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http://purl.uniprot.org/citations/24005904http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24005904http://www.w3.org/2000/01/rdf-schema#comment"Macrophages play a critical role in chronic inflammation and metabolic diseases. We identified a longer splice variant of ubiquitin specific protease (USP) 2-69 as a novel molecule that modulates pathways implicated in metabolic disorders. Expression levels of aP2/FABP4 and PAI-1/SERPINE1 genes were increased by 4- and 1.8-fold, respectively, after short hairpin RNA-mediated knockdown (KD) of the USP2 gene, and such expression was alleviated by overexpression of USP2-69 in human myeloid cell lines. Supernatants derived from USP2-KD cells induced IL6 (∼6-fold) and SAA3 (∼15-fold) in 3T3-L1 adipocytes to suggest the anti-inflammatory properties of USP2. In addition, we observed a 30% decrease in the number of macrophages in mesenteric adipose tissue derived from USP2-69 transgenic mice fed a high-fat diet for 14 wk compared with that in their C57BL/6 littermates (P<0.01), which was consistent with a ∼40% decrease in transcription of aP2 and PAI-1. The aP2 locus exhibited elevated chromatin accessibility (>2.1-fold), methylation of histone H3 lysine 4 (>4.5-fold), and acetylation of histone H4 (>2.5-fold) in USP2-KD cells. Transfection of isopeptidase-mutated USP2-69 did not alter chromatin conformation on the aP2 locus in USP2-KD cells. Our results suggest that USP2-69 suppresses meta-inflammatory molecules involved in the development of type-2 diabetes."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.org/dc/terms/identifier"doi:10.1096/fj.13-233528"xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Miyamoto T."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Kitamura H."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Ito M."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Kimura S."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Ohara O."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Okamoto S."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Ishizuka M."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Hase K."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Naoe Y."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Shimamoto Y."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Kikuguchi C."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Miyoshi I."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Kanehira K."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Watarai H."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Okabe J."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Toda C."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"El-Osta A."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/author"Meek B."xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/name"FASEB J"xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/pages"4940-4953"xsd:string
http://purl.uniprot.org/citations/24005904http://purl.uniprot.org/core/title"Ubiquitin-specific protease 2-69 in macrophages potentially modulates metainflammation."xsd:string