Intermolecular disulfide bonds at central nervous system synaptic junctions

Biochem Biophys Res Commun. 1976 Dec 20;73(4):858-64. doi: 10.1016/0006-291x(76)90200-x.

Abstract

Most proteins in isolated synaptic junctions and nearly all those in postsynaptic densities (the fibrous protein matrix underlying the postsynaptic membrane at the synapse) are extensively cross-linked by disulfide bonds into polymers with a molecular weight of 350,000 or greater. Since the postsynaptic density appears to consist primarily of a matrix of cytoplasmic proteins, such as tubulin and neurofilament protein, our results indicate that at the membrane such proteins may use disulfide bonds to differentiate into the postsynaptic density and tie into the postsynaptic membrane.

Publication types

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

MeSH terms

  • Animals
  • Central Nervous System / chemistry*
  • Central Nervous System / cytology
  • Disulfides / chemistry*
  • Male
  • Nerve Tissue Proteins / analysis
  • Nerve Tissue Proteins / chemistry*
  • Rats
  • Rats, Sprague-Dawley
  • Synapses / chemistry*

Substances

  • Disulfides
  • Nerve Tissue Proteins