Data Entry: Please note that the research database will be replaced by UNIverse by the end of October 2023. Please enter your data into the system https://universe-intern.unibas.ch. Thanks

Login for users with Unibas email account...

Login for registered users without Unibas email account...

 
11β-Hydroxysteroid dehydrogenase 1: Regeneration of active glucocorticoids is only part of the story
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 3266645
Author(s) Odermatt, Alex; Klusonova, Petra
Author(s) at UniBasel Odermatt, Alex
Klusonova, Petra
Year 2015
Title 11β-Hydroxysteroid dehydrogenase 1: Regeneration of active glucocorticoids is only part of the story
Journal The journal of steroid biochemistry and molecular biology
Volume 151
Pages / Article-Number 85-92
Abstract 11β-Hydroxysteroid dehydrogenase 1 (11β-HSD1) is an endoplasmic reticulum membrane enzyme with its catalytic site facing the luminal space. It functions primarily as a reductase, driven by the supply of its cosubstrate NADPH by hexose-6-phosphate dehydrogenase (H6PDH). Extensive research has been performed on the role of 11β-HSD1 in the regeneration of active glucocorticoids and its role in inflammation and metabolic disease. Besides its important role in the fine-tuning of glucocorticoid action, 11β-HSD1 is a multi-functional carbonyl reductase converting several 11- and 7-oxosterols into the respective 7-hydroxylated forms. Moreover, 11β-HSD1 has a role in phase I biotransformation reactions and catalyzes the carbonyl reduction of several non-steroidal xenobiotics. Recent observations from experiments using selective inhibitors and studies with transgenic mice indicated a role for 11β-HSD1 in oxysterol metabolism and in bile acid homeostasis, with evidence for glucocorticoid-independent effects on gene expression. This review focuses on the promiscuity of 11β-HSD1 to accept structurally distinct substrates and discusses recent progress mainly on non-glucocorticoid substrates. This article is part of a Special Issue entitled 'Enzyme Promiscuity and Diversity'.
Publisher Pergamon
ISSN/ISBN 0960-0760
edoc-URL http://edoc.unibas.ch/39520/
Full Text on edoc No
Digital Object Identifier DOI 10.1016/j.jsbmb.2014.08.011
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/25151952
Document type (ISI) Journal Article, Review
 
   

MCSS v5.8 PRO. 0.358 sec, queries - 0.000 sec ©Universität Basel  |  Impressum   |    
29/03/2024