LTP induced by activation of voltage-dependent Ca2+ channels requires protein kinase activity

Neuroreport. 1995 Jun 19;6(9):1281-4. doi: 10.1097/00001756-199506090-00013.

Abstract

We have examined the requirement for protein kinase activity in long-term potentiation (LTP) induced by activation of voltage-dependent Ca2+ channels (VDCCs) in hippocampal slices. We previously demonstrated that LTP induced by application of the K+ channel blocker tetraethylammonium (TEA-LTP) consisted of two distinct components, an NMDA receptor-dependent component and a VDCC-dependent component. The results herein demonstrate that both the NMDA and VDCC-dependent components of TEA-LTP are blocked by K-252a, a broad spectrum protein kinase inhibitor. Furthermore, VDCC-dependent TEA-LTP is attenuated by KN-62, a specific inhibitor of Ca2+/calmodulin dependent protein kinase II (CaM-KII). These results demonstrate that LTP induced by VDCC activation requires protein kinase activity and suggest that different routes of postsynaptic Ca2+ influx activate protein kinases to trigger the induction of LTP but that these enzyme systems may be contained in different cell compartments.

Publication types

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

MeSH terms

  • Animals
  • Calcium Channels / drug effects
  • Calcium Channels / physiology*
  • Carbazoles / pharmacology
  • Enzyme Inhibitors / pharmacology
  • Hippocampus / physiology*
  • Indole Alkaloids
  • Long-Term Potentiation*
  • Membrane Potentials / drug effects
  • N-Methylaspartate / pharmacology
  • Protein Kinases / physiology*
  • Rats
  • Rats, Sprague-Dawley
  • Time Factors

Substances

  • Calcium Channels
  • Carbazoles
  • Enzyme Inhibitors
  • Indole Alkaloids
  • N-Methylaspartate
  • staurosporine aglycone
  • Protein Kinases