Oligodendrocyte adhesion activates protein kinase C-mediated phosphorylation of myelin basic protein

Science. 1986 Dec 12;234(4782):1395-8. doi: 10.1126/science.2431483.


When isolated adult oligodendrocytes adhere to a substratum myelinogenesis occurs. Investigation of the mechanism by which this happens indicated that the oligodendrocyte-substratum interaction activated protein kinase C-dependent phosphorylation of myelin basic protein and promoted the synthesis of myelin basic protein. In addition, when agents that activate protein kinase C (second messenger diacylglycerol or a tumor-promoting phorbol ester) were added to nonattached oligodendrocytes, they mimicked the influence of the substratum by inducing phosphorylation of myelin basic protein; and reagents that increase cellular adenosine 3', 5'-monophosphate (cyclic AMP) inhibited phosphorylation of myelin basic protein. Thus, at least in vitro, the interaction between oligodendrocytes and the substratum may mediate myelinogenic events, and phosphorylation of myelin basic protein may be an early requirement in the sequence of steps that ultimately results in myelin formation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 1-Methyl-3-isobutylxanthine / pharmacology
  • Adult
  • Calcimycin / pharmacology
  • Cell Adhesion
  • Colforsin / pharmacology
  • Cyclic AMP / metabolism
  • Enzyme Activation
  • Humans
  • Myelin Basic Protein / metabolism*
  • Neuroglia / cytology*
  • Oligodendroglia / cytology*
  • Phosphorylation
  • Protein Kinase C / metabolism*
  • Tetradecanoylphorbol Acetate / pharmacology


  • Myelin Basic Protein
  • Colforsin
  • Calcimycin
  • Cyclic AMP
  • Protein Kinase C
  • Tetradecanoylphorbol Acetate
  • 1-Methyl-3-isobutylxanthine