The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Rat P45017αfrom Testis: Characterization of a Full-Length cDNA Encoding a Unique Steroid Hydroxylase Capable of Catalyzing Both Δ4- and Δ5-Steroid-17,20-Lyase Reactions
Open accessAbstract
A cDNA clone encoding the complete rat 17 alpha-hydroxylase (P450(17 alpha] from testis has been identified and sequenced. The deduced amino acid sequence is found to have 69% similarity with human P450(17 alpha), 64% similarity with bovine P450(17 alpha), and 47% similarity with chicken P450(17 alpha). The protein contains 507 amino acids being one amino acid shorter than the human P450(17 alpha) as the result of a codon being absent at the position of amino acid 139 in the human sequence. The cDNA hybridizes to a single mRNA (approximately 2.0 kilobases) in rat testis RNA and Southern analysis indicates the presence of a single CYP17 gene in the rat genome. Expression of this cDNA in COS1 cells leads to production of a steroid hydroxylase which is capable of converting both 17 alpha-hydroxypregnenolone and 17 alpha-hydroxyprogesterone into C19 steroids, dehydroepiandrosterone, and androstenedione, respectively. This activity profile is distinct from that of either the human or bovine forms of P450(17 alpha) which are unable to catalyze 17,20-lyase conversion of delta 4-C21 steroids to delta 4-C19 steroids at significant rates.
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Citations
Cites
Expression of Bovine 17α-Hydroxylase Cytochrome P-450 cDNA in Nonsteroidogenic (COS 1) Cells
Zuber, M. X., Simpson, E. R., & Waterman, M. R. (1986) · Science · doi:10.1126/science.3535074 · Cited by 388
Self-citationVOUTILAINEN, R., TAPANAINEN, J., CHUNG, B.-C., MATTESON, K. J., & MILLER, W. L. (1986) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem-63-1-202 · Cited by 253
Cited by
Overview of steroidogenic enzymes in the pathway from cholesterol to active steroid hormones
Payne, A. H., & Hales, D. B. (2004) · Endocrine Reviews · doi:10.1210/er.2003-0030 · Cited by 1,766
17α-Hydroxylase/17,20 lyase deficiency: from clinical investigation to molecular definition
YANASE, T., SIMPSON, E. R., & WATERMAN, M. R. (1991) · Endocrine Reviews · doi:10.1210/edrv-12-1-91 · Cited by 390
Self-citationFlück, C. E., Miller, W. L., & Auchus, R. J. (2003) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-030143 · Cited by 173
Androgen biosynthetic pathways in the human prostate
Luu-The, V., Bélanger, A., & Labrie, F. (2008) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2008.01.008 · Cited by 169
Missense mutation serine106—-proline causes 17 alpha-hydroxylase deficiency
Lin, D., Harikrishna, J. A., Moore, C. C., Jones, K. L., & Miller, W. L. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98506-6 · Cited by 135
Metadata
- Authors
- Fevold, H. R., Lorence, M. C., McCarthy, J. L., Trant, J. M., Kagimoto, M., Waterman, M. R., & Mason, J. I.
- Venue
- Molecular Endocrinology
- Publisher
- The Endocrine Society
- Published
- 1989-06
- Volume
- 3
- Issue
- 6
- Pages
- 968-975
- ISSN
- 0888-8809 (ISSN-L)
- 1944-9917
- OpenAlex
- W1995421298
- Cited by
- 159
- References
- 2
- FWCI
- 4.34
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Rat P45017αfrom Testis: Characterization of a Full-Length cDNA Encoding a Unique Steroid Hydroxylase Capable of Catalyzing Both Δ4- and Δ5-Steroid-17,20-Lyase Reactions. https://app.cochat.ai/papers/10.1210/mend-3-6-968
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- Fevold, H. R., Lorence, M. C., McCarthy, J. L., Trant, J. M., Kagimoto, M., Waterman, M. R., & Mason, J. I. (1989). Rat P45017αfrom Testis: Characterization of a Full-Length cDNA Encoding a Unique Steroid Hydroxylase Capable of Catalyzing Both Δ4- and Δ5-Steroid-17,20-Lyase Reactions. Molecular Endocrinology. https://doi.org/10.1210/mend-3-6-968
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
