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Journal of Neuroscience, Vol 3, 2153-2163, Copyright © 1983 by Society for Neuroscience
Increased transport of 44,000- to 49,000-dalton acidic proteins during regeneration of the goldfish optic nerve: a two-dimensional gel analysis
LI Benowitz and ER Lewis
Proteins synthesized in goldfish retinal ganglion cells and rapidly
transported to the terminals of regenerating optic nerves were analyzed by
two-dimensional (2-D) gel electrophoresis. Among the rapidly transported
components, the most dramatic change observed during regeneration was for a
family of polypeptides having molecular weights between 44,000 and 49,000
(44-49K) and isoelectric points of 4.6 to 4.9. Studies using
[35S]methionine as a metabolic precursor in the eye showed that these
proteins are present in both membranous and soluble fractions of the optic
tectum, particularly during early stages of regeneration. Contralateral
visual pathways, left intact to serve as controls, showed only very low
levels of the proteins. These labeling changes were quantified in
double-isotope studies, in which proteins from intact and regenerating
sides were differentially labeled with [3H]proline and [14C]proline,
comigrated on 2-D gels, and then counted for 3H/14C ratios. The labeling
change for the 44-49K acidic proteins relative to the intact state was
found to be over 100-fold in some day 19 regeneration samples and about
30-fold on day 40. Silver-stained gels of a tectal membrane fraction also
revealed increased levels of the 44-49K acidic proteins during
regeneration, indicating that the observed synthetic changes are
accompanied by a net accumulation of the proteins.
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