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Apoptosis inducing anthraquinone rhein and emodin differentially suppress human dehydroepiandrosterone sulfotransferase (hSULT2A1) and phenol sulfotransferases (hSULT1A1) in Hep-G2 and Caco-2 cells

Article type: Research Article

Authors: Maiti, Smarajita; c; 1; * | Dutta, Sangita Maitia; b | Chen, Guangpinga

Affiliations: [a] Department of Physiological Sciences, Center for Veterinary Health Sciences, Oklahoma State University, Stillwater, OK, USA | [b] Department of Zoology, Vidyasagar University, WB, India | [c] Founder and Secretary, Agricure Biotech Research Society, Mahatabpur, Midnapore, WB, India

Correspondence: [*] Corresponding author: Dr. Smarajit Maiti, Department of Physiological Sciences, Center for Veterinary Health Sciences, Oklahoma State University, Stillwater, OK 74078, USA. E-mails: [email protected], [email protected] (Guangping Chen), [email protected] (Sangita Maiti Dutta).

Note: [1] Present address: Post Graduate Department of Biochemistry and Biotechnology, Oriental Institute of Science and Technology, Cell & Molecular Therapy, Lab, Vidyasagar University, Midnapore-721102, WB, India.

Keywords: Physiological role, rhein and emodin, sulfotransferase, suppression effect

DOI: 10.3233/MNM-140015

Journal: Mediterranean Journal of Nutrition and Metabolism, vol. 7, no. 3, pp. 145-153, 2014

Published: 01 August 2014
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Abstract

The anti-cancer and apoptosis-inducing drugs rhein (4, 5-dihydroxyanthraquinone-2-carboxylic acid) and emodin (3-methyl-1, 6, 8-trihydro-xyanthrax-quinone) are clinically very important. They modulate cell cycle via tumor suppressor gene, immuno-receptors and ligand activated nuclear receptors. Our recent observation suggests for the first time that 10 days of treatment of either drug with various concentrations (0.01 to 100 ¼M) differentially suppressed the sulfotransferases (SULTs) activities and protein expressions in human hepatocellular carcinoma (Hep G2) and intestinal carcinoma (Caco-2) cell lines. SULTs are phase II drug metabolizing enzymes which catalyze the sulfuryl group transfer to hydroxyl containing endobiotics and xenobiotics. In the present investigation, dehydroepiandrosterone SULT (hSULT1A1) was markedly suppressed by these drugs in human cells. This is the first time report which demonstrates that rhein and emodin may regulate human SULTs. Our finding has important physiological and clinical implications. It will help in the understanding of the SULTs regulations by clinically important drugs and xenobiotics. In future, these drugs may be used in a better defined manner, taking into account its SULTs suppression effects with possible physiological consequences.

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