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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


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

DC Field Value Language Seo, Young Kyo - Mirkheshti, Nooshin - Song, Chung S. - Kim, Soyoung - Dodds, Sherry - Ahn, Soon C. - Christy, Barbara - Mendez-Meza, Rosario - Ittmann, Michael M. - Abboud-Werner, Sherry - Chatterjee, Bandana - 2014-11-04T00:06:41Z - 2014-11-04T00:06:41Z - 2014-11-03 - 2013-06 -
dc.identifier.citation MOLECULAR ENDOCRINOLOGY, v.27, no.6, pp.925 - 939 -
dc.identifier.issn 0888-8809 -
dc.identifier.uri -
dc.description.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. -
dc.description.statementofresponsibility open -
dc.language ENG -
dc.publisher ENDOCRINE SOC -
dc.subject ACTIVITY IN-VITRO -
dc.subject 1,25-DIHYDROXYVITAMIN D-3 -
dc.subject BINDING PROTEIN -
dc.subject CELLS -
dc.subject ACID -
dc.subject PROMOTER -
dc.subject ENZYMES -
dc.title SULT2B1b Sulfotransferase: Induction by Vitamin D Receptor and Reduced Expression in Prostate Cancer -
dc.type ARTICLE -
dc.identifier.scopusid 2-s2.0-84877890627 -
dc.identifier.wosid 000319205300006 -
dc.type.rims ART -
dc.description.wostc 1 *
dc.description.scopustc 2 * 2015-05-06 * 2014-11-03 *
dc.identifier.doi 10.1210/me.2012-1369 -
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