Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:11358968rdf:typepubmed:Citationlld:pubmed
pubmed-article:11358968lifeskim:mentionsumls-concept:C0262950lld:lifeskim
pubmed-article:11358968lifeskim:mentionsumls-concept:C0033235lld:lifeskim
pubmed-article:11358968lifeskim:mentionsumls-concept:C1709694lld:lifeskim
pubmed-article:11358968lifeskim:mentionsumls-concept:C0086597lld:lifeskim
pubmed-article:11358968lifeskim:mentionsumls-concept:C1707271lld:lifeskim
pubmed-article:11358968pubmed:issue29lld:pubmed
pubmed-article:11358968pubmed:dateCreated2001-7-16lld:pubmed
pubmed-article:11358968pubmed:abstractTextThe processing of the fibrillar procollagen precursors to mature collagens is an essential requirement for fibril formation. The enzymes involved in these events are known as the procollagen N and C proteinases. The latter, which cleaves the C-propeptides of the fibrillar procollagens I-III, is identical to the previously described bone morphogenetic protein-1 (BMP-1). Surprisingly, unlike the other fibrillar collagens, the processing of the C-propeptide domain of the procollagen V homotrimer was found to be mediated by furin rather than BMP-1. However, the presence of putative BMP-1 cleavage sites in the alpha1(V) C-propeptide sequence prompted us to reconsider the procollagen V C-propeptide cleavage by BMP-1. Using a recombinant system to produce substantial amounts of the proalpha1(V) homotrimer, we have previously shown that the C-propeptide is spontaneously released in the culture medium. The trimeric C-propeptide fragment, resulting from the furin cleavage, still encompassed the predicted BMP-1 cleavage sites. It was purified and tested as a substrate for BMP-1. In parallel, the release of the C-propeptide in the culture medium was inhibited by the addition of a specific furin inhibitor, allowing the re-examination of BMP-1 activity on the intact molecule. We showed that BMP-1 does cleave both substrates at one of the two predicted C-proteinase cleavage sites. Our results favor a role for PCP/BMP-1 in physiological C-terminal processing of procollagen V and imply a general mechanism for fibrillar collagen C-terminal processing.lld:pubmed
pubmed-article:11358968pubmed:languageenglld:pubmed
pubmed-article:11358968pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11358968pubmed:citationSubsetIMlld:pubmed
pubmed-article:11358968pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11358968pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11358968pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11358968pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11358968pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11358968pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11358968pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:11358968pubmed:statusMEDLINElld:pubmed
pubmed-article:11358968pubmed:monthJullld:pubmed
pubmed-article:11358968pubmed:issn0021-9258lld:pubmed
pubmed-article:11358968pubmed:authorpubmed-author:KesslerEElld:pubmed
pubmed-article:11358968pubmed:authorpubmed-author:RuggieroFFlld:pubmed
pubmed-article:11358968pubmed:authorpubmed-author:FichardAAlld:pubmed
pubmed-article:11358968pubmed:authorpubmed-author:BruselMMlld:pubmed
pubmed-article:11358968pubmed:authorpubmed-author:Chanut-Delala...lld:pubmed
pubmed-article:11358968pubmed:issnTypePrintlld:pubmed
pubmed-article:11358968pubmed:day20lld:pubmed
pubmed-article:11358968pubmed:volume276lld:pubmed
pubmed-article:11358968pubmed:ownerNLMlld:pubmed
pubmed-article:11358968pubmed:authorsCompleteYlld:pubmed
pubmed-article:11358968pubmed:pagination27051-7lld:pubmed
pubmed-article:11358968pubmed:dateRevised2008-11-21lld:pubmed
pubmed-article:11358968pubmed:meshHeadingpubmed-meshheading:11358968...lld:pubmed
pubmed-article:11358968pubmed:meshHeadingpubmed-meshheading:11358968...lld:pubmed
pubmed-article:11358968pubmed:meshHeadingpubmed-meshheading:11358968...lld:pubmed
pubmed-article:11358968pubmed:meshHeadingpubmed-meshheading:11358968...lld:pubmed
pubmed-article:11358968pubmed:meshHeadingpubmed-meshheading:11358968...lld:pubmed
pubmed-article:11358968pubmed:meshHeadingpubmed-meshheading:11358968...lld:pubmed
pubmed-article:11358968pubmed:meshHeadingpubmed-meshheading:11358968...lld:pubmed
pubmed-article:11358968pubmed:meshHeadingpubmed-meshheading:11358968...lld:pubmed
pubmed-article:11358968pubmed:meshHeadingpubmed-meshheading:11358968...lld:pubmed
pubmed-article:11358968pubmed:meshHeadingpubmed-meshheading:11358968...lld:pubmed
pubmed-article:11358968pubmed:meshHeadingpubmed-meshheading:11358968...lld:pubmed
pubmed-article:11358968pubmed:year2001lld:pubmed
pubmed-article:11358968pubmed:articleTitleBone morphogenetic protein-1 (BMP-1) mediates C-terminal processing of procollagen V homotrimer.lld:pubmed
pubmed-article:11358968pubmed:affiliationTel-Aviv University Sackler Faculty of Medicine, Goldschleger Eye Research Institute, Sheba Medical Center, Tel-Hashomer 52621, Israel.lld:pubmed
pubmed-article:11358968pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11358968pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11358968lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11358968lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11358968lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11358968lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11358968lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:11358968lld:pubmed