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The Journal of Neuroscience, January 11, 2006, 26(2):508-517; doi:10.1523/JNEUROSCI.2544-05.2006

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Development/Plasticity/Repair
Glypican-1 and 4(V) Collagen Are Required for Schwann Cell Myelination

Michael A. Chernousov, Katrina Rothblum, Richard C. Stahl, Ann Evans, Lisa Prentiss, and David J. Carey

Weis Center for Research, Geisinger Clinic, Danville, Pennsylvania 17822-2601

Schwann cell myelination requires interactions with the extracellular matrix (ECM) mediated by cell surface receptors. Previously, we identified a type V collagen family member, 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 4(V) collagen-binding protein on the Schwann cell surface is the heparan sulfate proteoglycan glypican-1. We investigated the role of 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 4(V)-NTD to Schwann cells, adhesion and spreading of Schwann cells on 4(V)-NTD, and incorporation of 4(V) collagen into Schwann cell ECM. In cocultures, 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 4(V) collagen expression significantly inhibited myelination. These results demonstrate an important role for these proteins in peripheral nerve terminal differentiation.

Key words: Schwann cell; extracellular matrix; proteoglycan; myelin; collagen; dorsal root ganglion

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Received June 21, 2005; revised October 19, 2005; accepted November 3, 2005.

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