Kindling induces a long-lasting change in the activity of a hippocampal membrane calmodulin-dependent protein kinase system

Brain Res. 1986 Jul 2;377(1):47-53. doi: 10.1016/0006-8993(86)91189-3.

Abstract

Septal kindling has been shown to produce a long-lasting decrease in endogenous calcium/calmodulin-dependent phosphorylation of hippocampal synaptic plasma membrane proteins, including two major bands of approximately 50,000 and 60,000 Daltons. These two proteins differ from the B-50 protein and tubulin, as evidenced by differences in migration in SDS-PAGE gels and by lack of cross-immunoreactivity with specific antibodies. Identity of these two proteins with the rho and sigma subunits of purified calmodulin-dependent kinase (CaM Kinase II) is suggested by similar migration in SDS-PAGE and two-dimensional gels, by similar calmodulin binding in two-dimensional gels, and similar 125I-peptide mapping of the 50,000 Dalton protein. These results demonstrate that septal kindling is associated with changes in the activity of a major Ca2+/calmodulin-dependent kinase system in hippocampal synaptic plasma membrane. This long-lasting modulation of kinase activity may provide a molecular insight into some aspects of neuronal plasticity.

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

  • Animals
  • Calmodulin / physiology*
  • Hippocampus / metabolism*
  • Kindling, Neurologic*
  • Male
  • Membrane Proteins / metabolism
  • Nerve Tissue Proteins / metabolism
  • Phosphorylation
  • Protein Kinases / metabolism*
  • Rats
  • Rats, Inbred Strains
  • Septum Pellucidum / physiology*
  • Synaptic Membranes / metabolism

Substances

  • Calmodulin
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Protein Kinases