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Cited by 271Hormonal Regulation and HypertensionAdrenal Hormones and DisordersEstrogen and related hormone effects

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Human placental 11 beta-hydroxysteroid dehydrogenase: evidence for and partial purification of a distinct NAD-dependent isoform.

Brown, R W, Chapman, K E, Edwards, C R, Seckl, J R·1993·Endocrinology
DOI 10.1210/endo.132.6.8504762
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Abstract

Excess glucocorticoids impair fetal growth and cause teratogenesis. Placental 11 beta-hydroxysteroid dehydrogenase (11 beta HSD) catalyzes the inactivation of cortisol to cortisone, preventing the high maternal cortisol levels from reaching the fetal circulation and thus preserving the low cortisol fetal environment. In previous work, an NADP-dependent isoform of 11 beta HSD has been purified from rat liver, a cDNA isolated, and the human homolog cloned. However, much evidence suggests tissue-specific 11 beta HSD activities that cannot be explained by the liver-type isoform. Therefore, we have partially purified human placental 11 beta HSD and compared it to the enzyme in rat liver. Human placental subcellular fractions exhibited NAD-dependent 11 beta HSD activity, but showed little activity with NADP. The enzyme had a pH optimum of 7-8.5 (peak, 7.7), was only sparingly soluble in detergents (solubility with Triton X-100 was very poor), and exhibited little latency or change in pH profile in detergent solution. By contrast, rat liver 11 beta HSD was exclusively NADP dependent and was easily solubilized by a wide range of detergents (including Triton X-100), revealing substantial latency and altered pH profile [optimum of 10, becoming 7-10 (peak, 9.5) in detergent]. These data do not merely reflect species differences, as rat placental 11 beta HSD was similar to the human placental isoform. AMP affinity chromatography, which was completely without affinity for rat liver 11 bet…

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Metadata

Authors
Brown, R. W., Chapman, K. E., Edwards, C. R., & Seckl, J. R.
Affiliations
Western General Hospital (GB)
ORCID
Venue
Endocrinology
Publisher
The Endocrine Society
Published
1993-06
Volume
132
Issue
6
Pages
2614-2621
ISSN
  • 0013-7227 (ISSN-L)
  • 1945-7170
DOI
10.1210/endo.132.6.8504762
OpenAlex
W1994741408
Cited by
271
References
0
Citations by year
2025: 1 · 2024: 1 · 2023: 4 · 2022: 2 · 2021: 6 · 2020: 1 · 2019: 2 · 2018: 3 · 2017: 5 · 2016: 4 · 2015: 9 · 2014: 6 · 2013: 8 · 2012: 5
FWCI
17.81
Type
journal article
Language
en
Open access
closed
Locations
  • Endocrinology (publishedVersion)
  • PubMed (publishedVersion)
Funders
Wellcome Trust
Topics
  • Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Hormonal Regulation and Hypertension
  • Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
Keywords
11β-hydroxysteroid dehydrogenase, enzyme purification, cortisol, cortisone, placenta, rat liver, subcellular fractionation, detergent solubility, pH optimum
MeSH terms
Animals, Chromatography, Affinity, Detergents, Female, Humans, Hydrogen-Ion Concentration, Hydroxysteroid Dehydrogenases, Isoenzymes, Liver, Male, NAD, Placenta, Solubility, Subcellular Fractions, Substrate Specificity, Tissue Distribution, Rats, Wistar, 11-beta-Hydroxysteroid Dehydrogenases, Rats

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Brown, R. W., Chapman, K. E., Edwards, C. R., & Seckl, J. R. (1993). Human placental 11 beta-hydroxysteroid dehydrogenase: evidence for and partial purification of a distinct NAD-dependent isoform. Endocrinology. https://doi.org/10.1210/endo.132.6.8504762