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Seo, Young Kyo
School of Life Sciences
Research Interests
  • How the fundamental processes of gene regulation are used in the control and management of metabolic homeostasis

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SULT2B1b Sulfotransferase: Induction by Vitamin D Receptor and Reduced Expression in Prostate Cancer

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Title
SULT2B1b Sulfotransferase: Induction by Vitamin D Receptor and Reduced Expression in Prostate Cancer
Author
Seo, Young KyoMirkheshti, NooshinSong, Chung S.Kim, SoyoungDodds, SherryAhn, Soon C.Christy, BarbaraMendez-Meza, RosarioIttmann, Michael M.Abboud-Werner, SherryChatterjee, Bandana
Keywords
HUMAN HYDROXYSTEROID SULFOTRANSFERASE;  CHOLESTEROL SULFOTRANSFERASE;  ACTIVITY IN-VITRO;  1,25-DIHYDROXYVITAMIN D-3;  ANDROGEN RECEPTOR;  BINDING PROTEIN;  CELLS;  ACID;  PROMOTER;  ENZYMES
Issue Date
2013-06
Publisher
ENDOCRINE SOC
Citation
MOLECULAR ENDOCRINOLOGY, v.27, no.6, pp.925 - 939
Abstract
An elevated tumor tissue androgen level, which reactivates androgen receptor in recurrent prostate cancer, arises from the intratumor synthesis of 5 alpha-dihydrotestosterone through use of the precursor steroid dehydroepiandrosterone (DHEA) and is fueled by the steroidogenic enzymes 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD1), aldoketoreductase (AKR1C3), and steroid 5-alpha reductase, type 1 (SRD5A1) present in cancer tissue. Sulfotransferase 2B1b (SULT2B1b) (in short, SULT2B) is a prostate-expressed hydroxysteroid SULT that converts cholesterol, oxysterols, and DHEA to 3 beta-sulfates. DHEA metabolism involving sulfonation by SULT2B can potentially interfere with intraprostate androgen synthesis due to reduction of free DHEA pool and, thus, conversion of DHEA to androstenedione. Here we report that in prostatectomy specimens from treatment-naive patients, SULT2B expression is markedly reduced in malignant tissue (P < .001, Mann-Whitney U test) compared with robust expression in adjacent nonmalignant glands. SULT2B was detected in formalin-fixed specimens by immunohistochemistry on individual sections and tissue array. Immunoblotting of protein lysates of frozen cancer and matched benign tissue confirmed immunohistochemistry results. An in-house-developed rabbit polyclonal antibody against full-length human SULT2B was validated for specificity and used in the analyses. Ligand-activated vitamin D receptor induced the SULT2B1 promoter in vivo in mouse prostate and increased SULT2B mRNA and protein levels in vitro in prostate cancer cells. A vitamin D receptor/retinoid X receptor-alpha-bound DNA element (with a DR7 motif) mediated induction of the transfected SULT2B1 promoter in calcitriol-treated cells. SULT2B knockdown caused an increased proliferation rate of prostate cancer cells upon stimulation by DHEA. These results suggest that the tumor tissue SULT2B level may partly control prostate cancer growth, and its induction in a therapeutic setting may inhibit disease progression.
URI
https://scholarworks.unist.ac.kr/handle/201301/8191
DOI
10.1210/me.2012-1369
ISSN
0888-8809
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