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Journal of Neuroscience, Vol 6, 1843-1855, Copyright © 1986 by Society for Neuroscience
A protein associated with axon growth, GAP-43, is widely distributed and developmentally regulated in rat CNS
RD Jacobson, I Virag and JH Skene
Development or regeneration of axons in several systems is accompanied by
20-100-fold increases in the synthesis of an acidic, axonally transported
membrane protein with an apparent molecular weight of 43- 50,000 (Benowitz
and Lewis, 1983; Skene and Willard, 1981a, b), which we designate GAP-43.
We have proposed that some step(s) in axon growth require production of
GAP-43, and perhaps a small number of other "growth-associated proteins,"
at rates much higher than those typical of mature neurons. This hypothesis
predicts that virtually all neurons synthesize GAP-43 at elevated levels
during normal CNS development. Here we show that a protein similar to
GAP-43 from regenerating toad nerves is prominent among the newly
synthesized (35S-methionine- labeled) and total (Coomassie blue-stained)
proteins in neonatal rat cerebral cortex and cerebellum, suggesting that
synthesis of GAP-43 is indeed a common feature of many developing neurons.
Synthesis and accumulation of the protein decline an order of magnitude as
animals mature. Antibodies raised against the rat cortex GAP-43 also
recognize electrophoretically similar proteins from regenerating toad optic
nerves and from developing hamster sensorimotor cortex, indicating that
structural features of GAP-43 are conserved in evolution. Cell-free
translation of polyadenylated RNA from neonatal and adult cortex suggests
that developmental regulation of GAP-43 synthesis is mediated largely
through changes in mRNA abundance. These observations together suggest that
developmental regulation of GAP-43 gene expression may be common to most
vertebrate CNS neurons. GAP-43 remains detectable at a low level in adult
rat cortex, and it co-migrates on two-dimensional gels with B-50, a
synaptic membrane protein which is a preferred substrate for protein kinase
C in adult brains. Phosphorylation of the protein by endogenous kinase(s)
in vitro is 4-7-fold greater in growth cone membranes than in mature
synaptic membranes, which raises the possibility that local modification of
the protein in axon terminals may be synergistic with regulation of GAP-43
synthesis in the cell body.
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