Cited by 361Sexual Differentiation and DisordersSteroid Chemistry and BiochemistryAdrenal Hormones and Disorders

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The role of 17 beta-hydroxysteroid dehydrogenases

Mindnich, R, Möller, G, Adamski, J·2004·Molecular and Cellular Endocrinology

DOI 10.1016/j.mce.2003.12.006

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Abstract

The biological activity of steroid hormones is regulated at the pre-receptor level by several enzymes including 17 beta-hydroxysteroid dehydrogenases (17 beta -HSD). The latter are present in many microorganisms, invertebrates and vertebrates. Dysfunctions in human 17 beta-hydroxysteroid dehydrogenases result in disorders of biology of reproduction and neuronal diseases, the enzymes are also involved in the pathogenesis of various cancers. 17 beta-hydroxysteroid dehydrogenases reveal a remarkable multifunctionality being able to modulate concentrations not only of steroids but as well of fatty and bile acids. Current knowledge on genetics, biochemistry and medical implications is presented in this review.

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Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs
Okazaki, Y., Furuno, M., Kasukawa, T., Adachi, J., Bono, H. U., Kondo, S., Nikaido, I., Osato, N., Saito, R., Suzuki, H., et al. (2002) · Nature · doi:10.1038/nature01266 · Cited by 1,660
Short-chain dehydrogenases/reductases (SDR)
Jörnvall, H., Persson, B., Krook, M., Atrian, S., Gonzàlez‐Duarte, R., Jeffery, J., & Ghosh, D. (1995) · Biochemistry · doi:10.1021/bi00018a001 · Cited by 1,241
Hormonal carcinogenesis
Henderson, B. E., & Feigelson, H. S. (2000) · Carcinogenesis · doi:10.1093/carcin/21.3.427 · Cited by 821
Human 3α-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones
PENNING, T. M., BURCZYNSKI, M. E., JEZ, J. M., HUNG, C.-F., LIN, H.-K., MA, H., MOORE, M., PALACKAL, N., & RATNAM, K. (2000) · Biochemical Journal · doi:10.1042/bj3510067 · Cited by 649
Short-chain dehydrogenases/reductases (SDR): the 2002 update
Oppermann, U. C. T., Filling, C., Hult, M., Shafqat, N., Wu, X., Lindh, M., Shafqat, J., Nordling, E., Kallberg, Y., Persson, B., et al. (2003) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00164-3 · Cited by 633
Male pseudohermaphroditism caused by mutations of testicular 17β-hydroxysteroid dehydrogenase 3
Geissler, W. M., Davis, D. L., Wu, L., Bradshaw, K. D., Patel, S., Mendonca, B. B., Elliston, K. O., Wilson, J. D., Russell, D. W., & Andersson, S. (1994) · Nature Genetics · doi:10.1038/ng0594-34 · Cited by 570
Neurosteroid metabolism in the human brain
Stoffel‐Wagner, B. (2001) · European Journal of Endocrinology · doi:10.1530/eje.0.1450669 · Cited by 546
Oestrogen as a neuroprotective hormone
Behl, C. (2002) · Nature reviews. Neuroscience · doi:10.1038/nrn846 · Cited by 489
Expression cloning and characterization of human 17 beta-hydroxysteroid dehydrogenase type 2, a microsomal enzyme possessing 20 alpha-hydroxysteroid dehydrogenase activity
Wu, L., Einstein, M., Geissler, W. M., Chan, H. K., Elliston, K. O., & Andersson, S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31480-7 · Cited by 437
Ligand binding was acquired during evolution of nuclear receptors
Escrivá, H., Safi, R., Hänni, C., Langlois, M., Saumitou‐Laprade, P., Stéhelin, D., Capron, A., Pierce, R. J., & Laudet, V. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.13.6803 · Cited by 403

Show all 203 references

Research works printed but not linked: 5

Brereton, 2001, Pan1b (17betaHSD11): enzymatic activity and distribution in the lung, Mol. Cell Endocrinol., 171/2, 111, 10.1016/S0303-7207(00)00417-2 · DOI
Liu, H., Robert, A., Luu-The, V., 2001. Structure and expression of the gene of a second form of human type 7 17beta-HSD. In: The Endocrine Society 83rd Annual Meeting, Denver, CO, USA, pp. 430.
Mendonca, 1999, 17Beta-hydroxysteroid dehydrogenase 3 deficiency in women, J. Clin. Endocrinol. Metab., 84, 802, 10.1210/jc.84.2.802 · DOI · Paper page
Mindnich, R., Deluca, D., Adamski, J. Identification and characterization of 17beta-hydroxysteroid dehydrogenases in the zebrafish, Danio rerio, Mol. Cell Endocrinol., in press.
Zhang, Y., Dufort, I., Soucy, P., Labrie, F., Luu-The, V., 1995. Cloning and expression of human type V 17β-hydroxysteroid dehydrogenase. In: Proceedings of the 77th Annual Meeting of the Endocrine Society, Washington, DC, pp. 622.

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Authors: Mindnich, R., Möller, G., & Adamski, J.
Affiliations: Helmholtz Munich (DE)
Corresponding author: Adamski, J
ORCID: Möller, G
Adamski, J
Venue: Molecular and Cellular Endocrinology
Publisher: Elsevier BV
Published: 2004-04
Volume: 218
Issue: 1-2
Pages: 7-20
ISSN: 0303-7207 (ISSN-L)
DOI: 10.1016/j.mce.2003.12.006
OpenAlex: W2083859759
Cited by: 354
References: 203
Citations by year: 2026: 7 · 2025: 11 · 2024: 9 · 2023: 8 · 2022: 13 · 2021: 14 · 2020: 9 · 2019: 11 · 2018: 12 · 2017: 12 · 2016: 13 · 2015: 15 · 2014: 14 · 2013: 8 · 2012: 10
FWCI: 2.84
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Molecular and Cellular Endocrinology (publishedVersion)
PubMed (publishedVersion)
Site cant be reached (submittedVersion)
Funders: Deutsche Forschungsgemeinschaft
Topics: Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Sexual Differentiation and Disorders
Physical Sciences › Chemistry › Organic Chemistry › Steroid Chemistry and Biochemistry
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
Keywords: 17β-hydroxysteroid dehydrogenase, steroid hormone metabolism, steroidogenesis, reproductive disorders, neuronal diseases, carcinogenesis, fatty acid metabolism, bile acid metabolism, enzyme genetics, enzyme biochemistry
MeSH terms: Androgens, Animals, Estrogens, Humans, 17-Hydroxysteroid Dehydrogenases, Molecular Structure

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The role of 17 beta-hydroxysteroid dehydrogenases

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