| http://purl.uniprot.org/citations/17467270 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17467270 | http://www.w3.org/2000/01/rdf-schema#comment | "Dehydroepiandrosterone (DHEA) is 7alpha-hydroxylated by the cytochome P450 7B1 (CYP7B1) in the human brain and liver. This produces 7alpha-hydroxy-DHEA that is a substrate for 11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1) which exists in the same tissues and carries out the inter-conversion of 7alpha- and 7beta-hydroxy-DHEA through a 7-oxo-intermediary. Since the role of 11beta-HSD1 is to transform the inactive cortisone into active cortisol, its competitive inhibition by 7alpha-hydroxy-DHEA may support the paradigm of native anti-glucocorticoid arising from DHEA. Therefore, our objective was to use human tissues to assess the presences of both CYP7B1 and 11beta-HSD1. Human skin was selected then and used to test its ability to produce 7alpha-hydroxy-DHEA, and to test the interference of 7alpha- and 7beta-hydroxy-DHEA and 7-oxo-DHEA with the 11beta-HSD1-mediated oxidoreduction of cortisol and cortisone. Immuno-histochemical studies showed the presence of both CYP7B1 and 11beta-HSD1 in the liver, skin and tonsils. DHEA was readily 7alpha-hydroxylated when incubated using skin slices. A S9 fraction of dermal homogenates containing the 11beta-HSD1 carried out the oxidoreduction of cortisol and cortisone. Inhibition of the cortisol oxidation by 7alpha-hydroxy-DHEA and 7beta-hydroxy-DHEA was competitive with a Ki at 1.85+/-0.495 and 0.255+/-0.005 microM, respectively. Inhibition of cortisone reduction by 7-oxo-DHEA was of a mixed type with a Ki at 1.13+/-0.15 microM. These findings may support the previously proposed native anti-glucocorticoid paradigm and suggest that the 7alpha-hydroxy-DHEA production is a key for the fine tuning of glucocorticoid levels in tissues."xsd:string |
| http://purl.uniprot.org/citations/17467270 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jsbmb.2007.03.026"xsd:string |
| http://purl.uniprot.org/citations/17467270 | http://purl.uniprot.org/core/author | "Morfin R."xsd:string |
| http://purl.uniprot.org/citations/17467270 | http://purl.uniprot.org/core/author | "Hennebert O."xsd:string |
| http://purl.uniprot.org/citations/17467270 | http://purl.uniprot.org/core/author | "Chalbot S."xsd:string |
| http://purl.uniprot.org/citations/17467270 | http://purl.uniprot.org/core/author | "Alran S."xsd:string |
| http://purl.uniprot.org/citations/17467270 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17467270 | http://purl.uniprot.org/core/name | "J Steroid Biochem Mol Biol"xsd:string |
| http://purl.uniprot.org/citations/17467270 | http://purl.uniprot.org/core/pages | "326-333"xsd:string |
| http://purl.uniprot.org/citations/17467270 | http://purl.uniprot.org/core/title | "Dehydroepiandrosterone 7alpha-hydroxylation in human tissues: possible interference with type 1 11beta-hydroxysteroid dehydrogenase-mediated processes."xsd:string |
| http://purl.uniprot.org/citations/17467270 | http://purl.uniprot.org/core/volume | "104"xsd:string |
| http://purl.uniprot.org/citations/17467270 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17467270 |
| http://purl.uniprot.org/citations/17467270 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17467270 |
| http://purl.uniprot.org/uniprot/#_O75881-mappedCitation-17467270 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17467270 |
| http://purl.uniprot.org/uniprot/#_Q05C57-mappedCitation-17467270 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17467270 |
| http://purl.uniprot.org/uniprot/O75881 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/17467270 |
| http://purl.uniprot.org/uniprot/Q05C57 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/17467270 |