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Cyclic AMP-stimulated protein kinase activity in rabbit peripheral myelin

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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.

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Author notes

  1. Vivian Zabrenetzky

    Present address: NICHD, Section on Nerve Growth Factors, NIH, 9000 Rockville Pike, Building 6, 1A02, 20205, Bethesda, Maryland

  2. Vivien Krygier-Brévart

    Present address: Pall Corporation, 30 Sea Cliff, 11542, Glen Cove, New York

Authors and Affiliations

  1. Institute of Neurotoxicology Departments of Neuroscience and Pathology Rose F. Kennedy Center for Research in Mental Retardation and Human Development, Albert Einstein College of Medicine, 10461, Bronx, New York

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

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  1. Vivian Zabrenetzky
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  2. Vivien Krygier-Brévart
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  3. Peter S. Spencer
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Zabrenetzky, V., Krygier-Brévart, V. & Spencer, P.S. Cyclic AMP-stimulated protein kinase activity in rabbit peripheral myelin. Neurochem Res 9, 121–132 (1984). https://doi.org/10.1007/BF00967664

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