{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,19]],"date-time":"2026-10-19T16:48:22Z","timestamp":1792428502093,"version":"4.5.0"},"reference-count":0,"publisher":"Oxford University Press (OUP)","issue":"3","content-domain":{"domain":["eje.bioscientifica.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1996,3]]},"abstract":"<jats:p>Diederich S, Quinkler M, Miller K, Heilmann P, Sch\u00f6nesh\u00f6fer M, Oelkers W. Human kidney 11\u03b2hydroxysteroid dehydrogenase: regulation by adrenocorticotropin? Eur J Endocrinol 1996;134:301\u20137. ISSN 0804\u20134643<\/jats:p>\n        <jats:p>In ectopic adrenocorticotropin (ACTH) syndrome (EAS) with higher ACTH levels than in pituitary Cushing's syndrome and during ACTH infusion, the ratio of cortisol to cortisone in plasma and urine is increased, suggesting inhibition of renal 11\u03b2-hydroxysteroid dehydrogenase (11\u03b2-HSD) by ACTH or by ACTH-dependent steroids. Measuring the conversion of cortisol to cortisone by human kidney slices under different conditions, we tested the possibility of 11\u03b2-HSD regulation by ACTH and corticosteroids. Slices prepared from unaffected parts of kidneys removed because of renal cell carcinoma were incubated with unlabeled or labeled cortisol, and cortisol and cortisone were quantitated after HPLC separation by UV or radioactive detection. The 11\u03b2-HSD activity was not influenced by incubation with increasing concentrations (10<jats:sup>\u221212<\/jats:sup>\u201310<jats:sup>\u22129<\/jats:sup> mol\/l) of ACTH (1\u201324 or 1\u201339) for 1 h. Among 12 ACTH-dependent steroids tested (10<jats:sup>\u22129<\/jats:sup>\u201310<jats:sup>\u22126<\/jats:sup> mol\/l), only corticosterone (IC<jats:sub>50<\/jats:sub> = 2 \u00d7 10<jats:sup>\u22127<\/jats:sup> mol\/l), 18-OH-corticosterone and 11\u03b2OH-androstenedione showed a significant dose-dependent inhibition of 11\u03b2-HSD activity. The percentage conversion rate of cortisol to cortisone was concentration dependent over the whole range of cortisol concentrations tested (10<jats:sup>\u22128<\/jats:sup>\u201310<jats:sup>\u22125<\/jats:sup> mol\/l). A direct inhibitory effect of ACTH on 11\u03b2-HSD is, therefore, unlikely. The only steroids inhibiting the conversion of cortisol to cortisone are natural substrates for 11\u03b2-HSD Kinetic studies show a saturation of the enzyme at high cortisol concentrations. Thus, the reduced percentage renal cortisol inactivation in EAS seems to be due mainly to overload of the enzyme with endogenous substrates (cortisol, corticosterone and others) rather than to direct inhibition of 11\u03b2-HSD by ACTH or ACTHdependent steroids, not being substrates of 11\u03b2-HSD.<\/jats:p>\n        <jats:p>S Diederich, Department of Endocrinology, Klinikum Benjamin Franklin, Freie Universit\u00e4t Berlin, Hindenburgdamm 30, 12200 Berlin, Germany<\/jats:p>","DOI":"10.1530\/eje.0.1340301","type":"journal-article","created":{"date-parts":[[2008,12,15]],"date-time":"2008-12-15T22:12:49Z","timestamp":1229379169000},"page":"301-307","update-policy":"https:\/\/doi.org\/10.1530\/crossmarkpolicy-1","source":"Crossref","is-referenced-by-count":26,"title":["Human kidney 11\u03b2-hydroxysteroid dehydrogenase: regulation by adrenocorticotropin?"],"prefix":"10.1093","volume":"134","author":[{"given":"S","family":"Diederich","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M","family":"Quinkler","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"K","family":"Miller","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P","family":"Heilmann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M","family":"Sch\u00f6nesh\u00f6fer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"W","family":"Oelkers","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","container-title":["European Journal of Endocrinology"],"original-title":[],"link":[{"URL":"https:\/\/eje.bioscientifica.com\/view\/journals\/eje\/134\/3\/eje_134_3_008.xml","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/eje.bioscientifica.com\/view\/journals\/eje\/134\/3\/eje_134_3_008.xml","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,2,14]],"date-time":"2023-02-14T16:21:45Z","timestamp":1676391705000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/ejendo\/article\/134\/3\/301\/6750984"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1996,3]]},"references-count":0,"journal-issue":{"issue":"3"},"URL":"https:\/\/doi.org\/10.1530\/eje.0.1340301","relation":{},"ISSN":["0804-4643","1479-683X"],"issn-type":[{"value":"0804-4643","type":"print"},{"value":"1479-683X","type":"electronic"}],"subject":[],"published":{"date-parts":[[1996,3]]}}}