Journal of Neuroscience, Vol 8, 1759-1766, Copyright © 1988 by Society for Neuroscience
Light- and electron-microscopical study of phosphoprotein B-50 following denervation and reinnervation of the rat soleus muscle
J Verhaagen, AB Oesteicher, PM Edwards, H Veldman, FG Jennekens and WH Gispen
Department of Neurology, University Hospital, Utrecht, The Netherlands.
The neuron-specific phosphoprotein B-50 was originally identified as a
phosphoprotein in synaptic plasma membranes isolated from adult brain
tissue. In this paper we study the reinnervation of the soleus muscle, a
target muscle of sciatic nerve axons, using affinity-purified anti-B- 50
antibodies. Light-microscopical evaluation of the reinnervation process
revealed that the period of muscle fiber reinnervation corresponds closely
with the time in which high B-50 immunoreactivity was observed in the nerve
fibers that invade the muscle and in the newly formed neuromuscular
junctions. Upon completion of reinnervation, B-50 immunoreactivity
decreased. In the newly innervating terminals, B- 50 was associated with
presynaptic vesicular structures and with the presynaptic plasma membrane.
In intact mature neuromuscular junctions, virtually no B-50
immunoreactivity could be detected with either light- or
electron-microscopic procedures. These observations corroborate the
association of high levels of B-50/GAP43 during axon outgrowth and support
the concept that B-50 may be a key molecule in the reconstruction of axonal
structures. We also observed an unexpected transient increase in B-50
immunoreactivity in the degenerating neuromuscular junctions. This
observation cannot be explained in terms of increased neuronal synthesis of
B-50, since the degenerating axon processes have been completely
disconnected from their cell bodies. Thus, our evidence implies that a rise
of B-50 immunoreactivity can be associated with stages of neuronal
degeneration as well as with those of neuronal differentiation and axon
outgrowth.