The major calmodulin-stimulated phosphoprotein of synaptic junctions and the major post-synaptic density protein are distinct

Neurosci Lett. 1983 Dec 30;43(2-3):161-5. doi: 10.1016/0304-3940(83)90181-7.

Abstract

The major post-synaptic density protein (mPSDp) present in isolated synaptic junction fractions is distinct from the major phosphoprotein (50Kpp) that is labelled by an endogenous calmodulin-stimulated protein kinase. mPSDp and the 50Kpp have different apparent molecular weights on sodium dodecyl sulphate polyacrylamide gels and the presence of 50Kpp in brain soluble fractions indicates that the two proteins have different subcellular distributions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calmodulin / metabolism*
  • Cerebral Cortex / enzymology*
  • Electrophoresis, Polyacrylamide Gel
  • Male
  • Membrane Proteins / metabolism*
  • Molecular Weight
  • Nerve Tissue Proteins / metabolism*
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Protein Kinases / metabolism*
  • Rats
  • Rats, Inbred Strains
  • Stimulation, Chemical
  • Synapses / enzymology*
  • Synaptic Membranes / enzymology

Substances

  • Calmodulin
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Phosphoproteins
  • postsynaptic density proteins
  • Protein Kinases