{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T06:07:32Z","timestamp":1791007652878,"version":"4.1.0"},"reference-count":0,"publisher":"Rockefeller University Press","issue":"6","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1996,3,15]]},"abstract":"<jats:p>Stable attachment of external epithelia to the basement membrane and underlying stroma is mediated by transmembrane proteins such as the integrin alpha6beta4 and bullous pemphigoid antigen 2 within the hemidesmosomes along the basolateral surface of the epithelial cell and their ligands that include a specialized subfamily of laminins. The laminin 5 molecule (previously termed kalinin\/nicein\/epiligrin) is a member of this epithelial-specific subfamily. Laminin 5 chains are not only considerably truncated within domains III-VI, but are also extensively proteolytically processed in vitro and in vivo. As a result, the domains expected to be required for the association of laminins with other basement membrane components are lacking in the mature laminin 5 molecule. Therefore, the tight binding of laminin 5 to the basement membrane may occur by a unique mechanism. To examine laminin 5 in tissue, we chose human amnion as the source, because of its availability and the similarity of the amniotic epithelial basement membrane with that of skin. We isolated the laminin 5 contained within the basement membrane of human amnion. In addition to monomeric laminin 5, we find that much of the laminin 5 isolated is covalently adducted with laminin 6 (alpha3beta1gamma1) and a novel laminin isotype we have termed laminin 7 (alpha3beta2gamma1). We propose that the association between laminin 5 and laminins 6 and 7 is a mechanism used in amnion to allow stable association of laminin 5 with the basement membrane. The beta2 chain is seen at the human amniotic epithelial-stromal interface and at the dermal-epidermal junction of fetal and adult bovine skin by immunofluorescence, but is not present, or only weakly present, in neonatal human skin.<\/jats:p>","DOI":"10.1083\/jcb.132.6.1189","type":"journal-article","created":{"date-parts":[[2004,5,15]],"date-time":"2004-05-15T01:23:47Z","timestamp":1084584227000},"page":"1189-1198","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":225,"title":["Human amnion contains a novel laminin variant, laminin 7, which like laminin 6, covalently associates with laminin 5 to promote stable epithelial-stromal attachment."],"prefix":"10.1083","volume":"132","author":[{"given":"M F","family":"Champliaud","sequence":"first","affiliation":[{"name":"Cutaneous Biology Research Center, Massachusetts General Hospital, Charlestown 02129, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"G P","family":"Lunstrum","sequence":"additional","affiliation":[{"name":"Cutaneous Biology Research Center, Massachusetts General Hospital, Charlestown 02129, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P","family":"Rousselle","sequence":"additional","affiliation":[{"name":"Cutaneous Biology Research Center, Massachusetts General Hospital, Charlestown 02129, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"T","family":"Nishiyama","sequence":"additional","affiliation":[{"name":"Cutaneous Biology Research Center, Massachusetts General Hospital, Charlestown 02129, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"D R","family":"Keene","sequence":"additional","affiliation":[{"name":"Cutaneous Biology Research Center, Massachusetts General Hospital, Charlestown 02129, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R E","family":"Burgeson","sequence":"additional","affiliation":[{"name":"Cutaneous Biology Research Center, Massachusetts General Hospital, Charlestown 02129, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[1996,3,15]]},"container-title":["The Journal of cell biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/rupress.org\/jcb\/article-pdf\/132\/6\/1189\/1479770\/1189.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/rupress.org\/jcb\/article-pdf\/132\/6\/1189\/1479770\/1189.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,7,22]],"date-time":"2023-07-22T06:15:24Z","timestamp":1690006524000},"score":1,"resource":{"primary":{"URL":"https:\/\/rupress.org\/jcb\/article\/132\/6\/1189\/15222\/Human-amnion-contains-a-novel-laminin-variant"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1996,3,15]]},"references-count":0,"journal-issue":{"issue":"6","published-print":{"date-parts":[[1996,3,15]]}},"URL":"https:\/\/doi.org\/10.1083\/jcb.132.6.1189","relation":{},"ISSN":["0021-9525","1540-8140"],"issn-type":[{"value":"0021-9525","type":"print"},{"value":"1540-8140","type":"electronic"}],"subject":[],"published":{"date-parts":[[1996,3,15]]}}}