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Journal of Neuroscience, Vol 10, 3635-3645, Copyright © 1990 by Society for Neuroscience
Inhibition of Schwann cell myelination in vitro by antibody to the L1 adhesion molecule
PM Wood, M Schachner and RP Bunge
Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110.
The specific axonal and Schwann cell surface molecules that mediate the
initiation of myelination have not been identified. We have used cocultures
of purified rat dorsal root ganglion neurons and Schwann cells and purified
polyclonal antibodies to the L1 adhesion molecule to study the role of L1
in myelin formation. Schwann cells were first arrested in a
basal-lamina-free premyelination stage (by serum/ascorbate deprivation),
then manipulated to allow basal lamina deposition and myelination (by
serum/ascorbate addition) in the absence or presence of anti-L1. Using
electron microscopy, immunocytochemistry, and myelin sheath quantitation
after Sudan-black staining, we determined the effect of anti-L1 on (1)
basal lamina formation, (2) the segregation by Schwann cells of axons into
a 1:1 relationship, (3) galactocerebroside (Gal-C) expression, (4) laminin
deposition, and (5) myelin formation. Anti-L1 strongly blocked myelin
formation, Gal-C expression, and axon segregation but did not block basal
lamina formation. In controls, elongated Schwann cell processes completely
covered the axons and exhibited uniform surface staining for laminin; in
anti-L1-treated cultures, shortened Schwann cells, intensely stained for
laminin, were observed in clusters separated by unstained lengths of axons.
When 50 micrograms/ml exogenous purified laminin was added to the medium,
Schwann cell length and laminin staining were similar in control and
treated cultures. However, the inhibition of myelination of anti-L1 was not
altered by the addition of laminin. Myelination was also inhibited with
antigen-binding fragments (Fab) of polyclonal anti- L1, but an antibody to
liver membranes did not block myelination. These results indicate that L1
is involved in the linear extension of Schwann cell processes along axons,
the engulfment of axons, and the induction of myelin-specific components
within the Schwann cell. We conclude that anti-L1 prevents myelination by
blocking these events rather than by blocking basal lamina deposition.
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