Abstract
Cytomatrix proteins, of primary functional importance in central nervous system neuron terminals, are provided to their site of action in the terminal by axonal transport. Slow component b (SCb) of axonal transport has been proposed to be the biochemical counterpart of the moving cytoplasmic matrix, or cytomatrix, in axons. In the current study, axonally transported SCb proteins destined for neuron terminals were pulse-radiolabeled with [ 35S]methionine in guinea pig retinal ganglion cells. After SCb proteins reached the terminals in the superior colliculi, synaptosomes were prepared to distinguish between SCb proteins in the preterminal axons and those of the presynaptic terminals. Study of the initial entry and turnover of individual SCb proteins in presynaptic terminals revealed different residence times of certain SCb proteins in comparison with their cohorts. Preliminary information about the structural relationships of the proteins comprising the presynaptic cytomatrix was obtained by examining the solubility of individual SCb proteins relative to other SCb proteins, or membranes from osmotically lysed terminals. Last, treatment of those radiolabeled synaptosomes with varying concentrations of salts was performed to determine possible effects on observed structural relationships.
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