HORMONE-RELATED TUMORS: NOVEL APPROACHES TO PREVENTION AND TREATMENT
Copyright © 2002 by the New York Academy of Sciences
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Annals of the New York Academy of Sciences 963:221-228 (2002)
© 2002 New York Academy of Sciences
Human Type 1 Estrogen Sulfotransferase
Catecholestrogen Metabolism and Potential Involvement in Cancer Promotion
FRÉDÉRIC FAUCHER,
LUCILLE LACOSTE AND
VAN LUU-THE
Oncology and Molecular Endocrinology Research Center, Laval University Medical Center (CHUL) and Laval University, Quebec G1V 4G2, Canada
Address for correspondence: Dr. Van Luu-The, Oncology and Molecular Endocrinology Research Center, Laval University Medical Center (CHUL), 2705 Laurier Boulevard, Quebec, (Quebec) G1V 4G2, Canada. Voice: 418-654-2296; fax: 418-654-2761.
Ann. N.Y. Acad. Sci. 963: 221-228 (2002).
Using purified human type 1 estrogen sulfotransferase (hEST1), we show that the best substrate for this enzyme is 2-hydroxy-catecholestrogen. The enzyme also catalyzes the transformation of 4-hydroxy-estrogens and 16-hydroxy-estrogens, but with a lower affinity. We also present evidence to indicate that estrogen sulfotransferase may play a role in processes other than the detoxification and elimination of steroids. Indeed, hEST1 may also be involved in the production of stable precursors for local steroid biosynthesis or in the activation of promutagenic estrogen metabolites into carcinogens.
Key Words: steroidogenesis • estrogen sulfotransferase • expression • transfection • estrogens • catecholestrogens
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