Genetic and pharmacological evidence for more than one human steroid 5α-reductase

Elizabeth P. Jenkins, Stefan Andersson, Julianne Imperato-McGinley, Jean D. Wilson, David W. Russell

Research output: Contribution to journalArticle

351 Scopus citations

Abstract

The enzyme steroid 5α-reductase catalyzes the conversion of testosterone into the more potent androgen, dihydrotestosterone, and impairment of this reaction causes a form of male pseudohermaphroditism in which genetic males differentiate predominantly as phenotypic females. We previously isolated cDNA clones that encode a human steroid 5α-reductase enzyme. Here, we report molecular and genetic studies demonstrating that the gene encoding this cDNA is normal in subjects with the genetic disease steroid 5α-reductase deficiency. We further show that in contrast to the major steroid 5α-reductase in the prostate and cultured skin fibroblasts, the cDNA-encoded enzyme exhibits a neutral to basic pH optima and is much less sensitive to inhibition by the 4-aza steroid, finasteride (MK-906). The results provide genetic, biochemical, and pharmacological support for the existence of at least two steroid 5α-reductase isozymes in man.

Original languageEnglish (US)
Pages (from-to)293-300
Number of pages8
JournalJournal of Clinical Investigation
Volume89
Issue number1
DOIs
StatePublished - Jan 1 1992

Keywords

  • 4-Azasteroid inhibitors
  • Androgens
  • Dihydrotestosterone
  • Isozymes
  • Pseudohermaphroditism

ASJC Scopus subject areas

  • Medicine(all)

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