Inhibitory Effects of Nitrative Stress on the Sulfation of 17.BETA.-Estradiol and 4-Methoxyestradiol by Human MCF 10A Mammary Epithelial Cells
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- Hui Ying
- College of Pharmacy, The University of Toledo Department of Obstetric and Gynecology, Beijing Hospital
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- Yasuda Tomoko
- College of Pharmacy, The University of Toledo
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- Yasuda Shin
- College of Pharmacy, The University of Toledo
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- Liu Ming-Yih
- National Synchrotron Radiation Research Center, Taiwan
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- Sakakibara Yoichi
- Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, University of Miyazaki
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- Suiko Masahito
- Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, University of Miyazaki
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- Wall Katherine Ann
- College of Pharmacy, The University of Toledo
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- Liu Ming-Cheh
- College of Pharmacy, The University of Toledo
Bibliographic Information
- Other Title
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- Inhibitory effects of nitrative stress on the sulfation of 17β-estradiol and 4-methoxyestradiol by human MCF 10A mammary epithelial cells
- Inhibitory effects of nitrative stress on the sulfation of 17 v estradiol and 4 methoxyestradiol by human MCF 10A mammary epithelial cells
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Abstract
Prolonged exposure to high level of estrogen is a known risk factor for breast carcinogenesis. It has been suggested recently that nitrative stress may be an etiologic factor for breast carcinogenesis. Since sulfation plays a major role in the homeostasis of estrogens and their metabolites, we attempted in the present study to find out whether nitrative stress may affect the homeostasis of estrogens through sulfation. Metabolic labeling experiments revealed that the amount of sulfated 17β-estradiol or 4-methoxyestradiol decreased dramatically in MCF-10A mammary epithelial cells incubated in the presence of 3-morpholinosydnonimine (SIN-1) or diethylenetriamine NONOate (DETA NONOate), two nitric oxide donors commonly used to simulate nitrative stress conditions. In searching for the mechanism underlying the decrease of the sulfation of 17β-estradiol and 4-methoxyestradiol, we demonstrated in an in vitro nitration experiment, that the human cytosolic sulfotransferase isoform 1E1 (SULT1E1), a major estrogen-sulfating enzyme, lost its estrogen-sulfating activity proportionately to the degree of nitration on tyrosine residues. Moreover, cell lysates prepared from MCF-10A cells treated with SIN-1 or DETA NONOate also showed much lower 4-methoxyestradiol-sulfating activities, compared with those determined with cell lysate prepared from control MCF-10A cells.
Journal
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- Biological and Pharmaceutical Bulletin
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Biological and Pharmaceutical Bulletin 33 (9), 1633-1637, 2010
The Pharmaceutical Society of Japan
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Details 詳細情報について
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- CRID
- 1390001204626736256
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- NII Article ID
- 130000322369
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- NII Book ID
- AA10885497
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- ISSN
- 13475215
- 09186158
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- NDL BIB ID
- 10797185
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed