Cited by 53Aldose Reductase and TaurineSteroid Chemistry and BiochemistryHormonal Regulation and Hypertension

Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3α-hydroxysteroid dehydrogenase

Qin, Ke-Nan, New, Maria I., Cheng, K.-C.·1993·The Journal of Steroid Biochemistry and Molecular Biology

Abstract

Rat liver 3 alpha-hydroxysteroid dehydrogenase cDNA was previously cloned by us. In this study, we used the rat cDNA as the probe to screen a human liver lambda gt11 cDNA library. A total of four different cDNAs were identified and sequenced. The sequence of one of the cDNAs is identical to that of the human chlordecone reductase cDNA except that our clone contains a much longer 5'-coding sequence than previously reported. The other three cDNAs display high degrees of sequence homology to those of both rat 3 alpha-hydroxysteroid dehydrogenase and human chlordecone reductase. Because 3 alpha-hydroxysteroid dehydrogenase and human chlordecone reductase belong to the aldo-keto reductase superfamily, we named these human clones HAKRa to HAKRd. Northern blot analysis showed that the liver expresses the highest levels of all four clones. Expression of all four clones was also detected in the brain, kidney, lung, and testis, whereas the placenta expressed only the messenger RNA for HAKRb. Genomic blot analysis using HAKRb as the probe detected multiple DNA fragments hybridized to the probe and a high degree of restriction fragment length polymorphism, suggesting the complexity of this supergene family.

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Crossref · 10.1016/0960-0760(93)90308-j

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Authors
Qin, K.-N., New, M. I., & Cheng, K.-C.
Affiliations
Cornell University (US)
Corresponding author
Cheng, K.-C.
Venue
The Journal of Steroid Biochemistry and Molecular Biology
Publisher
Elsevier BV
Published
1993-12
Volume
46
Issue
6
Pages
673-679
ISSN
0960-0760 (ISSN-L)
OpenAlex
W2025844136
Cited by
53
References
22
Citations by year
2026: 1 · 2023: 1 · 2021: 1 · 2019: 1 · 2016: 1 · 2015: 1 · 2013: 1
FWCI
1.23
Type
journal article
Language
en
Open access
closed
Locations
  • The Journal of Steroid Biochemistry and Molecular Biology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (7r01dk044177-04)
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK44177)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Steroid Chemistry and Biochemistry
  • Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Hormonal Regulation and Hypertension
Keywords
3α-hydroxysteroid dehydrogenase, aldo-keto reductase superfamily, cDNA cloning, human liver, tissue expression, restriction fragment length polymorphism, sequence homology
MeSH terms
Alcohol Oxidoreductases, Amino Acid Sequence, Animals, Base Sequence, Brain, Cloning, Molecular, Female, Humans, Kidney, Liver, Lung, Male, Molecular Sequence Data, Organ Specificity, Placenta, Pregnancy, Sequence Homology, Nucleic Acid, Testis, 3-Hydroxysteroid Dehydrogenases, DNA Probes, Gene Library, Sequence Homology, Amino Acid, DNA, Complementary, 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific), Rats, NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases

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