Structure-function relationships and molecular genetics of the 3β-hydroxysteroid dehydrogenase gene family

Simard, Jacques; Sanchez, Rocio; Durocher, Francine; Rhéaume, Eric; Turgeon, Carl; Labrie, Yvan; Luu-The, Van; Mebarki, Farida; Morel, Yves; de Launoit, Yvan; Labrie, Fernand

doi:10.1016/0960-0760(95)00198-0

Cited by 24Sexual Differentiation and DisordersAdrenal Hormones and DisordersSteroid Chemistry and Biochemistry

Structure-function relationships and molecular genetics of the 3β-hydroxysteroid dehydrogenase gene family

Simard, Jacques, Sanchez, Rocio, Durocher, Francine, Rhéaume, Eric, Turgeon, Carl, Labrie, Yvan, Luu-The, Van, Mebarki, Farida +3 more·1995·The Journal of Steroid Biochemistry and Molecular Biology

DOI 10.1016/0960-0760(95)00198-0

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Abstract

The isoenzymes of the 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene-isomerase (3 beta-HSD) gene family catalyse the transformation of all 5-ene-3 beta-hydroxysteroids into the corresponding 4-ene-3-keto-steroids and are responsible for the interconversion of 3 beta-hydroxy- and 3-keto-5 alpha-androstane steroids. The two human 3 beta-HSD genes and the three related pseudogenes are located on the chromosome 1p13.1 region, close to the centromeric marker D1Z5. The 3 beta-HSD isoenzymes prefer NAD+ to NADP+ as cofactor with the exception of the rat liver type III and mouse kidney type IV, which both prefer NADPH as cofactor for their specific 3-ketosteroid reductase activity due to the presence of Tyr36 in the rat type III and of Phe36 in mouse type IV enzymes instead of Asp36 found in other 3 beta-HSD isoenzymes. The rat types I and IV, bovine and guinea pig 3 beta-HSD proteins possess an intrinsic 17 beta-HSD activity specific to 5 alpha-androstane 17 beta-ol steroids, thus suggesting that such "secondary" activity is specifically responsible for controlling the bioavailability of the active androgen DHT. To elucidate the molecular basis of classical form of 3 beta-HSD deficiency, the structures of the types I and II 3 beta-HSD genes in 12 male pseudohermaphrodite 3 beta-HSD deficient patients as well as in four female patients were analyzed. The 14 different point mutations characterized were all detected in the type II 3 beta-HSD gene, which is the gene predominantly expressed in the adrenals and gonads, while no mutation was detected in the type I 3 beta-HSD gene predominantly expressed in the placenta and peripheral tissues. The mutant type II 3 beta-HSD enzymes carrying mutations detected in patients affected by the salt-losing form exhibit no detectable activity in intact transfected cells, at the exception of L108W and P186L proteins, which have some residual activity (approximately 1%). Mutations found in nonsalt-loser patients have some residual activity ranging from approximately 1 to approximately 10% compared to the wild-type enzyme. Characterization of mutant proteins provides unique information on the structure-function relationships of the 3 beta-HSD superfamily.

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Enzyme isoforms vary greatly between species, so care should be taken when using animal models to study intracrinology.
“It should again be noted that care should be taken when using animal models to study intracrinology as the enzyme isoforms vary greatly between species.”
From Intracrine androgen biosynthesis, metabolism and action revisited (2018) · cites this paper as Simard et al., 1995

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Structure-function relationships of 3β-hydroxysteroid dehydrogenase: contribution made by the molecular genetics of 3β-hydroxysteroid dehydrogenase deficiency
Morel, Y., Mébarki, F., Rhéaume, E., Sanchez, R., Forest, M. G., & Simard, J. (1997) · Steroids · doi:10.1016/s0039-128x(96)00178-x · Cited by 67 · see citing works
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Structure, function and tissue-specific gene expression of 3β-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase enzymes in classical and peripheral intracrine steroidogenic tissues.
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Expression of liver-specific member of the 3 beta-hydroxysteroid dehydrogenase family, an isoform possessing an almost exclusive 3-ketosteroid reductase activity.
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Structure and Expression of a New Complementary DNA Encoding the almost Exclusive 3β-Hydroxysteroid Dehydrogenase/Δ 5 -Δ 4 -lsomerase in Human Adrenals and Gonads
Rhéaume, E., Lachance, Y., Zhao, H.-F., Breton, N., Dumont, M., Launoit, Y. D., Trudel, C., Luu-The, V., Simard, J., & Labrie, F. (1991) · Molecular Endocrinology · doi:10.1210/mend-5-8-1147 · Cited by 362 · see citing works
Self-citation

Authors: Simard, J., Sanchez, R., Durocher, F., Rhéaume, E., Turgeon, C., Labrie, Y., Luu-The, V., Mebarki, F., Morel, Y., de Launoit, Y., & Labrie, F.
Affiliations: Centre hospitalier de l'Université Laval (CA)
Université Laval (CA)
Inserm (FR)
Corresponding author: Simard, Jacques
ORCID: Simard, Jacques
Durocher, Francine
Morel, Yves
Venue: The Journal of Steroid Biochemistry and Molecular Biology
Publisher: Elsevier BV
Published: 1995-12
Volume: 55
Issue: 5-6
Pages: 489-505
ISSN: 0960-0760 (ISSN-L)
DOI: 10.1016/0960-0760(95)00198-0
OpenAlex: W2030229758
Cited by: 24
References: 108
Citations by year: 2023: 1 · 2022: 1 · 2020: 1 · 2019: 1 · 2017: 2 · 2016: 1 · 2012: 1
FWCI: 0.87
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: The Journal of Steroid Biochemistry and Molecular Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sexual Differentiation and Disorders
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Steroid Chemistry and Biochemistry
Keywords: 3β-hydroxysteroid dehydrogenase, 17β-hydroxysteroid dehydrogenase, 5α-reductase, pseudogenes, pseudohermaphroditism, point mutations, residual enzyme activity, structure-function relationship
MeSH terms: Amino Acid Sequence, Animals, Cattle, Chromosome Mapping, Endocrine System Diseases, Female, Genes, Humans, Isoenzymes, Kinetics, Male, Molecular Sequence Data, Multienzyme Complexes, Progesterone Reductase, Steroid Isomerases, Structure-Activity Relationship, Trout, 3-Hydroxysteroid Dehydrogenases, Sequence Alignment, Point Mutation, Sequence Homology, Amino Acid, Mice, Rats

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Structure-function relationships and molecular genetics of the 3β-hydroxysteroid dehydrogenase gene family

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