Causevic, Maja; Mohaupt, Markus (2007). 11beta-Hydroxysteroid dehydrogenase type 2 in pregnancy and preeclampsia. Molecular aspects of medicine, 28(2), pp. 220-6. Amsterdam: Elsevier 10.1016/j.mam.2007.04.003
Full text not available from this repository. (Request a copy)Cortisol availability is controlled by 11beta-hydroxysteroid dehydrogenase type 2 (11beta-HSD2), which inactivates cortisol in cortisone, unable to bind to the glucocorticoid receptor. The 11beta-HSD2 enzyme activity limits either intracellular cortisol concentrations or within the uteroplacental compartment the transfer of cortisol into the fetal circulation. Mechanisms, by which 11beta-HSD2 activity is controlled, include transcriptional control, posttranscriptional modifications of 11beta-HSD2 transcript half-life, epigenetic regulation via methylation of genomic DNA and direct inhibition of enzymatic activity. The 11beta-HSD2 expression and activity is reduced in preeclampsia and the enzyme activity correlates with factors associated with increased vasoconstriction, such as an increased angiotensin II receptor subtype 1 expression, and notably fetal growth. Numerous signals such as proinflammatory cytokines known to be present and/or elevated in preeclampsia regulate 11beta-HSD2 activity. Shallow trophoblast invasion with the resulting hypoxemia seems to critically reduce available 11beta-HSD2 activity. A positive feedback exists as activated glucocorticoid receptors do enhance 11beta-HSD2 mRNA transcription and mRNA stability. No data are currently available on pregnancy and either epigenetic or direct effects on the activity of the translated enzyme.
Item Type: |
Journal Article (Further Contribution) |
|---|---|
Division/Institute: |
04 Faculty of Medicine > Department of Dermatology, Urology, Rheumatology, Nephrology, Osteoporosis (DURN) > Clinic of Nephrology and Hypertension |
UniBE Contributor: |
Mohaupt, Markus |
ISSN: |
0098-2997 |
ISBN: |
17532462 |
Publisher: |
Elsevier |
Language: |
English |
Submitter: |
Markus Georg Mohaupt |
Date Deposited: |
04 Oct 2013 14:54 |
Last Modified: |
05 Dec 2022 14:16 |
Publisher DOI: |
10.1016/j.mam.2007.04.003 |
PubMed ID: |
17532462 |
Web of Science ID: |
000247975400004 |
URI: |
https://boris.unibe.ch/id/eprint/23029 (FactScience: 38663) |
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