The mechanism of ATP-induced long-term potentiation involves extracellular phosphorylation of membrane proteins in guinea-pig hippocampal CA1 neurons

Neurosci Lett. 1995 Mar 3;187(2):130-2. doi: 10.1016/0304-3940(95)11347-9.

Abstract

The mechanism of ATP-induced long-term potentiation was studied pharmacologically using guinea-pig hippocampal slices. Application of 1-10 microM ATP for 10 min transiently depressed and then slowly augmented the synaptic transmission in CA1 neurons leading to long-term potentiation (LTP). This ATP-induced LTP was blocked by the addition of K-252b, an ecto-protein kinase inhibitor, but was enhanced by the addition of RK682, an ecto-phosphatase inhibitor, both of which do not permeate the cell membrane. These results suggest that ATP applied to the perfusate provides enough substrate for ecto-protein kinase to induce LTP through phosphorylation of extracellular domains of membrane proteins in CA1 neurons.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

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

Substances

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