Effects of phenolic environmental estrogens on the sulfotransferase activity of the mouse intestine and a human colon carcinoma cell line, Caco-2

Hiroomi Tamura, Michio Matsui

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

In order to explore the possible role of sulfation in the inactivation of environmental estrogens at gastrointestinal sites and their subsequent removal, we investigated the effects of phenolic environmental estrogens on sulfotransferase (ST) activity. The mouse intestine and a human colon carcinoma cell line, Caco-2, were studied. ST enzymes were found to have a high affinity for diethylstilbestrol (DES) and bisphenol A (BPA), whereas phenol ST (PST) activity was strongly inhibited by nonylphenol and genistein in both mice and humans. Kinetic analysis showed that this inhibition was competitive. These observations suggest that nonylphenol and genistein compounds might inhibit PST activity in the human intestine and that they might escape detoxification by sulfation.

Original languageEnglish
Pages (from-to)468-472
Number of pages5
JournalJournal of Health Science
Volume47
Issue number5
DOIs
Publication statusPublished - 2001

Fingerprint

Sulfotransferases
Genistein
Intestines
Estrogens
Colon
Arylsulfotransferase
Cells
Carcinoma
Cell Line
Detoxification
Diethylstilbestrol
Phenol
Human Activities
Kinetics
Enzymes
estrone sulfotransferase
nonylphenol
bisphenol A

Keywords

  • Bisphenol A
  • Caco-2
  • Diethylstilbestrol
  • Environmental estrogen
  • Sulfotransferase

ASJC Scopus subject areas

  • Toxicology
  • Health, Toxicology and Mutagenesis

Cite this

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abstract = "In order to explore the possible role of sulfation in the inactivation of environmental estrogens at gastrointestinal sites and their subsequent removal, we investigated the effects of phenolic environmental estrogens on sulfotransferase (ST) activity. The mouse intestine and a human colon carcinoma cell line, Caco-2, were studied. ST enzymes were found to have a high affinity for diethylstilbestrol (DES) and bisphenol A (BPA), whereas phenol ST (PST) activity was strongly inhibited by nonylphenol and genistein in both mice and humans. Kinetic analysis showed that this inhibition was competitive. These observations suggest that nonylphenol and genistein compounds might inhibit PST activity in the human intestine and that they might escape detoxification by sulfation.",
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AB - In order to explore the possible role of sulfation in the inactivation of environmental estrogens at gastrointestinal sites and their subsequent removal, we investigated the effects of phenolic environmental estrogens on sulfotransferase (ST) activity. The mouse intestine and a human colon carcinoma cell line, Caco-2, were studied. ST enzymes were found to have a high affinity for diethylstilbestrol (DES) and bisphenol A (BPA), whereas phenol ST (PST) activity was strongly inhibited by nonylphenol and genistein in both mice and humans. Kinetic analysis showed that this inhibition was competitive. These observations suggest that nonylphenol and genistein compounds might inhibit PST activity in the human intestine and that they might escape detoxification by sulfation.

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