Yes |
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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 journal › Article
}
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.
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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 -