Use of Xenopus laevis as a model for investigating in vitro and in vivo endocrine disruption in amphibians
Identifieur interne : 001113 ( Istex/Corpus ); précédent : 001112; suivant : 001114Use of Xenopus laevis as a model for investigating in vitro and in vivo endocrine disruption in amphibians
Auteurs : Yue-Wern Huang ; Jason B. Matthews ; Kirsten C. Fertuck ; Tim R. ZacharewskiSource :
- Environmental Toxicology and Chemistry [ 0730-7268 ] ; 2005-08.
English descriptors
Abstract
The estrogenic activity of 17β‐estradiol (E2), α‐zearalenol (α‐ZEA), genistein (GEN), and 4‐t‐octylphenol (4‐t‐OP) was investigated using Xenopus laevis‐based assays. All test compounds competed with [3H]E2 for binding to a recombinant Xenopus estrogen receptor (xER) with the following relative affinities: E2 > α‐ZEA > 4‐t‐OP > GEN. The ability of these compounds to induce xER‐mediated reporter gene expression was then assessed in MCF‐7 human breast cancer cells cotransfected with a Gal4‐xERdef chimeric estrogen receptor and a Gal4‐regulated luciferase reporter gene. Luciferase activity was increased 30‐ to 50‐fold by 10 nM E2 relative to that in solvent control. Maximal reporter gene activity induced by 10 nM α‐ZEA was 54% of that induced by E2; however, the activity did not increase following doses of up to 10 μM. A dose of 1 μM 4‐t‐OP induced 23% of the maximal reporter gene activity induced by E2, whereas 10 μM GEN induced activity to the same level as E2. A dose‐dependent increase in vitellogenin (VTG) mRNA expression was observed in Xenopus treated intraperitoneally with E2 at 0.05 to 5 mg/kg/d for three consecutive days, with the maximal induction observed in the group receiving 1 mg/kg/d. The α‐ZEA, GEN, and 4‐t‐OP also significantly induced VTG mRNA expression, although at higher doses. These results demonstrate the utility of X laevis as an amphibian model to assess the estrogenic activity of endocrine disruptors.
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DOI: 10.1897/04-378R1.1
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<creator xml:id="au3" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Kirsten C.</givenNames>
<familyName>Fertuck</familyName>
</personName>
</creator>
<creator xml:id="au4" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Tim R.</givenNames>
<familyName>Zacharewski</familyName>
</personName>
</creator>
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<affiliationGroup><affiliation xml:id="af1" countryCode="US" type="organization"><unparsedAffiliation>Department of Biochemistry and Molecular Biology and National Food Safety and Toxicology Center, Michigan State University, East Lansing, Michigan 48824, USA</unparsedAffiliation>
</affiliation>
<affiliation xml:id="curr1" countryCode="US"><unparsedAffiliation>The current address of Y. Huang is Department of Biological Sciences, University of Missouri‐Rolla, 105 Schrenk Hall, 1870 Miner Circle, Rolla, MO 65409–1120, USA</unparsedAffiliation>
</affiliation>
</affiliationGroup>
<keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">Xenopus</keyword>
<keyword xml:id="kwd2">Estrogen receptor</keyword>
<keyword xml:id="kwd3">Competitive binding</keyword>
<keyword xml:id="kwd4">Gene expression</keyword>
<keyword xml:id="kwd5">Vitellogenin</keyword>
</keywordGroup>
<abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title>
<p>The estrogenic activity of 17β‐estradiol (E<sub>2</sub>
), α‐zearalenol (α‐ZEA), genistein (GEN), and 4‐<i>t</i>
‐octylphenol (4‐<i>t</i>
‐OP) was investigated using <i>Xenopus laevis</i>
‐based assays. All test compounds competed with [<sup>3</sup>
H]E<sub>2</sub>
for binding to a recombinant <i>Xenopus</i>
estrogen receptor (xER) with the following relative affinities: E<sub>2</sub>
> α‐ZEA > 4‐<i>t</i>
‐OP > GEN. The ability of these compounds to induce xER‐mediated reporter gene expression was then assessed in MCF‐7 human breast cancer cells cotransfected with a Gal4‐xERdef chimeric estrogen receptor and a Gal4‐regulated luciferase reporter gene. Luciferase activity was increased 30‐ to 50‐fold by 10 nM E<sub>2</sub>
relative to that in solvent control. Maximal reporter gene activity induced by 10 nM α‐ZEA was 54% of that induced by E<sub>2</sub>
; however, the activity did not increase following doses of up to 10 μM. A dose of 1 μM 4‐<i>t</i>
‐OP induced 23% of the maximal reporter gene activity induced by E<sub>2</sub>
, whereas 10 μM GEN induced activity to the same level as E<sub>2</sub>
. A dose‐dependent increase in vitellogenin (VTG) mRNA expression was observed in <i>Xenopus</i>
treated intraperitoneally with E<sub>2</sub>
at 0.05 to 5 mg/kg/d for three consecutive days, with the maximal induction observed in the group receiving 1 mg/kg/d. The α‐ZEA, GEN, and 4‐<i>t</i>
‐OP also significantly induced VTG mRNA expression, although at higher doses. These results demonstrate the utility of X <i>laevis</i>
as an amphibian model to assess the estrogenic activity of endocrine disruptors.</p>
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<mods version="3.6"><titleInfo lang="en"><title>Use of Xenopus laevis as a model for investigating in vitro and in vivo endocrine disruption in amphibians</title>
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<titleInfo type="abbreviated" lang="en"><title>Xenopus as a model for studying endocrine disruption</title>
</titleInfo>
<titleInfo type="alternative" contentType="CDATA" lang="en"><title>Use of Xenopus laevis as a model for investigating in vitro and in vivo endocrine disruption in amphibians</title>
</titleInfo>
<name type="personal"><namePart type="given">Yue‐wern</namePart>
<namePart type="family">Huang</namePart>
<affiliation>Department of Biochemistry and Molecular Biology and National Food Safety and Toxicology Center, Michigan State University, East Lansing, Michigan 48824, USA</affiliation>
<affiliation>Current Address: The current address of Y. Huang is Department of Biological Sciences, University of Missouri‐Rolla, 105 Schrenk Hall, 1870 Miner Circle, Rolla, MO 65409–1120, USA</affiliation>
<affiliation>Department of Biochemistry and Molecular Biology and National Food Safety and Toxicology Center, Michigan State University, East Lansing, Michigan 48824, USA</affiliation>
<role><roleTerm type="text">author</roleTerm>
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<name type="personal"><namePart type="given">Jason B.</namePart>
<namePart type="family">Matthews</namePart>
<affiliation>Department of Biochemistry and Molecular Biology and National Food Safety and Toxicology Center, Michigan State University, East Lansing, Michigan 48824, USA</affiliation>
<role><roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal"><namePart type="given">Kirsten C.</namePart>
<namePart type="family">Fertuck</namePart>
<affiliation>Department of Biochemistry and Molecular Biology and National Food Safety and Toxicology Center, Michigan State University, East Lansing, Michigan 48824, USA</affiliation>
<role><roleTerm type="text">author</roleTerm>
</role>
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<name type="personal"><namePart type="given">Tim R.</namePart>
<namePart type="family">Zacharewski</namePart>
<affiliation>Department of Biochemistry and Molecular Biology and National Food Safety and Toxicology Center, Michigan State University, East Lansing, Michigan 48824, USA</affiliation>
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<originInfo><publisher>Wiley Periodicals, Inc.</publisher>
<place><placeTerm type="text">Hoboken</placeTerm>
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<dateIssued encoding="w3cdtf">2005-08</dateIssued>
<dateCaptured encoding="w3cdtf">2004-07-30</dateCaptured>
<dateValid encoding="w3cdtf">2005-01-31</dateValid>
<copyrightDate encoding="w3cdtf">2005</copyrightDate>
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<languageTerm type="code" authority="iso639-2b">eng</languageTerm>
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<abstract lang="en">The estrogenic activity of 17β‐estradiol (E2), α‐zearalenol (α‐ZEA), genistein (GEN), and 4‐t‐octylphenol (4‐t‐OP) was investigated using Xenopus laevis‐based assays. All test compounds competed with [3H]E2 for binding to a recombinant Xenopus estrogen receptor (xER) with the following relative affinities: E2 > α‐ZEA > 4‐t‐OP > GEN. The ability of these compounds to induce xER‐mediated reporter gene expression was then assessed in MCF‐7 human breast cancer cells cotransfected with a Gal4‐xERdef chimeric estrogen receptor and a Gal4‐regulated luciferase reporter gene. Luciferase activity was increased 30‐ to 50‐fold by 10 nM E2 relative to that in solvent control. Maximal reporter gene activity induced by 10 nM α‐ZEA was 54% of that induced by E2; however, the activity did not increase following doses of up to 10 μM. A dose of 1 μM 4‐t‐OP induced 23% of the maximal reporter gene activity induced by E2, whereas 10 μM GEN induced activity to the same level as E2. A dose‐dependent increase in vitellogenin (VTG) mRNA expression was observed in Xenopus treated intraperitoneally with E2 at 0.05 to 5 mg/kg/d for three consecutive days, with the maximal induction observed in the group receiving 1 mg/kg/d. The α‐ZEA, GEN, and 4‐t‐OP also significantly induced VTG mRNA expression, although at higher doses. These results demonstrate the utility of X laevis as an amphibian model to assess the estrogenic activity of endocrine disruptors.</abstract>
<subject lang="en"><genre>keywords</genre>
<topic>Xenopus</topic>
<topic>Estrogen receptor</topic>
<topic>Competitive binding</topic>
<topic>Gene expression</topic>
<topic>Vitellogenin</topic>
</subject>
<relatedItem type="host"><titleInfo><title>Environmental Toxicology and Chemistry</title>
<subTitle>An International Journal</subTitle>
</titleInfo>
<titleInfo type="abbreviated"><title>Environmental Toxicology and Chemistry</title>
</titleInfo>
<genre type="journal">journal</genre>
<subject><genre>article-category</genre>
<topic>Environmental Toxicology</topic>
</subject>
<identifier type="ISSN">0730-7268</identifier>
<identifier type="eISSN">1552-8618</identifier>
<identifier type="DOI">10.1002/(ISSN)1552-8618</identifier>
<identifier type="PublisherID">ETC</identifier>
<part><date>2005</date>
<detail type="volume"><caption>vol.</caption>
<number>24</number>
</detail>
<detail type="issue"><caption>no.</caption>
<number>8</number>
</detail>
<extent unit="pages"><start>2002</start>
<end>2009</end>
<total>8</total>
</extent>
</part>
</relatedItem>
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<identifier type="DOI">10.1897/04-378R1.1</identifier>
<identifier type="ArticleID">ETC5620240822</identifier>
<accessCondition type="use and reproduction" contentType="copyright">Copyright © 2005 SETAC</accessCondition>
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<recordOrigin>Wiley Periodicals, Inc.</recordOrigin>
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