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http://purl.uniprot.org/citations/19151918http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19151918http://www.w3.org/2000/01/rdf-schema#comment"ADAMTS-12, a metalloproteinase that belongs to ADAMTS family, is strongly upregulated during chondrogenesis and demonstrates prominent expression in the growth plate chondrocytes. ADAMTS-12 potently inhibits chondrocyte differentiation, as revealed by altered expression of both early and later genes critical for chondrogenesis. In addition, ADAMTS-12-mediated inhibition of chondrogenesis depends on its enzymatic activity, since its point mutant lacking enzymatic activity completely loses this activity. Furthermore, the C-terminal four thrombospondin motifs known to bind COMP substrate is necessary for its full proteolytic activity and inhibition of chondrocyte differentiation. Mechanism studies demonstrate that ADAMTS-12 induces PTHrP, whereas it inhibits IHH during chondrogenesis. Furthermore, PTHrP induces ADAMTS-12 and ADAMTS-12 is hardly detectable in PTHrP-/-growth plate chondrocytes. Importantly, knocking down ADAMTS-12 mRNA levels or blocking ADAMTS-12 activity almost abolishes the PTHrP-mediated inhibition of type X collagen expression. Collectively, these findings demonstrate that ADAMTS-12, a downstream molecule of PTHrP signaling, is a novel regulator of chondrogenesis."xsd:string
http://purl.uniprot.org/citations/19151918http://purl.org/dc/terms/identifier"doi:10.1007/s00018-008-8633-x"xsd:string
http://purl.uniprot.org/citations/19151918http://purl.uniprot.org/core/author"Bai X.H."xsd:string
http://purl.uniprot.org/citations/19151918http://purl.uniprot.org/core/author"Liu C.J."xsd:string
http://purl.uniprot.org/citations/19151918http://purl.uniprot.org/core/author"Luan Y."xsd:string
http://purl.uniprot.org/citations/19151918http://purl.uniprot.org/core/author"Wang D.W."xsd:string
http://purl.uniprot.org/citations/19151918http://purl.uniprot.org/core/author"Yu X.P."xsd:string
http://purl.uniprot.org/citations/19151918http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19151918http://purl.uniprot.org/core/name"Cell Mol Life Sci"xsd:string
http://purl.uniprot.org/citations/19151918http://purl.uniprot.org/core/pages"667-680"xsd:string
http://purl.uniprot.org/citations/19151918http://purl.uniprot.org/core/title"Regulation of chondrocyte differentiation by ADAMTS-12 metalloproteinase depends on its enzymatic activity."xsd:string
http://purl.uniprot.org/citations/19151918http://purl.uniprot.org/core/volume"66"xsd:string
http://purl.uniprot.org/citations/19151918http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19151918
http://purl.uniprot.org/citations/19151918http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19151918
http://purl.uniprot.org/uniprot/#_D6REX0-mappedCitation-19151918http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19151918
http://purl.uniprot.org/uniprot/#_P58397-mappedCitation-19151918http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19151918
http://purl.uniprot.org/uniprot/P58397http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19151918
http://purl.uniprot.org/uniprot/D6REX0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19151918