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

doi:10.1210/en.2002-221030

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

Research output: Contribution to journal › Article › Research › peer-review

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 language	English
Pages (from-to)	2084-2091
Number of pages	8
Journal	Endocrinology
Volume	144
Issue number	5
DOIs	https://doi.org/10.1210/en.2002-221030
Publication status	Published - 1 May 2003
Externally published	Yes

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Cite this

@article{ce4de9cdf3e743b3b19606fb0dc1eced,

title = "17β-hydroxysteroid dehydrogenase type XI localizes to human steroidogenic cells",

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 ",

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

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journal = "Endocrinology",

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17β-hydroxysteroid dehydrogenase type XI localizes to human steroidogenic cells. / Chai, Zhong-Lin; Brereton, Phillip; Suzuki, Takashi; Sasano, Hironobu; Obeyesekere, Varuni; Escher, Genevieve; Saffery, Richard; Fuller, Peter; Enriquez, Carla; Krozowski, Zygmunt.

In: Endocrinology, Vol. 144, No. 5, 01.05.2003, p. 2084-2091.

Research output: Contribution to journal › Article › Research › peer-review

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AU - Chai, Zhong-Lin

AU - Brereton, Phillip

AU - Suzuki, Takashi

AU - Sasano, Hironobu

AU - Obeyesekere, Varuni

AU - Escher, Genevieve

AU - Saffery, Richard

AU - Fuller, Peter

AU - Enriquez, Carla

AU - Krozowski, Zygmunt

PY - 2003/5/1

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