Linked Life Data

12553867

Source:http://linkedlifedata.com/resource/pubmed/id/12553867

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-1-29
pubmed:abstractText
The 11beta-hydroxysteroid dehydrogenases (11beta-HSDs) convert cortisol to its inactive metabolite cortisone and vice versa. 11beta-HSD type 1 (11beta-HSD-1) functions as a reductase in vivo, regulating intracellular cortisol levels and its access to the glucocorticoid receptor. In contrast, 11beta-HSD-2 only mediates oxidation of natural glucocorticoids, and protects the mineralocorticoid receptor from high cortisol concentrations. We investigated the in vivo and in vitro effects of ACTH on the recently characterized 11beta-HSDs in guinea pig liver and kidney. Tissue slices of untreated guinea pigs were incubated with (3)H-labelled cortisol or cortisone and ACTH(1-24) (10(-10) and 10(-9) mol/l). The 11beta-HSD activities in liver and kidney slices were not influenced by in vitro incubation with ACTH(1-24). In addition, guinea pigs were treated with ACTH(1-24) or saline injections s.c. for 3 days. Liver and kidney tissue slices of these animals were incubated with (3)H-labelled cortisol or cortisone. In vivo ACTH treatment significantly increased reductase and decreased oxidase activity in liver and kidney. Furthermore, 11beta-HSD-1 activity assessed by measurement of the urinary ratio of (tetrahydrocortisol (THF)+5alphaTHF)/(tetrahydrocortisone) was significantly increased after ACTH treatment compared with the control group. Plasma levels of cortisol, cortisone, progesterone, 17-hydroxyprogesterone and androstenedione increased significantly following in vivo ACTH treatment. The enhanced reductase activity of the hepatic and renal 11beta-HSD-1 is apparently caused by cortisol or other ACTH-dependent steroids rather than by ACTH itself. This may be an important fine regulation of the glucocorticoid tonus for stress adaptation in every organ, e.g. enhanced gluconeogenesis in liver.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-0795
pubmed:author
pubmed:issnType
Print
pubmed:volume
176
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
185-92
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12553867-11-beta-Hydroxysteroid Dehydrogenases, pubmed-meshheading:12553867-17-alpha-Hydroxyprogesterone, pubmed-meshheading:12553867-Adaptation, Psychological, pubmed-meshheading:12553867-Adrenocorticotropic Hormone, pubmed-meshheading:12553867-Androstenedione, pubmed-meshheading:12553867-Animals, pubmed-meshheading:12553867-Anti-Inflammatory Agents, pubmed-meshheading:12553867-Cortisone, pubmed-meshheading:12553867-Culture Techniques, pubmed-meshheading:12553867-Enzyme Activation, pubmed-meshheading:12553867-Guinea Pigs, pubmed-meshheading:12553867-Hydrocortisone, pubmed-meshheading:12553867-Hydroxysteroid Dehydrogenases, pubmed-meshheading:12553867-Kidney, pubmed-meshheading:12553867-Liver, pubmed-meshheading:12553867-Male, pubmed-meshheading:12553867-Progesterone, pubmed-meshheading:12553867-Stimulation, Chemical, pubmed-meshheading:12553867-Stress, Psychological
pubmed:year
2003
pubmed:articleTitle
Enhanced 11beta-hydroxysteroid dehydrogenase type 1 activity in stress adaptation in the guinea pig.
pubmed:affiliation
Department of Endocrinology, Klinikum Benjamin Franklin, Freie Universität Berlin, Berlin, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't