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Molecular Pharmacology

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Research ArticleArticle

Transcriptional Regulation of Human Cytosolic Sulfotransferase 1C3 by Peroxisome Proliferator-Activated Receptor γ in LS180 Human Colorectal Adenocarcinoma Cells

Sarah Dubaisi, Hailin Fang, Thomas A. Kocarek and Melissa Runge-Morris
Molecular Pharmacology November 2016, 90 (5) 562-569; DOI: https://doi.org/10.1124/mol.116.106005
Sarah Dubaisi
Department of Pharmacology (S.D.) and Institute of Environmental Health Sciences (H.F., T.A.K, M.R.-M.), Wayne State University, Detroit, Michigan
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Hailin Fang
Department of Pharmacology (S.D.) and Institute of Environmental Health Sciences (H.F., T.A.K, M.R.-M.), Wayne State University, Detroit, Michigan
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Thomas A. Kocarek
Department of Pharmacology (S.D.) and Institute of Environmental Health Sciences (H.F., T.A.K, M.R.-M.), Wayne State University, Detroit, Michigan
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Melissa Runge-Morris
Department of Pharmacology (S.D.) and Institute of Environmental Health Sciences (H.F., T.A.K, M.R.-M.), Wayne State University, Detroit, Michigan
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Abstract

Cytosolic sulfotransferase 1C3 (SULT1C3) is the least characterized of the three human SULT1C subfamily members. Originally identified as an orphan SULT by computational analysis of the human genome, we recently reported that SULT1C3 is expressed in human intestine and LS180 colorectal adenocarcinoma cells and is upregulated by agonists of peroxisome proliferator-activated receptor (PPAR) α and γ. To determine the mechanism responsible for PPAR-mediated upregulation, we prepared reporter plasmids containing fragments of the SULT1C3 5′-flanking region. During initial attempts to amplify a 2.8-kb fragment from different sources of human genomic DNA, a 1.9-kb fragment was sometimes coamplified with the expected 2.8-kb fragment. Comparison of the 1.9-kb fragment sequence to the published SULT1C3 5′-flanking sequence revealed an 863-nt deletion (nt −146 to −1008 relative to the transcription start site). Transfection analysis in LS180 cells demonstrated that PPARα, δ, and γ agonist treatments induced luciferase expression from a reporter plasmid containing the 2.8-kb but not the 1.9-kb fragment. The PPAR agonists also activated a 1-kb reporter containing the 863-nt deletion region. Computational analysis identified three peroxisome proliferator response elements (PPREs) within the 863-nt region and serial deletions and site-directed mutations indicated that the most distal PPRE (at nt −769) was essential for obtaining PPAR-mediated transcriptional activation. Although agonists of all three PPARs could activate SULT1C3 transcription, RNA interference analysis indicated the predominance of PPARγ. These data demonstrate that the PPARγ regulatory network includes SULT1C3 and imply that this enzyme contributes to the control of such PPARγ-regulated intestinal processes as growth, differentiation, and metabolism.

Footnotes

    • Received July 5, 2016.
    • Accepted August 24, 2016.
  • This research was supported by the National Institutes of Health National Institute of Environmental Health Sciences [Grants R01 ES022606 and Center Grant P30ES020957].

  • dx.doi.org/10.1124/mol.116.106005.

  • Copyright © 2016 by The American Society for Pharmacology and Experimental Therapeutics
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Molecular Pharmacology: 90 (5)
Molecular Pharmacology
Vol. 90, Issue 5
1 Nov 2016
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Research ArticleArticle

Regulation of SULT1C3 by PPARγ

Sarah Dubaisi, Hailin Fang, Thomas A. Kocarek and Melissa Runge-Morris
Molecular Pharmacology November 1, 2016, 90 (5) 562-569; DOI: https://doi.org/10.1124/mol.116.106005

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Research ArticleArticle

Regulation of SULT1C3 by PPARγ

Sarah Dubaisi, Hailin Fang, Thomas A. Kocarek and Melissa Runge-Morris
Molecular Pharmacology November 1, 2016, 90 (5) 562-569; DOI: https://doi.org/10.1124/mol.116.106005
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