| http://purl.uniprot.org/citations/22940536 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22940536 | http://www.w3.org/2000/01/rdf-schema#comment | "The atherogenic 7-oxysterols, 7-ketocholesterol (7-KC) and 7β-hydroxycholesterol (7βOHC), can directly impair arterial function. Inter-conversion of 7-KC and 7βOHC has recently been shown as a novel role for the glucocorticoid-metabolizing enzyme 11β-hydroxysteroid dehydrogenase type 1 (11β-HSD1). Since this enzyme is expressed in vascular smooth muscle cells, we addressed the hypothesis that inter-conversion of 7-KC and 7βOHC by 11β-HSD1 may contribute to regulation of arterial function. Incubation (4-24 h) of aortic rings with either 7-KC (25 μM) or 7βOHC (20 μM) had no effect on endothelium-dependent (acetylcholine) or -independent (sodium nitroprusside) relaxation. In contrast, exposure to 7-KC (but not to 7βOHC) attenuated noradrenaline-induced contraction (E(max)) after 4 h (0.78 ± 0.28 vs 0.40 ± 0.08 mN/mm; p < 0.05) and 24 h (2.28 ± 0.34 vs 1.56 ± 0.48 mN/mm; p < 0.05). Both 7-oxysterols were detected by GCMS in the aortic wall of chow-fed C57Bl6/J mice, with concentrations of 7-KC (1.41 ± 0.81 ng/mg) higher (p = 0.05) than 7βOHC (0.16 ± 0.06 ng/mg). In isolated mouse aortic rings 11β-HSD1 was shown to act as an oxo-reductase, inter-converting 7-KC and 7βOHC. This activity was lost in aorta from 11β-HSD1(-/-) mice, which had low oxysterol levels. Renal homogenates from 11β-HSD1(-/-) mice were used to confirm that the type 2 isozyme of 11β-HSD does not inter-convert 7-KC and 7βOHC. These results demonstrate that 7-KC has greater effects than 7βOHC on vascular function, and that 11β-HSD1 can inter-convert 7-KC and 7βOHC in the arterial wall, contributing to the regulation of 7-oxysterol levels and potentially influencing vascular function. This mechanism may be important in the cardioprotective effects of 11β-HSD1 inhibitors."xsd:string |
| http://purl.uniprot.org/citations/22940536 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.biochi.2012.08.007"xsd:string |
| http://purl.uniprot.org/citations/22940536 | http://purl.uniprot.org/core/author | "Andrew R."xsd:string |
| http://purl.uniprot.org/citations/22940536 | http://purl.uniprot.org/core/author | "Walker B.R."xsd:string |
| http://purl.uniprot.org/citations/22940536 | http://purl.uniprot.org/core/author | "Hadoke P.W."xsd:string |
| http://purl.uniprot.org/citations/22940536 | http://purl.uniprot.org/core/author | "Mitic T."xsd:string |
| http://purl.uniprot.org/citations/22940536 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/22940536 | http://purl.uniprot.org/core/name | "Biochimie"xsd:string |
| http://purl.uniprot.org/citations/22940536 | http://purl.uniprot.org/core/pages | "548-555"xsd:string |
| http://purl.uniprot.org/citations/22940536 | http://purl.uniprot.org/core/title | "11beta-Hydroxysteroid dehydrogenase type 1 contributes to the regulation of 7-oxysterol levels in the arterial wall through the inter-conversion of 7-ketocholesterol and 7beta-hydroxycholesterol."xsd:string |
| http://purl.uniprot.org/citations/22940536 | http://purl.uniprot.org/core/volume | "95"xsd:string |
| http://purl.uniprot.org/citations/22940536 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22940536 |
| http://purl.uniprot.org/citations/22940536 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22940536 |
| http://purl.uniprot.org/uniprot/#_P50172-mappedCitation-22940536 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/22940536 |
| http://purl.uniprot.org/uniprot/#_Q4JHD9-mappedCitation-22940536 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/22940536 |
| http://purl.uniprot.org/uniprot/#_Q3TJI8-mappedCitation-22940536 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/22940536 |
| http://purl.uniprot.org/uniprot/P50172 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/22940536 |
| http://purl.uniprot.org/uniprot/Q4JHD9 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/22940536 |
| http://purl.uniprot.org/uniprot/Q3TJI8 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/22940536 |