Limited proteolytic modification of a neurofilament protein involves a proteinase activated by endogenous levels of calcium.
Posttranslational modification of a structural protein by limited proteolysis is demonstrated for the first time in the nervous system. The 145,000 dalton subunit of neurofilaments in mouse retinal ganglion cell (RGC) axons is selectively converted in vitro to the major 143,000 and 140,000 dalton neurofilament subunits by a neutral proteinase that is activated by endogenous levels of calcium and is distinguishable from other known brain proteinases. The close similarities between this in vitro process and the previously observed modification of the 145,000 dalton neurofilament protein during axoplasmic transport in vivo suggest that the same enzymatic mechanism is involved. These findings imply that limited proteolysis is an active process along central axons in vivo and that this enzyme may play a specific role in the function of the neuronal cytoskeleton.
D000818:Animals; D002118:Calcium / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D007381:Intermediate Filament Proteins / Q000235:genetics* / Q000302:isolation & purification; D007700:Kinetics; D051379:Mice; D008810:Mice, Inbred C57BL; D008970:Molecular Weight; D016900:Neurofilament Proteins; D010447:Peptide Hydrolases / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
D007381:Intermediate Filament Proteins; D016900:Neurofilament Proteins; D010447:Peptide Hydrolases; D002118:Calcium