Block of synapse formation between cerebral cortical neurons by a protein kinase inhibitor

Neurosci Lett. 1992 Feb 3;135(2):255-8. doi: 10.1016/0304-3940(92)90449-h.

Abstract

Synchronized Ca2+ transients in cultured hippocampal neurons reflect the pattern of underlying electrical activity. Here we demonstrate a similar synchronization of cerebral cortical neurons in culture, and show that this functional coupling is correlated to the appearance of morphologically identified synapses using electron microscopy. During screening of a series of drugs for inhibition of in vitro synaptogenesis, the continuous presence of a protein kinase inhibitor (K-252b) in the culture medium was found to block the synchronous firing and to decrease significantly the number of morphologically identifiable synapses. Since K-252b does not permeate the cell membrane, the results strongly suggest that phosphorylation of cell surface protein(s) by a K-252b sensitive-protein kinase is an essential process in synapse formation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcium / metabolism
  • Carbazoles / pharmacology
  • Cells, Cultured
  • Cerebral Cortex / cytology*
  • Cerebral Cortex / drug effects
  • Cerebral Cortex / ultrastructure
  • Female
  • Indole Alkaloids
  • Microscopy, Electron
  • Pregnancy
  • Protein Kinase C / antagonists & inhibitors
  • Protein Kinase Inhibitors*
  • Rats
  • Synapses / drug effects*
  • Synapses / ultrastructure

Substances

  • Carbazoles
  • Indole Alkaloids
  • Protein Kinase Inhibitors
  • staurosporine aglycone
  • Protein Kinase C
  • Calcium