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11 Structure, regulation and role of 3β-hydroxysteroid dehydrogenase, 17β-hydroxysteroid dehydrogenase and aromatase enzymes in the formation of sex steroids in classical and peripheral intracrine tissues
Abstract
In addition to the classical steroidogenic tissues, namely the ovaries, testes, adrenals and placenta, a large series of human peripheral tissues possess all the enzymatic systems required for the formation of active androgens and oestrogens from a relatively large supply of precursor steroids provided by the adrenals. This chapter describes the structure, function, tissue-specific expression and regulation of the 3 beta-HSD and 17 beta-HSD gene families as well as some information about the aromatase gene. While, so far, most therapeutic approaches have been aimed and limited at controlling steroid formation by the classical steroidogenic tissues, it is clear that major efforts should now be turned towards intracrinology in order to understand better the physiological mechanisms controlling local steroid formation in peripheral target tissues and thus be in a position to develop novel therapeutic approaches that take into account the high proportion of steroids that are made locally and are responsible for the growth and function of normal as well as cancerous tissue.
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Women at menopause are not only deprived from estrogens because of rapid loss of ovarian activity but also have been deprived from androgens for a longer period because of progressive decrease of serum DHEA levels starting years before menopause.
“women, at menopause, are not only deprived from estrogens because of a rapid loss of ovarian activity but also have been deprived from androgens for a longer period because of a progressive decrease of serum DHEA levels starting quite a few years before menopause.”
From Endocrine and intracrine sources of androgens in women: inhibition of breast cancer and other roles of androgens and their precursor dehydroepiandrosterone (2003) · cites this paper as [90]
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Self-citationCouët, J., Martel, C., Labrie, Y., Luo, S., Simard, J., & Labrie, F. (1994) · Journal of Investigative Dermatology · doi:10.1111/1523-1747.ep12389663 · Cited by 10
Self-citationSimard, J., Zhao, H. F., Labrie, C., et al. (1991) · Springer eBooks · doi:10.1007/978-1-4612-3200-1_28 · Cited by 3
Self-citation
Flagged first, then by citations
Research works printed but not linked: 2
- Dupont, 1992, Immunochemical localization of 3β-hydroxysteroid dehydrogenase/Δ5-Δ4 isomerase (3β-HSD) in human ovary, Journal of Clinical Endocrinology and Metabolism, 74, 994, 10.1210/jc.74.5.994 · DOI
- Riley, 1992, Immunohistochemical localization of 3β-hydroxy-5-ene-steroid dehydrogenase/Δ5-Δ4 isomerase in human placenta and fetal membranes, Journal of Clinical Endocrinology and Metabolism, 96, 127
Cited by
Sorted by citations
Labrie, F., Luu-The, V., Labrie, C., Bélanger, A., Simard, J., Lin, S.-X., & Pelletier, G. (2003) · Endocrine Reviews · doi:10.1210/er.2001-0031 · Cited by 544
Self-citationLabrie, F., Luu-The, V., Labrie, C., & Simard, J. (2001) · Frontiers in Neuroendocrinology · doi:10.1006/frne.2001.0216 · Cited by 366
Self-citationThe 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 · Cited by 354
Hahner, S., Ross, R. J., Arlt, W., Bancos, I., Burger-Stritt, S., Torpy, D. J., Husebye, E. S., & Quinkler, M. (2021) · Nature Reviews Disease Primers · doi:10.1038/s41572-021-00252-7 · Cited by 223
Arlt, W., Justl, H.-G., Callies, F., Reincke, M., Hübler, D., Oettel, M., Ernst, M., Schulte, H. M., & Allolio, B. (1998) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.83.6.4850 · Cited by 199
Oral Androstenedione Administration and Serum Testosterone Concentrations in Young Men
Leder, B. Z. (2000) · JAMA · doi:10.1001/jama.283.6.779 · Cited by 135
Effect of dehydroepiandrosterone on vaginal and uterine histomorphology in the rat.
Sourla, A., Flamand, M., Bélanger, A., & Labrie, F. (1998) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(98)00052-1 · Cited by 40
Self-citationSimard, J., Sanchez, R., Durocher, F., Rhéaume, E., Turgeon, C., Labrie, Y., Luu-The, V., Mebarki, F., Morel, Y., de Launoit, Y., et al. (1995) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/0960-0760(95)00198-0 · Cited by 24
Self-citation
Metadata
- Authors
- Labrie, F., Simard, J., Luu-The, V., Pelletier, G., Belghmi, K., & Bélanger, A.
- Affiliations
- Centre hospitalier de l'Université Laval (CA)
- ORCID
- Simard, Jacques
- Venue
- Baillière s Clinical Endocrinology and Metabolism
- Publisher
- Elsevier BV
- Published
- 1994-04
- Volume
- 8
- Issue
- 2
- Pages
- 451-474
- ISSN
- 0950-351X (ISSN-L)
- OpenAlex
- W2032143202
- Cited by
- 78
- References
- 114
- Citations by year
- 2023: 1 · 2022: 1 · 2021: 1 · 2014: 4 · 2013: 1
- FWCI
- 1.89
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Baillière s Clinical Endocrinology and Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
- Physical Sciences › Chemistry › Organic Chemistry › Steroid Chemistry and Biochemistry
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
- Keywords
- 3β-hydroxysteroid dehydrogenase, 17β-hydroxysteroid dehydrogenase, aromatase, sex steroid biosynthesis, tissue-specific gene expression, steroidogenic enzyme regulation, androgens, estrogen, adrenal steroids, intracrinology
- MeSH terms
- Amino Acid Sequence, Animals, Aromatase, Chemistry, Genes, Humans, Isoenzymes, Molecular Sequence Data, Gonadal Steroid Hormones, Structure-Activity Relationship, 17-Hydroxysteroid Dehydrogenases, 3-Hydroxysteroid Dehydrogenases, Chemical Phenomena
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