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http://purl.uniprot.org/citations/24971753http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24971753http://www.w3.org/2000/01/rdf-schema#comment"Lysyl oxidase is a multifunctional enzyme required for collagen biosynthesis. Various growth factors regulate lysyl oxidase during osteoblast differentiation, subject to modulation by cytokines such as TNF-α in inflammatory osteopenic disorders including diabetic bone disease. Canonical Wnt signaling promotes osteoblast development. Here we investigated the effect of Wnt3a and TNF-α on lysyl oxidase expression in pluripotent C3H10T1/2 cells, bone marrow stromal cells, and committed osteoblasts. Lysyl oxidase was up-regulated by a transcriptional mechanism 3-fold in C3H10T1/2 cells, and 2.5-fold in bone marrow stromal cells. A putative functional TCF/LEF element was identified in the lysyl oxidase promoter. Interestingly, lysyl oxidase was not up-regulated in committed primary rat calvarial- or MC3T3-E1 osteoblasts. TNF-α down-regulated lysyl oxidase both in Wnt3a-treated and in non-treated C3H10T1/2 cells by a post-transcriptional mechanism mediated by miR203. Non-differentiated cells do not produce a collagen matrix; thus, a novel biological role for lysyl oxidase in pluripotent cells was investigated. Lysyl oxidase shRNAs effectively silenced lysyl oxidase expression, and suppressed the growth of C3H10T1/2 cells by 50%, and blocked osteoblast differentiation. We propose that interference with lysyl oxidase expression under excess inflammatory conditions such as those that occur in diabetes, osteoporosis, or rheumatoid arthritis can result in a diminished pool of pluripotent cells which ultimately contributes to osteopenia."xsd:string
http://purl.uniprot.org/citations/24971753http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0100669"xsd:string
http://purl.uniprot.org/citations/24971753http://purl.uniprot.org/core/author"Khosravi R."xsd:string
http://purl.uniprot.org/citations/24971753http://purl.uniprot.org/core/author"Bais M.V."xsd:string
http://purl.uniprot.org/citations/24971753http://purl.uniprot.org/core/author"Trackman P.C."xsd:string
http://purl.uniprot.org/citations/24971753http://purl.uniprot.org/core/author"Saxena D."xsd:string
http://purl.uniprot.org/citations/24971753http://purl.uniprot.org/core/author"Xu W.P."xsd:string
http://purl.uniprot.org/citations/24971753http://purl.uniprot.org/core/author"Faibish M."xsd:string
http://purl.uniprot.org/citations/24971753http://purl.uniprot.org/core/author"Sodek K.L."xsd:string
http://purl.uniprot.org/citations/24971753http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24971753http://purl.uniprot.org/core/name"PLoS One"xsd:string
http://purl.uniprot.org/citations/24971753http://purl.uniprot.org/core/pages"e100669"xsd:string
http://purl.uniprot.org/citations/24971753http://purl.uniprot.org/core/title"A novel function for lysyl oxidase in pluripotent mesenchymal cell proliferation and relevance to inflammation-associated osteopenia."xsd:string
http://purl.uniprot.org/citations/24971753http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/24971753http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24971753
http://purl.uniprot.org/citations/24971753http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24971753
http://purl.uniprot.org/uniprot/#_A6IX14-mappedCitation-24971753http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24971753
http://purl.uniprot.org/uniprot/#_P16636-mappedCitation-24971753http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24971753
http://purl.uniprot.org/uniprot/A6IX14http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24971753
http://purl.uniprot.org/uniprot/P16636http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24971753