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Journal of Neuroscience, Vol 8, 2571-2581, Copyright © 1988 by Society for Neuroscience
Distribution and phosphorylation of the growth-associated protein GAP- 43 in regenerating sympathetic neurons in culture
KF Meiri, M Willard and MI Johnson
Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110.
Sympathetic neurons regenerating in culture were studied in order to gain
further insight into the intracellular distribution and phosphorylation of
GAP-43, a protein that has been suggested to have a role in axonal
outgrowth and neuronal plasticity (Willard et al., 1987). Superior cervical
ganglion neurons from embryonic rats were highly reactive with a polyclonal
antibody against the growth- associated protein GAP-43 soon after they were
placed in culture on a laminin substrate. As these neurons extended
neurites, the distribution of GAP-43 reactivity changed. The cell body
became progressively less reactive, whereas the growth cone at the tip of
the growing neurite reacted strongly. The pattern of immunofluorescence was
punctate both in the growth cone and the adjacent neurite, but appeared
more diffusely distributed in the cell body. The antibody reacted only with
cells that had been subjected to treatment that permeabilized the plasma
membrane. When antibody was supplied in the medium of growing neurons, it
neither bound to the cells nor altered normal neurite initiation or
elongation. Of the different types of cells in these cultures, the antibody
reacted only with neurons; it did not react with Schwann cells or
fibroblasts. The stimulation of protein kinase C in these cultures resulted
in a 7-fold stimulation of the phosphorylation of a protein of similar
electrophoretic mobility to GAP-43. These observations demonstrate that
GAP-43 is neuron-specific, is present throughout the neuron but at higher
levels in the growth cone, and is a major substrate of protein kinase C.
The high concentration of GAP-43 in the growth cones may necessitate its
increased synthesis in neurons with elongating axons. Its location and
phosphorylation by kinase C suggest that it could perform a function in the
growth cone that is modulated by extracellular signals, such as those used
in pathfinding or in the control of axonal elongation.
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