Deletion of steroid 5α-reductase 2 gene in male pseudohermaphroditism

Stefan Andersson, David M. Berman, Elizabeth P. Jenkins, David W. Russell

Research output: Contribution to journalArticle

573 Citations (Scopus)

Abstract

THE conversion of testosterone into dihydrotestosterone by steroid 5α-reductase is a key reaction in androgen action, and is essential both for the formation of the male phenotype during embryogenesis and for androgen-mediated growth of tissues such as the prostate1,2. Single gene defects that impair this conversion lead to pseudohermaphroditism in which 46 X, Y males have male internal urogenital tracts, but female external genitalia3. We have described the isolation of a human 5α-reductase complementary DNA from prostate4. Subsequent cloning and genetic studies showed that this gene (designated 5α-reductase 1) was normal in patients with 5α-reductase deficiency26. We report here the isolation of a second 5α-reductase cDNA by expression cloning and the polymerase chain reaction. The biochemical and pharmacological properties of this cDNA-encoded enzyme (designated 5α-reductase 2) are consistent with it being the major isozyme in genital tissue. A deletion in this gene is present in two related individuals with male pseudohermaphroditism caused by 5α-reductase deficiency. These results verify the existence of at least two 5α-reductases in man and provide insight into a fundamental hormone-mediated event in male sexual differentiation.

Original languageEnglish (US)
Pages (from-to)159-161
Number of pages3
JournalNature
Volume354
Issue number6349
StatePublished - Nov 14 1991

Fingerprint

XY Disorders of Sex Development 46
Oxidoreductases
Steroids
Genes
Complementary DNA
Androgens
Organism Cloning
Disorders of Sex Development
Sex Differentiation
Inborn Genetic Diseases
Dihydrotestosterone
Gene Deletion
Isoenzymes
Embryonic Development
Testosterone
Hormones
Pharmacology
Phenotype
Polymerase Chain Reaction

ASJC Scopus subject areas

  • General

Cite this

Andersson, S., Berman, D. M., Jenkins, E. P., & Russell, D. W. (1991). Deletion of steroid 5α-reductase 2 gene in male pseudohermaphroditism. Nature, 354(6349), 159-161.

Deletion of steroid 5α-reductase 2 gene in male pseudohermaphroditism. / Andersson, Stefan; Berman, David M.; Jenkins, Elizabeth P.; Russell, David W.

In: Nature, Vol. 354, No. 6349, 14.11.1991, p. 159-161.

Research output: Contribution to journalArticle

Andersson, S, Berman, DM, Jenkins, EP & Russell, DW 1991, 'Deletion of steroid 5α-reductase 2 gene in male pseudohermaphroditism', Nature, vol. 354, no. 6349, pp. 159-161.
Andersson S, Berman DM, Jenkins EP, Russell DW. Deletion of steroid 5α-reductase 2 gene in male pseudohermaphroditism. Nature. 1991 Nov 14;354(6349):159-161.
Andersson, Stefan ; Berman, David M. ; Jenkins, Elizabeth P. ; Russell, David W. / Deletion of steroid 5α-reductase 2 gene in male pseudohermaphroditism. In: Nature. 1991 ; Vol. 354, No. 6349. pp. 159-161.
@article{3bc3ff8305384c4d99cff59cf43efe11,
title = "Deletion of steroid 5α-reductase 2 gene in male pseudohermaphroditism",
abstract = "THE conversion of testosterone into dihydrotestosterone by steroid 5α-reductase is a key reaction in androgen action, and is essential both for the formation of the male phenotype during embryogenesis and for androgen-mediated growth of tissues such as the prostate1,2. Single gene defects that impair this conversion lead to pseudohermaphroditism in which 46 X, Y males have male internal urogenital tracts, but female external genitalia3. We have described the isolation of a human 5α-reductase complementary DNA from prostate4. Subsequent cloning and genetic studies showed that this gene (designated 5α-reductase 1) was normal in patients with 5α-reductase deficiency26. We report here the isolation of a second 5α-reductase cDNA by expression cloning and the polymerase chain reaction. The biochemical and pharmacological properties of this cDNA-encoded enzyme (designated 5α-reductase 2) are consistent with it being the major isozyme in genital tissue. A deletion in this gene is present in two related individuals with male pseudohermaphroditism caused by 5α-reductase deficiency. These results verify the existence of at least two 5α-reductases in man and provide insight into a fundamental hormone-mediated event in male sexual differentiation.",
author = "Stefan Andersson and Berman, {David M.} and Jenkins, {Elizabeth P.} and Russell, {David W.}",
year = "1991",
month = "11",
day = "14",
language = "English (US)",
volume = "354",
pages = "159--161",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6349",

}

TY - JOUR

T1 - Deletion of steroid 5α-reductase 2 gene in male pseudohermaphroditism

AU - Andersson, Stefan

AU - Berman, David M.

AU - Jenkins, Elizabeth P.

AU - Russell, David W.

PY - 1991/11/14

Y1 - 1991/11/14

N2 - THE conversion of testosterone into dihydrotestosterone by steroid 5α-reductase is a key reaction in androgen action, and is essential both for the formation of the male phenotype during embryogenesis and for androgen-mediated growth of tissues such as the prostate1,2. Single gene defects that impair this conversion lead to pseudohermaphroditism in which 46 X, Y males have male internal urogenital tracts, but female external genitalia3. We have described the isolation of a human 5α-reductase complementary DNA from prostate4. Subsequent cloning and genetic studies showed that this gene (designated 5α-reductase 1) was normal in patients with 5α-reductase deficiency26. We report here the isolation of a second 5α-reductase cDNA by expression cloning and the polymerase chain reaction. The biochemical and pharmacological properties of this cDNA-encoded enzyme (designated 5α-reductase 2) are consistent with it being the major isozyme in genital tissue. A deletion in this gene is present in two related individuals with male pseudohermaphroditism caused by 5α-reductase deficiency. These results verify the existence of at least two 5α-reductases in man and provide insight into a fundamental hormone-mediated event in male sexual differentiation.

AB - THE conversion of testosterone into dihydrotestosterone by steroid 5α-reductase is a key reaction in androgen action, and is essential both for the formation of the male phenotype during embryogenesis and for androgen-mediated growth of tissues such as the prostate1,2. Single gene defects that impair this conversion lead to pseudohermaphroditism in which 46 X, Y males have male internal urogenital tracts, but female external genitalia3. We have described the isolation of a human 5α-reductase complementary DNA from prostate4. Subsequent cloning and genetic studies showed that this gene (designated 5α-reductase 1) was normal in patients with 5α-reductase deficiency26. We report here the isolation of a second 5α-reductase cDNA by expression cloning and the polymerase chain reaction. The biochemical and pharmacological properties of this cDNA-encoded enzyme (designated 5α-reductase 2) are consistent with it being the major isozyme in genital tissue. A deletion in this gene is present in two related individuals with male pseudohermaphroditism caused by 5α-reductase deficiency. These results verify the existence of at least two 5α-reductases in man and provide insight into a fundamental hormone-mediated event in male sexual differentiation.

UR - http://www.scopus.com/inward/record.url?scp=0026055914&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026055914&partnerID=8YFLogxK

M3 - Article

VL - 354

SP - 159

EP - 161

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6349

ER -