{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T01:26:05Z","timestamp":1791249965842,"version":"4.1.0"},"reference-count":63,"publisher":"The Company of Biologists","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:p>Laminins promote early stages of peripheral nerve myelination by assembling basement membranes (BMs) on Schwann cell surfaces, leading to activation of \u03b21-integrins and other receptors. The BM composition, structural bonds and ligands needed to mediate this process, however, are not well understood. A mouse hypomorphic for laminin \u03b31-subunit expression that assembled endoneurial BMs with reduced component density exhibited an axonal sorting defect with amyelination but normal Schwann cell proliferation, the latter unlike the null. To identify the basis for this, and to dissect participating laminin interactions, Lamc1 gene-inactivated dorsal root ganglia were treated with recombinant laminins-211 and -111 lacking different architecture-forming and receptor-binding activities to induce myelination. Myelin-wrapping of axons by Schwann cells was found to require higher laminin concentrations than either proliferation or axonal ensheathment. Laminins that were unable to polymerize through deletions that removed critical LN-domains, or that lacked cell-adhesive LG-domains, caused reduced BMs and nearly absent myelination. Laminins engineered to bind weakly to \u03b16\u03b21 and\/or \u03b17\u03b21 integrins through their LG-domains, even though they could effectively assemble BMs, decreased myelination. Proliferation depended upon both integrin-binding to LG domains and polymerization. Collectively these findings reveal that laminins integrate scaffold-forming and cell-adhesion activities to assemble an endoneurial BM, with myelination and proliferation requiring additional \u03b16\u03b21\/\u03b17\u03b21-laminin LG-domain interactions, and that a high BM ligand\/structural-density is needed for efficient myelination.<\/jats:p>","DOI":"10.1242\/jcs.107995","type":"journal-article","created":{"date-parts":[[2012,7,6]],"date-time":"2012-07-06T05:25:38Z","timestamp":1341552338000},"source":"Crossref","is-referenced-by-count":38,"title":["Schwann Cell Myelination Requires Integration of Laminin Activities"],"prefix":"10.1242","author":[{"given":"Karen K.","family":"McKee","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dong-Hua","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rajesh","family":"Patel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zu-Lin","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sidney","family":"Strickland","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Junichi","family":"Takagi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kiyotoshi","family":"Sekiguchi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter D.","family":"Yurchenco","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","published-online":{"date-parts":[[2012,1,1]]},"reference":[{"key":"2021042600142733400_b1","doi-asserted-by":"publisher","first-page":"539","DOI":"10.1007\/BF01668507","article-title":"Comparison of the Schwann cell surface and Schwann cell extracellular matrix as promoters of neurite growth.","volume":"16","author":"Ard","year":"1987","journal-title":"J. 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