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 | |
| Publication status | Published - 1 May 2003 |
| Externally published | Yes |
Cite this
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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
TY - JOUR
T1 - 17β-hydroxysteroid dehydrogenase type XI localizes to human steroidogenic cells
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
Y1 - 2003/5/1
N2 - 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
AB - 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
UR - http://www.scopus.com/inward/record.url?scp=0038070588&partnerID=8YFLogxK
U2 - 10.1210/en.2002-221030
DO - 10.1210/en.2002-221030
M3 - Article
VL - 144
SP - 2084
EP - 2091
JO - Endocrinology
JF - Endocrinology
SN - 0013-7227
IS - 5
ER -