Structure and tissue-specific expression of 3ß-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase genes in human and rat classical and peripheral steroidogenic tissues
Abstract
The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones. We have recently characterized two types of human 3 beta-HSD cDNA clones and the corresponding genes which encode deduced proteins of 371 and 372 amino acids, respectively, and share 93.5% homology. The human 3 beta-HSD genes containing 4 exons were assigned by in situ hybridization to the p11-p13 region of the short arm of chromosome 1. We have also recently elucidated the structure of three types of rat 3 beta-HSD cDNAs as well as that of one type of 3 beta-HSD from bovine and macaque ovary lambda gt11 cDNA libraries which all encode 372 amino acid proteins. The human type I 3 beta-HSD is the almost exclusive mRNA species detected in the placenta and skin, while the human type II is the predominant mRNA species in the adrenals, ovaries and testes. The predicted rat type I and type II 3 beta-HSD proteins expressed in adrenals, gonads and adipose tissue share 94% homology while they share 80% similarity with the liver-specific type III 3 beta-HSD. Transient expression of human type I and type II as well as rat type I and type II 3 beta-HSD cDNAs in HeLa human cervical carcinoma cells reveals that 3 beta-ol dehydrogenase and 5-ene-4-ene isomerase activities reside within a single protein and these cDNAs encode functional 3 beta-HSD proteins that are capable of converting 3 beta-hydroxy-5-ene-steroids into 3-keto-4-ene derivatives as well as the interconversion of 3 beta-hydroxy and 3-keto-5 alpha-androstane steroids. We have found that the rat type III mRNA species was below the detection limit in intact female liver while, following hypophysectomy, its accumulation increased to 55% of the levels measured in intact or HYPOX male rats, an increase which can be blocked by administration of ovine prolactin (oPRL). In addition, in female rats, treatment with oPRL for 10 days starting 15 days after HYPOX, markedly decreased ovarian 3 beta-HSD mRNA accumulation accompanied by a similar decrease in 3 beta-HSD activity and protein levels. Treatment with the gonadotropin hCG reversed the potent inhibitory effect of oPRL on these parameters and stimulated 3 beta-HSD mRNA levels in ovarian interstitial cells.(ABSTRACT TRUNCATED AT 400 WORDS)
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Enzymes required for formation of androgens and estrogens are expressed in rat peripheral tissues.
“the enzymes required for the formation of androgens and estrogens are expressed in rat peripheral tissues (260,261).”
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 [261]
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 [261]
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- Authors
- Labrie, F., Simard, J., Luu-The, V., Pelletier, G., Bélanger, A., Lachance, Y., Zhao, H. F., Labrie, C., Breton, N., de Launoit, Y., Dumont, M., Dupont, E., Rhéaume, E., Martel, C., Couët, J., & Trudel, C.
- Affiliations
- Centre hospitalier de l'Université Laval (CA)
- Université Laval (CA)
- Corresponding author
- Labrie, F.
- Venue
- The Journal of Steroid Biochemistry and Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1992-03
- Volume
- 41
- Issue
- 3-8
- Pages
- 421-435
- ISSN
- 0960-0760 (ISSN-L)
- OpenAlex
- W2039836892
- Cited by
- 88
- References
- 51
- Citations by year
- 2023: 2 · 2021: 1 · 2020: 1 · 2019: 2 · 2018: 1 · 2017: 3 · 2015: 1 · 2014: 3 · 2013: 4 · 2012: 1
- FWCI
- 2.34
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The Journal of Steroid Biochemistry and Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Steroid Chemistry and Biochemistry
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
- Keywords
- 3β-hydroxysteroid dehydrogenase, steroidogenic enzymes, gene structure, chromosome 1, tissue-specific gene expression, placenta, adrenal gland, ovary, testis, liver, hypophysectomy, cDNA cloning, protein homology, enzyme activity, steroidogenesis
- MeSH terms
- Amino Acid Sequence, Animals, Female, Genes, Humans, Isoenzymes, Molecular Sequence Data, Multienzyme Complexes, Organ Specificity, Ovary, Progesterone Reductase, Sequence Homology, Nucleic Acid, Steroid Isomerases, Gene Library, Gene Expression Regulation, Enzymologic, Rats
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