Journal
JOURNAL OF NEUROSCIENCE
Volume 26, Issue 2, Pages 508-517Publisher
SOC NEUROSCIENCE
DOI: 10.1523/JNEUROSCI.2544-05.2006
Keywords
Schwann cell; extracellular matrix; proteoglycan; myelin; collagen; dorsal root ganglion
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Funding
- NINDS NIH HHS [NS21925, R01 NS021925] Funding Source: Medline
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Schwann cell myelination requires interactions with the extracellular matrix (ECM) mediated by cell surface receptors. Previously, we identified a type V collagen family member, alpha 4(V) collagen, which is expressed by Schwann cells during peripheral nerve differentiation. This collagen binds with high affinity to heparan sulfate through a unique binding motif in the noncollagenous N-terminal domain (NTD). The principal alpha 4(V) collagen-binding protein on the Schwann cell surface is the heparan sulfate proteoglycan glypican-1. We investigated the role of alpha 4(V) collagen and glypican-1 in Schwann cell terminal differentiation in cultures of Schwann cells and dorsal root ganglion neurons. Small interfering RNA-mediated suppression of glypican-1 expression decreased binding of alpha 4(V)-NTD to Schwann cells, adhesion and spreading of Schwann cells on alpha 4(V)-NTD, and incorporation of alpha 4(V) collagen into Schwann cell ECM. In cocultures, alpha 4(V) collagen coassembles with laminin on the surface of polarized Schwann cells to form tube-like ECM structures that are sites of myelination. Suppression of glypican-1 or alpha 4(V) collagen expression significantly inhibited myelination. These results demonstrate an important role for these proteins in peripheral nerve terminal differentiation.
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