pubmed-article:10806203 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10806203 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
pubmed-article:10806203 | lifeskim:mentions | umls-concept:C0521119 | lld:lifeskim |
pubmed-article:10806203 | lifeskim:mentions | umls-concept:C0377148 | lld:lifeskim |
pubmed-article:10806203 | lifeskim:mentions | umls-concept:C0171955 | lld:lifeskim |
pubmed-article:10806203 | lifeskim:mentions | umls-concept:C1823153 | lld:lifeskim |
pubmed-article:10806203 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
pubmed-article:10806203 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
pubmed-article:10806203 | lifeskim:mentions | umls-concept:C2349976 | lld:lifeskim |
pubmed-article:10806203 | lifeskim:mentions | umls-concept:C1552644 | lld:lifeskim |
pubmed-article:10806203 | lifeskim:mentions | umls-concept:C0337112 | lld:lifeskim |
pubmed-article:10806203 | pubmed:issue | 30 | lld:pubmed |
pubmed-article:10806203 | pubmed:dateCreated | 2000-8-31 | lld:pubmed |
pubmed-article:10806203 | pubmed:abstractText | Epithelial cells maintained in culture medium containing low calcium proteolytically process laminin 5 (alpha3beta3gamma2) within the alpha3 and gamma2 chains (). Experiments were designed to identify the enzyme(s) responsible for the laminin 5 processing and the sites of proteolytic cleavage. To characterize the nature of laminin 5 processing, we determined the N-terminal amino acid sequences of the proteolytic fragments produced by the processing events. The results indicate that the first alpha3 chain cleavage (200-l65 kDa alpha3) occurs within subdomain G4 of the G domain. The second cleavage (l65-l45 kDa alpha3) occurs within the lIla domain, 11 residues N-terminal to the start of domain II. The gamma chain is cleaved within the second epidermal growth factor-like repeat of domain Ill. The sequence cleaved within the gamma2 chain matches the consensus sequence for the cleavage of type I, II, and III procollagens by bone morphogenetic protein-1 (BMP-1), also known as type I procollagen C-proteinase (). Recombinant BMP-1 cleaves gamma2 in vitro, both within intact laminin 5 and at the predicted site of a recombinant gamma2 short arm. alpha3 is also cleaved by BMP-1 in vitro, but the cleavage site is yet to be determined. These results show the laminin alpha3 and gamma2 chains to be substrates for BMP-1 in vitro. We speculate that gamma2 cleavage is required for formation of the laminin 5-6 complex and that this complex is directly involved in assembly of the interhemidesmosomal basement membrane. This further suggests that BMP-1 activity facilitates basement membrane assembly, but not hemidesmosome assembly, in the laminin 5-rich dermal-epidermal junction basement membrane in vivo. | lld:pubmed |
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pubmed-article:10806203 | pubmed:language | eng | lld:pubmed |
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pubmed-article:10806203 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10806203 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10806203 | pubmed:month | Jul | lld:pubmed |
pubmed-article:10806203 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:10806203 | pubmed:author | pubmed-author:AmanoSS | lld:pubmed |
pubmed-article:10806203 | pubmed:author | pubmed-author:NishiyamaTT | lld:pubmed |
pubmed-article:10806203 | pubmed:author | pubmed-author:LeeSS | lld:pubmed |
pubmed-article:10806203 | pubmed:author | pubmed-author:BurgesonR ERE | lld:pubmed |
pubmed-article:10806203 | pubmed:author | pubmed-author:KochMM | lld:pubmed |
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pubmed-article:10806203 | pubmed:author | pubmed-author:TakaharaKK | lld:pubmed |
pubmed-article:10806203 | pubmed:author | pubmed-author:KeeneD RDR | lld:pubmed |
pubmed-article:10806203 | pubmed:author | pubmed-author:GereckeD RDR | lld:pubmed |
pubmed-article:10806203 | pubmed:author | pubmed-author:HudsonD LDL | lld:pubmed |
pubmed-article:10806203 | pubmed:author | pubmed-author:ChampliaudM... | lld:pubmed |
pubmed-article:10806203 | pubmed:author | pubmed-author:ScottI CIC | lld:pubmed |
pubmed-article:10806203 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10806203 | pubmed:day | 28 | lld:pubmed |
pubmed-article:10806203 | pubmed:volume | 275 | lld:pubmed |
pubmed-article:10806203 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10806203 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10806203 | pubmed:pagination | 22728-35 | lld:pubmed |
pubmed-article:10806203 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:10806203 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10806203 | pubmed:articleTitle | Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain. | lld:pubmed |
pubmed-article:10806203 | pubmed:affiliation | MGH/Harvard Cutaneous Biology Research Center, Massachusetts General Hospital, Charlestown, Massachusetts 02129, USA. | lld:pubmed |
pubmed-article:10806203 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10806203 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:10806203 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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