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Journal of Neuroscience, Vol 13, 3421-3432, Copyright © 1993 by Society for Neuroscience
Tyrosine phosphorylation in early embryonic growth cones
JL Bixby and P Jhabvala
Department of Molecular and Cellular Pharmacology, University of Miami School of Medicine, Florida 33136.
A large and growing body of evidence suggests that the regulation of
tyrosine phosphorylation is important in the induction of axon growth. We
have examined the subcellular distribution of enzymes regulating tyrosine
phosphorylation in early embryonic brain, employing a preparation of
isolated growth cone particles (GCPs). Because of the early developmental
age and well-characterized nature of our tissue source, our GCP preparation
offers some advantages over those described previously. As was found with
other GCPs, our GCPs had relatively high levels of both the
growth-associated protein GAP-43 and the intracellular tyrosine kinase
pp60c-arc. In addition, we found that both total tyrosine kinase activity
and total tyrosine phosphatase activity were concentrated two- to threefold
in the GCPs relative to a neuronal membrane fraction. Two other nonreceptor
tyrosine kinases, YES and FYN, were concentrated in the GCPs to a similar
degree as that seen for SRC. In addition, we examined the developmental
expression in brain of the three tyrosine kinases, using both a
quantitative ELISA and Western blot analysis. Our results show that FYN,
like SRC, reaches a peak of expression early in development, and declines
thereafter. In contrast, expression of YES peaks later, and remains high in
the adult brain. Immunofluorescence staining suggests that FYN is expressed
both by neurons and by glia, and possibly by neuronal precursor cells. Our
results implicate multiple tyrosine kinases as well as tyrosine
phosphatases in growth cone function. In addition, the concentration of FYN
in early embryonic growth cones combined with its early peak of expression
suggests an important role for FYN in early neuronal development.
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