Cited by 139Steroid Chemistry and BiochemistryCholesterol and Lipid MetabolismAldose Reductase and Taurine

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Cloning and expression of cDNA of human Δ4‐3‐oxosteroid 5β‐reductase and substrate specificity of the expressed enzyme

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KONDO, Kazu‐Hiro, KAI, Masa‐Hiro, SETOGUCHI, Yoshiko, EGGERTSEN, Gösta, SJÖBLOM, Peter, SETOGUCHI, Toshiaki, OKUDA, Kyu‐Ichiro, BJÖRKHEM, Ingemar·1994·European Journal of Biochemistry

DOI 10.1111/j.1432-1033.1994.tb19947.x

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Abstract

The enzyme delta 4-3-oxosteroid 5 beta-reductase (3-oxo-5 beta-steroid: NADP+ oxidoreductase and 4,5 beta-dihydrocortisone: NADP+ delta 4-oxidoreductase) catalyzes the reduction of the delta 4 double bond of bile acid intermediates and steroid hormones carrying the delta 4-3-one structure in the A/B cis configuration. Human delta 4-3-oxosteroid 5 beta-reductase cDNA was isolated from a liver cDNA library by cross hybridization with a previously cloned rat cDNA, which was used as a probe [Onishi, Y. Noshiro, M., Shimosato, T. & Okuda, K.-I. (1991) FEBS Lett. 283, 215-218]. DNA sequence analysis of a hybridization-positive clone predicted the human delta 4-3-oxosteroid 5 beta-reductase to contain 326 amino acids. The amino acid sequence of the human delta 4-3-oxosteroid 5 beta-reductase had 79% overall identity to the rat enzyme sequence. It also showed 54% and 50% overall identity with rat 3 alpha-hydroxysteroid dehydrogenase and human aldose reductase, respectively. RNA blotting analysis demonstrated the existence of a single delta 4-3-oxosteroid 5 beta-reductase mRNA of approximately 2.7 kb in human liver. Transfection of the cDNA into COS cells resulted in the expression of an active enzyme with a high activity toward the bile acid intermediates 7 alpha,12 alpha-dihydroxy-4-cholesten-3-one and 7 alpha-hydroxy-4-cholesten-3-one. In addition, the expressed enzyme showed a small but significant 5 beta-reduction activity toward 11 beta,17 alpha,21-trihydroxy-delta 4-pregnene-3,20-dione (cortisol) and 17 beta-hydroxy-delta 4-androsten-3-one (testosterone) whereas no activity was observed toward delta 4-pregnene-3,20-dione (progesterone) or delta 4-androstene-3-17-dione (androstenedione). The substrate specificity of the human enzyme is considerably narrower than that of the rat enzyme, and the enzyme seems to be more important for bile acid biosynthesis than for metabolism of steroid hormones.

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Authors: KONDO, K., KAI, M., SETOGUCHI, Y., EGGERTSEN, G., SJÖBLOM, P., SETOGUCHI, T., OKUDA, K., & BJÖRKHEM, I.
Affiliations: Karolinska Institutet (SE)
University of Miyazaki (JP)
Corresponding author: KONDO, Kazu‐Hiro
ORCID: SJÖBLOM, Peter
SETOGUCHI, Toshiaki
BJÖRKHEM, Ingemar
Venue: European Journal of Biochemistry
Publisher: Wiley
Published: 1994-01
Volume: 219
Issue: 1-2
Pages: 357-363
ISSN: 0014-2956 (ISSN-L)
1432-1033
DOI: 10.1111/j.1432-1033.1994.tb19947.x
OpenAlex: W1985481419
Cited by: 139
References: 36
Citations by year: 2025: 3 · 2024: 2 · 2023: 3 · 2022: 1 · 2021: 3 · 2020: 3 · 2019: 4 · 2018: 4 · 2017: 7 · 2016: 3 · 2015: 3 · 2014: 7 · 2013: 5 · 2012: 7
FWCI: 1.52
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 4079 d)
Locations: European Journal of Biochemistry (publishedVersion)
PubMed (publishedVersion)
Topics: Physical Sciences › Chemistry › Organic Chemistry › Steroid Chemistry and Biochemistry
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
Keywords: human cDNA cloning, substrate specificity, bile acid intermediates, 3α-hydroxysteroid dehydrogenase, aldose reductase, liver mRNA, recombinant enzyme expression, cortisol reduction, testosterone suppression
MeSH terms: Amino Acid Sequence, Animals, Base Sequence, Cell Line, Cloning, Molecular, Escherichia coli, Humans, Liver, Molecular Sequence Data, Oxidoreductases, Recombinant Proteins, RNA, Substrate Specificity, Transfection, Immunoblotting, Restriction Mapping, Gene Expression, Sequence Homology, Amino Acid, DNA, Complementary, Rats

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Cloning and expression of cDNA of human Δ4‐3‐oxosteroid 5β‐reductase and substrate specificity of the expressed enzyme

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