Differential interaction of natural and synthetic estrogens with extracellular binding proteins in a yeast estrogen screen

被引:50
作者
Arnold, SF
Collins, BM
Robinson, MK
Guillette, LJ
McLachlan, JA
机构
[1] TULANE UNIV,SCH PUBL HLTH & TROP MED,DEPT ENVIRONM HLTH SCI,NEW ORLEANS,LA
[2] TULANE UNIV,MED CTR,MOL & CELLULAR BIOL PROGRAM,NEW ORLEANS,LA
[3] TULANE UNIV,MED CTR,DEPT PHARMACOL,NEW ORLEANS,LA
[4] UNIV ROCHESTER,MED CTR,DEPT BIOCHEM,ROCHESTER,NY 14642
[5] UNIV FLORIDA,DEPT ZOOL,GAINESVILLE,FL 32611
关键词
estrogen; phytoestrogen; environmental estrogen; yeast estrogen screen; sex hormone-binding globulin; alpha-fetoprotein;
D O I
10.1016/S0039-128X(96)00183-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We have used the yeast estrogen screen (YES) consisting of the human estrogen receptor and a reporter containing two estrogen response elements linked to the lacZ gene to evaluate the interaction between ovarian, phyto-, and synthetic estrogens with extracellular binding proteins. YES was incubated,vith charcoal-stripped human serum, human sex hormone-binding globulin, or human alpha-feroprotein in the presence of concentrations of various estrogens that induced a 100% estrogenic response, as measured by beta-galactosidase activity. The activity of estradiol and coumestrol, a phyroestrogen, was reduced 75% with physiological levels of serum, sex hormone-binding globulin, or alpha-fetoprotein. The beta-galactosidase activity of genistein, another phytoestrogen, also decreased with extracellular proteins but to a lower extent than estradiol. In contrast, the activity of the synthetic estrogens diethylstilbestrol, kepone, and p,p'-DDD was only minimally reduced with extracellular proteins. These results indicate a potential fundamental difference in the interaction of estrogens from diverse sources with extracellular binding proteins. This suggests that the capacity for various estrogens to induce estrogen-associated responses is in part regulated by their affinity for extracellular binding proteins. (C) 1996 by Elsevier Science Inc.
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页码:642 / 646
页数:5
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