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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2006-1-12
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pubmed:abstractText |
Schwann cell myelination requires interactions with the extracellular matrix (ECM) mediated by cell surface receptors. Previously, we identified a type V collagen family member, alpha4(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 alpha4(V) collagen-binding protein on the Schwann cell surface is the heparan sulfate proteoglycan glypican-1. We investigated the role of alpha4(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 alpha4(V)-NTD to Schwann cells, adhesion and spreading of Schwann cells on alpha4(V)-NTD, and incorporation of alpha4(V) collagen into Schwann cell ECM. In cocultures, alpha4(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 alpha4(V) collagen expression significantly inhibited myelination. These results demonstrate an important role for these proteins in peripheral nerve terminal differentiation.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1529-2401
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
11
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pubmed:volume |
26
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
508-17
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16407548-Animals,
pubmed-meshheading:16407548-Cell Adhesion,
pubmed-meshheading:16407548-Cell Differentiation,
pubmed-meshheading:16407548-Cells, Cultured,
pubmed-meshheading:16407548-Coculture Techniques,
pubmed-meshheading:16407548-Collagen Type V,
pubmed-meshheading:16407548-Culture Media, Serum-Free,
pubmed-meshheading:16407548-Extracellular Matrix,
pubmed-meshheading:16407548-Ganglia, Spinal,
pubmed-meshheading:16407548-Heparan Sulfate Proteoglycans,
pubmed-meshheading:16407548-Laminin,
pubmed-meshheading:16407548-Myelin Sheath,
pubmed-meshheading:16407548-Neurons,
pubmed-meshheading:16407548-Protein Structure, Tertiary,
pubmed-meshheading:16407548-RNA, Messenger,
pubmed-meshheading:16407548-RNA, Small Interfering,
pubmed-meshheading:16407548-Rats,
pubmed-meshheading:16407548-Recombinant Fusion Proteins,
pubmed-meshheading:16407548-Schwann Cells,
pubmed-meshheading:16407548-Sciatic Nerve,
pubmed-meshheading:16407548-Transfection
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pubmed:year |
2006
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pubmed:articleTitle |
Glypican-1 and alpha4(V) collagen are required for Schwann cell myelination.
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pubmed:affiliation |
Weis Center for Research, Geisinger Clinic, Danville, Pennsylvania 17822-2601, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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