| pubmed-article:16407548 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16407548 | lifeskim:mentions | umls-concept:C0009325 | lld:lifeskim |
| pubmed-article:16407548 | lifeskim:mentions | umls-concept:C0596991 | lld:lifeskim |
| pubmed-article:16407548 | lifeskim:mentions | umls-concept:C0036387 | lld:lifeskim |
| pubmed-article:16407548 | lifeskim:mentions | umls-concept:C1706284 | lld:lifeskim |
| pubmed-article:16407548 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:16407548 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:16407548 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:16407548 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:16407548 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16407548 | pubmed:dateCreated | 2006-1-12 | lld:pubmed |
| pubmed-article:16407548 | 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. | lld:pubmed |
| pubmed-article:16407548 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16407548 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16407548 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16407548 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16407548 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16407548 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16407548 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16407548 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:16407548 | pubmed:issn | 1529-2401 | lld:pubmed |
| pubmed-article:16407548 | pubmed:author | pubmed-author:CareyDavid... | lld:pubmed |
| pubmed-article:16407548 | pubmed:author | pubmed-author:StahlRichard... | lld:pubmed |
| pubmed-article:16407548 | pubmed:author | pubmed-author:RothblumKatri... | lld:pubmed |
| pubmed-article:16407548 | pubmed:author | pubmed-author:ChernousovMic... | lld:pubmed |
| pubmed-article:16407548 | pubmed:author | pubmed-author:EvansAnnA | lld:pubmed |
| pubmed-article:16407548 | pubmed:author | pubmed-author:PrentissLisaL | lld:pubmed |
| pubmed-article:16407548 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:16407548 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:16407548 | pubmed:volume | 26 | lld:pubmed |
| pubmed-article:16407548 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16407548 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16407548 | pubmed:pagination | 508-17 | lld:pubmed |
| pubmed-article:16407548 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:16407548 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16407548 | pubmed:articleTitle | Glypican-1 and alpha4(V) collagen are required for Schwann cell myelination. | lld:pubmed |
| pubmed-article:16407548 | pubmed:affiliation | Weis Center for Research, Geisinger Clinic, Danville, Pennsylvania 17822-2601, USA. | lld:pubmed |
| pubmed-article:16407548 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16407548 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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