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Journal of Neuroscience, Vol 9, 625-638, Copyright © 1989 by Society for Neuroscience
Differentiation of axon-related Schwann cells in vitro: II. Control of myelin formation by basal lamina
CF Eldridge, MB Bunge and RP Bunge
Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110.
Several recent observations suggest that Schwann cell (SC) differentiation,
including myelin formation, is dependent upon the development of basal
lamina which characteristically surrounds each axon-SC unit in peripheral
nerve. This dependence can be tested in a neuron-SC culture system
developed in our laboratory in which SC differentiation, including basal
lamina formation and myelination, is faithfully reproduced. The use of
serum-free, defined medium (DM) with this culture system allows axon-driven
SC proliferation but not basal lamina formation or myelination. We
previously demonstrated that ascorbic acid, in the presence of a
nondialyzable serum factor(s), stimulates basal lamina assembly and myelin
formation with similar dose- response relationships (Eldridge et al.,
1987). We hypothesized that ascorbic acid acts to promote SC myelination
indirectly, by enabling the assembly of basal lamina. We now provide
support for this hypothesis by demonstrating the following. (1)
Pepsin-resistant triple- helical collagen molecules were produced only by
SCs grown in the presence of ascorbic acid, suggesting that triple-helical
type IV collagen may mediate the effect of ascorbic acid on basal lamina
formation. (2) The formation of myelin by oligodendrocytes, which myelinate
axons in the CNS without the concomitant deposition of basal lamina, was
little affected by ascorbic acid, suggesting that the biosynthesis and
assembly of myelin per se does not require ascorbic acid. (3) The provision
of exogenous basal lamina matrix to SCs grown with neurons in DM without
ascorbic acid promoted control levels of myelination (and basal lamina
formation); the provision of exogenous fibrillar collagen matrix did not.
(4) Purified laminin promoted control levels of myelination in the absence
of ascorbic acid, but purified type IV collagen and heparan sulfate
proteoglycan (HSPG) did not. Laminin caused SCs to assemble basal
lamina-like structures that contained not only laminin but also HSPG and
non-triple-helical type IV collagen. Thus, several types of experiments
demonstrate that SC myelin formation can be controlled by regulating the
ability of the SC to assemble basal lamina, illustrating that acquisition
of basal lamina is a crucial prefatory step for further SC differentiation.
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