The Role of Phosphoprotein B-50 in Phosphoinositide Metabolism in Brain Synaptic Plasma Membranes

  • W. H. Gispen
  • C. J. Van Dongen
  • P. N. E. De Graan
  • A. B. Oestreicher
  • H. Zwiers
Part of the Experimental Biology and Medicine book series (EBAM, volume 6)


In rat brain synaptic plasma membranes there is a \(C{{a}^{{{{2}^{ + }}}}}\)-dependent, cyclic nucleotide-independent protein kinase that is inhibited by ACTH1–24. Evidence suggests that this protein kinase is very similar to protein kinase C. One of its substrate proteins is the nervous tissue-specific protein B-50, which is predominantly localized in membranes of the presynaptic region of neurones. A variety of data suggest that this phosphoprotein may play a regulatory role in the conversion of phosphatidyl-myo-inositol 4-phosphate (PIP) into phosphatidyl-myo-inositol 4,5-bisphosphate (PIP2). These data were obtained using specific anti-B-50 immunoglobulins, prephosphorylation experiments, peptide and neurotransmitter modulation in tissue slices and subcellular fractions. Preliminary results of experiments on the interaction of purified PIP kinase and B-50 phosphoprotein further support this notion.


Subcellular Fraction Synaptic Plasma Membrane Endogenous Phosphorylation Molecular Weight Protein Band Inhibited Protein Kinase Activity 
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Copyright information

© The Humana Press Inc. 1985

Authors and Affiliations

  • W. H. Gispen
    • 1
  • C. J. Van Dongen
    • 1
  • P. N. E. De Graan
    • 1
  • A. B. Oestreicher
    • 1
  • H. Zwiers
    • 1
  1. 1.Division of Molecular Neurobiology, Rudolf Magnus Institute of Pharmacology and Institute of Molecular BiologyState University of UtrechtUtrechtThe Netherlands

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