Hepatic CYP1A in brown bullhead catalyzes the binding of 2-aminoanthracene to DNA in vivo and in vitro
Identifieur interne : 000797 ( Main/Exploration ); précédent : 000796; suivant : 000798Hepatic CYP1A in brown bullhead catalyzes the binding of 2-aminoanthracene to DNA in vivo and in vitro
Auteurs : David E. Watson [États-Unis] ; Richard T. Di Giulio [États-Unis]Source :
- Aquatic Toxicology [ 0166-445X ] ; 1996.
Abstract
Brown bullhead were injected i.p. with vehicle or β-naphthoflavone (βNF), followed 2 days later with vehicle or ring-tritiated 2-aminoanthracene ([3H]-AA), such that four treatments were obtained: (1) vehicle only; (2) βNF only; [3H]-AA only; βNF/[3H]-AA. Ethoxyresorufin-O-deethylase (EROD) activity in βNF-treated fish was 15-fold greater than in vehicletreated fish at day 0 and was also significantly greater than vehicle-treated fish at day 1. Western blot analysis revealed marked induction of hepatic CYP1A in fish treated with βNF and minor induction in fish treated with [3H]-AA compared with vehicle-treated fish. Hepatic DNA adducts, as measured by tritium-associated DNA, ranged from 1.47 to 2.57 pmol mg−1 DNA in fish injected only with [3H]-AA, but ranged from 5.70 to 7.82 pmol mg−1 DNA in fish injected with βNF prior to injection with [3H]-AA. Thus, βNF pretreatment significantly increased binding of [3H]-AA to hepatic DNA in vivo at all time points (P < 0.05). In vitro, hepatic microsomes from βNF-treated bullhead catalyzed the binding of [3H]-AA to DNA at a low but measurable level which was significantly inhibited (P < 0.05) by alpha-naphtho-flavone and tetrachlorobiphenyl. Collectively, these data indicate that CYP1A activates AA to a DNA-binding metabolite(s), and that CYP1A induction in bullhead results in greater DNA adduct formation in AA-exposed fish. Comparisons were made between this study and a parallel study using the same experimental design but conducted with a related Ictalurid catfish, the channel catfish.
Url:
DOI: 10.1016/S0166-445X(96)00800-4
Affiliations:
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Di Giulio</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:A3425090DA40EF9F1E252027477C0E6AC994218A</idno><date when="1997" year="1997">1997</date><idno type="doi">10.1016/S0166-445X(96)00800-4</idno><idno type="url">https://api.istex.fr/document/A3425090DA40EF9F1E252027477C0E6AC994218A/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">000386</idno><idno type="wicri:Area/Istex/Curation">000324</idno><idno type="wicri:Area/Istex/Checkpoint">000759</idno><idno type="wicri:doubleKey">0166-445X:1997:Watson D:hepatic:cyp:a</idno><idno type="wicri:Area/Main/Merge">000830</idno><idno type="wicri:Area/Main/Curation">000822</idno><idno type="wicri:Area/Main/Exploration">000797</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Hepatic CYP1A in brown bullhead catalyzes the binding of 2-aminoanthracene to DNA in vivo and in vitro</title><author><name sortKey="Watson, David E" sort="Watson, David E" uniqKey="Watson D" first="David E." last="Watson">David E. Watson</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Ecotoxicology Laboratory, School of the Environment, Duke University, Durham, NC 27708-0328</wicri:regionArea><placeName><region type="state">Caroline du Nord</region></placeName></affiliation><affiliation><wicri:noCountry code="no comma">E-mail: watson2@niehs.nih.gov</wicri:noCountry></affiliation></author><author><name sortKey="Di Giulio, Richard T" sort="Di Giulio, Richard T" uniqKey="Di Giulio R" first="Richard T." last="Di Giulio">Richard T. Di Giulio</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Ecotoxicology Laboratory, School of the Environment, Duke University, Durham, NC 27708-0328</wicri:regionArea><placeName><region type="state">Caroline du Nord</region></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j">Aquatic Toxicology</title><title level="j" type="abbrev">AQTOX</title><idno type="ISSN">0166-445X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1996">1996</date><biblScope unit="volume">37</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="21">21</biblScope><biblScope unit="page" to="36">36</biblScope></imprint><idno type="ISSN">0166-445X</idno></series><idno type="istex">A3425090DA40EF9F1E252027477C0E6AC994218A</idno><idno type="DOI">10.1016/S0166-445X(96)00800-4</idno><idno type="PII">S0166-445X(96)00800-4</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0166-445X</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Brown bullhead were injected i.p. with vehicle or β-naphthoflavone (βNF), followed 2 days later with vehicle or ring-tritiated 2-aminoanthracene ([3H]-AA), such that four treatments were obtained: (1) vehicle only; (2) βNF only; [3H]-AA only; βNF/[3H]-AA. Ethoxyresorufin-O-deethylase (EROD) activity in βNF-treated fish was 15-fold greater than in vehicletreated fish at day 0 and was also significantly greater than vehicle-treated fish at day 1. Western blot analysis revealed marked induction of hepatic CYP1A in fish treated with βNF and minor induction in fish treated with [3H]-AA compared with vehicle-treated fish. Hepatic DNA adducts, as measured by tritium-associated DNA, ranged from 1.47 to 2.57 pmol mg−1 DNA in fish injected only with [3H]-AA, but ranged from 5.70 to 7.82 pmol mg−1 DNA in fish injected with βNF prior to injection with [3H]-AA. Thus, βNF pretreatment significantly increased binding of [3H]-AA to hepatic DNA in vivo at all time points (P < 0.05). In vitro, hepatic microsomes from βNF-treated bullhead catalyzed the binding of [3H]-AA to DNA at a low but measurable level which was significantly inhibited (P < 0.05) by alpha-naphtho-flavone and tetrachlorobiphenyl. Collectively, these data indicate that CYP1A activates AA to a DNA-binding metabolite(s), and that CYP1A induction in bullhead results in greater DNA adduct formation in AA-exposed fish. Comparisons were made between this study and a parallel study using the same experimental design but conducted with a related Ictalurid catfish, the channel catfish.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Caroline du Nord</li></region></list><tree><country name="États-Unis"><region name="Caroline du Nord"><name sortKey="Watson, David E" sort="Watson, David E" uniqKey="Watson D" first="David E." last="Watson">David E. Watson</name></region><name sortKey="Di Giulio, Richard T" sort="Di Giulio, Richard T" uniqKey="Di Giulio R" first="Richard T." last="Di Giulio">Richard T. Di Giulio</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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