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http://purl.uniprot.org/citations/29669734http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29669734http://www.w3.org/2000/01/rdf-schema#comment"Secreted and cell-surface proteases are major mediators of extracellular matrix (ECM) turnover, but their mechanisms and regulatory impact are poorly understood. We developed a mass spectrometry approach using a cell-free ECM produced in vitro to identify fibronectin (FN) as a novel substrate of the secreted metalloprotease ADAMTS16. ADAMTS16 cleaves FN between its (I)5 and (I)6 modules, releasing the N-terminal 30 kDa heparin-binding domain essential for FN self-assembly. ADAMTS16 impairs FN fibrillogenesis as well as fibrillin-1 and tenascin-C assembly, thus inhibiting formation of a mature ECM by cultured fibroblasts. Furthermore ADAMTS16 has a marked morphogenetic impact on spheroid formation by renal tubule-derived MDCKI cells. The N-terminal FN domain released by ADAMTS16 up-regulates MMP3, which cleaves the (I)5-(I)6 linker of FN similar to ADAMTS16, therefore creating a proteolytic feed-forward mechanism. Thus, FN proteolysis not only regulates FN turnover, but also FN assembly, with potential long-term consequences for ECM assembly and morphogenesis."xsd:string
http://purl.uniprot.org/citations/29669734http://purl.org/dc/terms/identifier"doi:10.1074/mcp.ra118.000676"xsd:string
http://purl.uniprot.org/citations/29669734http://purl.uniprot.org/core/author"Hess D."xsd:string
http://purl.uniprot.org/citations/29669734http://purl.uniprot.org/core/author"Sack R."xsd:string
http://purl.uniprot.org/citations/29669734http://purl.uniprot.org/core/author"Mosher D.F."xsd:string
http://purl.uniprot.org/citations/29669734http://purl.uniprot.org/core/author"Apte S.S."xsd:string
http://purl.uniprot.org/citations/29669734http://purl.uniprot.org/core/author"Annis D.S."xsd:string
http://purl.uniprot.org/citations/29669734http://purl.uniprot.org/core/author"Chiquet-Ehrismann R."xsd:string
http://purl.uniprot.org/citations/29669734http://purl.uniprot.org/core/author"Schnellmann R."xsd:string
http://purl.uniprot.org/citations/29669734http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/29669734http://purl.uniprot.org/core/name"Mol Cell Proteomics"xsd:string
http://purl.uniprot.org/citations/29669734http://purl.uniprot.org/core/pages"1410-1425"xsd:string
http://purl.uniprot.org/citations/29669734http://purl.uniprot.org/core/title"A Selective Extracellular Matrix Proteomics Approach Identifies Fibronectin Proteolysis by A Disintegrin-like and Metalloprotease Domain with Thrombospondin Type 1 Motifs (ADAMTS16) and Its Impact on Spheroid Morphogenesis."xsd:string
http://purl.uniprot.org/citations/29669734http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/29669734http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/29669734
http://purl.uniprot.org/citations/29669734http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/29669734
http://purl.uniprot.org/uniprot/#_Q69Z28-mappedCitation-29669734http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/29669734
http://purl.uniprot.org/uniprot/Q69Z28http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/29669734