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Journal of Neuroscience, Vol 8, 3057-3066, Copyright © 1988 by Society for Neuroscience
Immunocytochemical localization by electron microscopy of 2'3'-cyclic nucleotide 3'-phosphodiesterase in developing oligodendrocytes of normal and mutant brain
PE Braun, F Sandillon, A Edwards, JM Matthieu and A Privat
Department of Biochemistry, McGill University, Montreal, Canada.
Oligodendrocytes or their putative progenitors were the only cells found to
be immunoreactive to polyclonal antisera against the enzyme 2'3'-cyclic
nucleotide 3'-phosphodiesterase (CNP) in developing and mature brains of
rats and mice, as visualized by light and electron microscopy. Prior to
myelination (day 6), oligodendrocytes of the corpus callosum have reticular
networks of CNP-containing filopodia, in addition to abundant CNP
throughout the cytoplasm. Some glioblast-like cells of the subventricular
zone are also immunoreactive to anti-CNP, suggesting that, as progenitors
of oligodendroglia, they express this myelination-related protein as one of
the earliest events in myelinogenesis. Following the commencement of
myelination (day 15), many oligodendrocytes lose much of their lacelike
network of fine projections, possessing, instead, larger CNP-filled
processes that extend to myelin-bearing fibers. CNP was always found only
in the cytoplasm-containing compartments of the cells and myelin sheaths;
neither lamellae nor cellular membranes were immunostained. These data
support our contention that CNP is not an intrinsic membrane protein,
despite its strong interaction with membrane components when cells are
disrupted. In mutant (mld) mice (day 25), the many distended and
uncompacted oligodendroglial processes that invest axons with only a few
turns of membrane contained cytoplasmic CNP, accounting for the elevated
levels of CNP activity previously noted in tissue fractions.
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