17β-hydroxysteroid dehydrogenase type XI localizes to human steroidogenic cells

Zhong-Lin Chai, Phillip Brereton, Takashi Suzuki, Hironobu Sasano, Varuni Obeyesekere, Genevieve Escher, Richard Saffery, Peter Fuller, Carla Enriquez, Zygmunt Krozowski

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49 Citations (Scopus)

Abstract

We searched expressed sequence tag databases with conserved domains of the short-chain alcohol dehydrogenase superfamily and identified another isoform of 17β-hydroxysteroid dehydrogenase, 17βHSDXI. This enzyme converts 5α-androstane-3α, 17β-diol to androsterone. The substrate has been implicated in supporting gestation and modulating γ-aminobutyric acid receptor activity, 17βHSDXI is colinear with human retinal short-chain dehydrogenase/reductase retSDR2, a protein with no known biological activity (accession no. AAF06939). Of the proteins with known function, 17βHSDXI is most closely related to the retinol-metabolizing enzyme retSDR1, with which it has 30% identity. There is a polymorphic stretch of 15 adenosines in the 5′ untranslated region of the cDNA sequence and a silent polymorphism at C719T. A 17βHSDXI construct with a stretch of 20 adenosines was found to produce significantly more enzyme activity than constructs containing 15 or less adenosines (43% vs. 26%, P

Original languageEnglish
Pages (from-to)2084-2091
Number of pages8
JournalEndocrinology
Volume144
Issue number5
DOIs
Publication statusPublished - 1 May 2003
Externally publishedYes

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