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Journal of Neuroscience, Vol 12, 4011-4022, Copyright © 1992 by Society for Neuroscience
Colocalization of NGF binding sites, trk mRNA, and low-affinity NGF receptor mRNA in primary sensory neurons: responses to injury and infusion of NGF
VM Verge, JP Merlio, J Grondin, P Ernfors, H Persson, RJ Riopelle, T Hokfelt and PM Richardson
Division of Neurosurgery, McGill University, Montreal, Canada.
The distributions of mRNAs for the protooncogene trk and the low- affinity
NGF receptor (LNGFR) were studied by hybridization with oligonucleotide
probes on sections of adult rat primary sensory and sympathetic ganglia.
For comparison with high-affinity binding sites, adjacent sections were
processed for NGF receptor radioautography. Among neurons in lumbar dorsal
root ganglia and trigeminal ganglia, trk mRNA and NGF-binding sites were
closely colocalized; this finding together with previous direct evidence in
other cell types is taken to indicate that trk protein is an essential
component of the high- affinity NGF receptor in adult sensory neurons. In
lumbar dorsal root ganglia and trigeminal ganglia, abundant LNGFR mRNA was
found in all neurons with strong 125I-NGF labeling and on additional
neurons lacking high-affinity NGF-binding sites. The presence of abundant
LNGFR in neurons with high-affinity receptors could be the cause and/or
consequence of their ability to respond to NGF. Neurons with abundant LNGFR
mRNA but few high-affinity NGF-binding sites may have receptors for other
members of the neurotrophin family. In nodose ganglia, neurons with high
concentrations of LNGFR mRNA greatly outnumbered the small percentage with
abundant trk mRNA. Following intrathecal infusion of NGF to otherwise
normal dorsal root ganglia, the concentrations of LNGFR mRNA but not those
of trk mRNA and NGF-binding sites were increased in NGF-responsive neurons.
The usual single normal pattern of frequency histograms of LNGFR labeling
indices became bimodal in response to NGF. Concentrations of NGF-binding
sites, LNGFR mRNA, and trk mRNA were all decreased by peripheral nerve
transection and restored by exogenous NGF, the restoration being complete
for LNGFR mRNA and partial for trk mRNA and NGF-binding sites. The data
indicate that NGF can regulate both LNGFR and trk mRNAs but do not clarify
the possible contribution of the LNGFR protein to high-affinity binding
sites.
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