Extracellular phosphorylation of membrane protein modifies theta burst-induced long-term potentiation in CA1 neurons of guinea-pig hippocampal slices

Neurosci Lett. 1995 Mar 3;187(2):133-6. doi: 10.1016/0304-3940(95)11342-8.


The involvement of ecto-protein kinase activity in activity-dependent long-term potentiation (LTP) was studied in CA1 neurons of guinea-pig hippocampal slices. Application of 5 microM K-252b, an ecto-protein kinase inhibitor, blocked LTP induced by a theta-burst stimulation (3 bursts composed of 5 pulses at 100 Hz with inter-burst intervals of 200 ms). On the other hand, under 10 microM RK682, an ecto-phosphatase inhibitor, a robust LTP was induced by a weak theta-burst stimulation (3 bursts composed of 3 pulses) which was just at the threshold for the induction of LTP in the control perfusate. These findings suggest that ATP released from presynaptic terminals during the burst stimulation plays an important role in the induction of LTP through phosphorylation of extracellular domains of synaptic membrane proteins, as the substrate for ecto-protein kinase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carbazoles / pharmacology
  • Electric Stimulation
  • Extracellular Space / metabolism*
  • Guinea Pigs
  • Hippocampus / cytology
  • Hippocampus / physiology*
  • In Vitro Techniques
  • Indole Alkaloids
  • Long-Term Potentiation* / drug effects
  • Membrane Proteins / metabolism*
  • Neurons / physiology*
  • Phosphoprotein Phosphatases / antagonists & inhibitors
  • Phosphoprotein Phosphatases / pharmacology
  • Phosphorylation
  • Protein Kinase Inhibitors
  • Protein Kinases*
  • Theta Rhythm*


  • Carbazoles
  • Indole Alkaloids
  • Membrane Proteins
  • Protein Kinase Inhibitors
  • RK 682
  • staurosporine aglycone
  • Protein Kinases
  • ectoprotein kinase
  • Phosphoprotein Phosphatases