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Integrated view on 17beta-hydroxysteroid dehydrogenases
Abstract
17beta-Hydroxysteroid dehydrogenases (17beta-HSDs) are important enzymes in steroid metabolism. Long known members of the protein family seemed to be well characterised concerning their role in the regulation of the biological potency of steroid hormones, but today more and more evidence points to pivotal contributions of these enzymes in a variety of other metabolic pathways. Therefore, studies on 17beta-HSDs develop towards metabolomic survey. Latest research results give new insights into the complex metabolic interconnectivity of the 17beta-HSDs. In this paper metabolic activities of 17beta-HSDs will be compared, their interplay with endogenous substrates summarised, and interlacing pathways depicted. Strategies on deciphering the physiological role of 17beta-HSDs and the genetic predisposition for associated diseases will be presented.
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“Mutations in CYP11B2 selectively impair aldosterone synthesis, causing hyponatremia and hyperkalemia with normal cortisol production (39,90).”
From Congenital Adrenal Hyperplasia—Current Insights in Pathophysiology, Diagnostics, and Management (2022) · cites this paper as [90]
In the citing paper
“Generally, these enzymes are multi-functional and often have overlapping substrate specificities and expression patterns, allowing for redundant enzymes to cover in case of deficiency of another enzyme [107,114].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [114]
In the citing paper
“To date, 14 human enzymes with 17β-HSD/oxoreductase activities have been identified [105,106,113].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [106]
In the citing paper
“The majority of 5α/β-3α-metabolites of testosterone and DHT, which contain a 17β-hydroxy, are converted to 17-keto steroids by the action of the oxidative 17β-HSDs, HSD17B2 and HSD17B4 [106].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [106]
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Flagged first, then by citations
8 of the 176 references couldn’t be matched to a known paper.
Research works printed but not linked: 2
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A Protein-Truncating HSD17B13 Variant and Protection from Chronic Liver Disease
Abul-Husn, N. S., Cheng, X., Li, A. H., Xin, Y., Schurmann, C., Stevis, P., Liu, Y., Kozlitina, J., Stender, S., Wood, G. C., et al. (2018) · New England Journal of Medicine · doi:10.1056/nejmoa1712191 · Cited by 827
Congenital Adrenal Hyperplasia—Current Insights in Pathophysiology, Diagnostics, and Management
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“20 enzymes to cover in case of deficiency of another enzyme [107,114].”
Genome-wide association study identifies 143 loci associated with 25 hydroxyvitamin D concentration
Revez, J. A., Lin, T., Qiao, Z., Xue, A., Holtz, Y., Zhu, Z., Zeng, J., Wang, H., Sidorenko, J., Kemper, K. E., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15421-7 · Cited by 416
An ADIOL-ERβ-CtBP Transrepression Pathway Negatively Regulates Microglia-Mediated Inflammation
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“However, there are at least 14 different members of the 17β-HSD family identified in humans and mice, and some of them could also potentially convert DHEA to ADIOL (Moeller and Adamski, 2009).”
Metadata
- Authors
- Moeller, G., & Adamski, J.
- Affiliations
- Helmholtz Munich (DE)
- ORCID
- Adamski, Jerzy
- Venue
- Molecular and Cellular Endocrinology
- Publisher
- Elsevier BV
- Published
- 2009-03
- Volume
- 301
- Issue
- 1-2
- Pages
- 7-19
- ISSN
- 0303-7207 (ISSN-L)
- OpenAlex
- W2048714965
- Cited by
- 214
- References
- 176
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 12 · 2023: 8 · 2022: 6 · 2021: 8 · 2020: 11 · 2019: 8 · 2018: 17 · 2017: 12 · 2016: 14 · 2015: 12 · 2014: 11 · 2013: 16 · 2012: 11
- FWCI
- 1.52
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Molecular and Cellular Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- Site cant be reached (submittedVersion)
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Steroid Chemistry and Biochemistry
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Hormonal Regulation and Hypertension
- Keywords
- 17β-hydroxysteroid dehydrogenase, steroid metabolism, steroid hormone regulation, metabolomics, endogenous substrates, genetic susceptibility, disease
- MeSH terms
- Animals, Disease, Humans, Polymorphism, Genetic, 17-Hydroxysteroid Dehydrogenases, Crystallography, X-Ray, Models, Animal
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