title: Presence and inducibility by beta-naphthoflavone of CYP1A1, CYP1B1 and phase II enzymes in Trematomus bernacchii, an Antarctic fish.
abstract: This study investigated some aspects of xenobiotic metabolism in the Nototheniidae Trematomus bernacchii, a key sentinel species for monitoring Antarctic ecosystems. After laboratory exposure to beta-naphthoflavone (betaNF), basal levels and time-course induction of CYP1A, CYP1B and CYP3A were measured as enzymatic activities, immunoreactive protein content and mRNA expression in liver, gills, intestine and heart. Additional analyses in the liver included enzymatic activities of testosterone hydroxylase, (omega)- and (omega-1)-lauric acid hydroxylase and some phase II enzymes related to the AhR battery genes, DT-diaphorase, glutathione S-transferases and UDP-glucuronyl transferases. Responsiveness of hepatic CYP1A1 after exposure to betaNF demonstrated an higher sensitivity of MEROD than EROD activity and long lasting expression of mRNA still induced after 20 days from the treatment. Testosterone metabolism, oxidation of lauric acid and activities of phase II enzymes were not affected by betaNF indicating that their modulation is not mediated by Ah receptor. Induction of CYP1A was more limited in gills and absent in intestine and heart. The first nucleotide sequence for CYP1B1 in an Antarctic fish has been obtained, revealing a homology of 89% and 72% respectively to CYP1B1 of plaice and CYP1B2 of carp. Constitutive expression of CYP1B1 was restricted to gills where it was also induced by betaNF. Obtained results represent an additional contribution to the ecotoxicological characterization of T. bernacchii and further support the use of biomarkers for early detection of chemical pollution in Antarctica.
authors.affiliation: Dipartimento di Patologia Animale Profilassi ed Igiene degli Alimenti, Università di Pisa, Viale delle Piagge 2, 56124 Pisa, Italy.
authors.forename: Domenica
authors.initials: D
authors.lastname: Di Bello
authors.forename: Emilia
authors.initials: E
authors.lastname: Vaccaro
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Longo
authors.forename: Francesco
authors.initials: F
authors.lastname: Regoli
authors.forename: Marco
authors.initials: M
authors.lastname: Nigro
authors.forename: Maura
authors.initials: M
authors.lastname: Benedetti
authors.forename: Pier Giovanni
authors.initials: PG
authors.lastname: Gervasi
authors.forename: Carlo
authors.initials: C
authors.lastname: Pretti
mesh_terms: D000818:Animals; D000864:Antarctic Regions; D001483:Base Sequence; D042926:Cytochrome P-450 CYP4A / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000096:biosynthesis* / Q000235:genetics; D004784:Environmental Monitoring / Q000379:methods*; D004790:Enzyme Induction / Q000187:drug effects; D005260:Female; D014453:Glucuronosyltransferase / Q000378:metabolism; D005982:Glutathione Transferase / Q000378:metabolism; D007527:Isoenzymes; D008099:Liver / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism; D008297:Male; D008969:Molecular Sequence Data; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000378:metabolism; D010473:Perciformes / Q000378:metabolism*; D012333:RNA, Messenger / Q000096:biosynthesis / Q000235:genetics; D020133:Reverse Transcriptase Polymerase Chain Reaction; D016415:Sequence Alignment; D019324:beta-Naphthoflavone / Q000633:toxicity*
chemical_list: D007527:Isoenzymes; D012333:RNA, Messenger; D019324:beta-Naphthoflavone; D003577:Cytochrome P-450 Enzyme System; D042926:Cytochrome P-450 CYP4A; D016660:NAD(P)H Dehydrogenase (Quinone); D014453:Glucuronosyltransferase; D005982:Glutathione Transferase