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http://purl.uniprot.org/citations/21304964http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21304964http://www.w3.org/2000/01/rdf-schema#comment"Recent studies demonstrated expression and activity of the intracellular cortisone-cortisol shuttle 11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1) in skeletal muscle and inhibition of 11beta-HSD1 in muscle cells improved insulin sensitivity. Glucocorticoids induce muscle atrophy via increased expression of the E3 ubiquitin ligases Atrogin-1 (Muscle Atrophy F-box (MAFbx)) and MuRF-1 (Muscle RING-Finger-1). We hypothesized that 11beta-HSD1 controls glucocorticoid-induced expression of atrophy E3 ubiquitin ligases in skeletal muscle. Primary human myoblasts were generated from healthy volunteers. 11beta-HSD1-dependent protein degradation was analyzed by [(3)H]-tyrosine release assay. RT-PCR was used to determine mRNA expression of E3 ubiquitin ligases and 11beta-HSD1 activity was measured by conversion of radioactively labeled [(3)H]-cortisone to [(3)H]-cortisol separated by thin-layer chromatography. We here demonstrate that 11beta-HSD1 is expressed and biologically active in interconverting cortisone to active cortisol in murine skeletal muscle cells (C2C12) as well as in primary human myotubes. 11Beta-HSD1 expression increased during differentiation from myoblasts to mature myotubes (p < 0.01), suggesting a role of 11beta-HSD1 in skeletal muscle growth and differentiation. Treatment with cortisone increased protein degradation by about 20% (p < 0.001), which was paralleled by an elevation of Atrogin-1 and MuRF-1 mRNA expression (p < 0.01, respectively). Notably, pre-treatment with the 11beta-HSD1 inhibitor carbenoxolone (Cbx) completely abolished the effect of cortisone on protein degradation as well as on Atrogin-1 and MuRF-1 expression. In summary, our data suggest that 11beta-HSD1 controls glucocorticoid-induced protein degradation in human and murine skeletal muscle via regulation of the E3 ubiquitin ligases Atrogin-1 and MuRF-1."xsd:string
http://purl.uniprot.org/citations/21304964http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0016674"xsd:string
http://purl.uniprot.org/citations/21304964http://purl.uniprot.org/core/author"Adams S."xsd:string
http://purl.uniprot.org/citations/21304964http://purl.uniprot.org/core/author"Mai K."xsd:string
http://purl.uniprot.org/citations/21304964http://purl.uniprot.org/core/author"Spranger J."xsd:string
http://purl.uniprot.org/citations/21304964http://purl.uniprot.org/core/author"Spuler S."xsd:string
http://purl.uniprot.org/citations/21304964http://purl.uniprot.org/core/author"Andres J."xsd:string
http://purl.uniprot.org/citations/21304964http://purl.uniprot.org/core/author"Fielitz J."xsd:string
http://purl.uniprot.org/citations/21304964http://purl.uniprot.org/core/author"Biedasek K."xsd:string
http://purl.uniprot.org/citations/21304964http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21304964http://purl.uniprot.org/core/name"PLoS One"xsd:string
http://purl.uniprot.org/citations/21304964http://purl.uniprot.org/core/pages"e16674"xsd:string
http://purl.uniprot.org/citations/21304964http://purl.uniprot.org/core/title"Skeletal muscle 11beta-HSD1 controls glucocorticoid-induced proteolysis and expression of E3 ubiquitin ligases atrogin-1 and MuRF-1."xsd:string
http://purl.uniprot.org/citations/21304964http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/21304964http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21304964
http://purl.uniprot.org/citations/21304964http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21304964
http://purl.uniprot.org/uniprot/#_F2Z3U6-mappedCitation-21304964http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21304964
http://purl.uniprot.org/uniprot/#_F6TSI8-mappedCitation-21304964http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21304964
http://purl.uniprot.org/uniprot/#_I6L984-mappedCitation-21304964http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21304964
http://purl.uniprot.org/uniprot/#_P28845-mappedCitation-21304964http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21304964
http://purl.uniprot.org/uniprot/#_P50172-mappedCitation-21304964http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21304964
http://purl.uniprot.org/uniprot/#_Q4JHD9-mappedCitation-21304964http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21304964
http://purl.uniprot.org/uniprot/#_Q0VAQ6-mappedCitation-21304964http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21304964
http://purl.uniprot.org/uniprot/#_Q3TJI8-mappedCitation-21304964http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21304964