Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/20823
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dc.contributor.authorVasiliou, V.en
dc.contributor.authorTorronen, R.en
dc.contributor.authorMalamas, M.en
dc.contributor.authorMarselos, M.en
dc.date.accessioned2015-11-24T19:10:23Z-
dc.date.available2015-11-24T19:10:23Z-
dc.identifier.issn0742-8413-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/20823-
dc.rightsDefault Licence-
dc.subjectAldehyde Dehydrogenase/*biosynthesis/metabolismen
dc.subjectAnimalsen
dc.subjectChickensen
dc.subjectCytosol/drug effects/*enzymologyen
dc.subjectEnzyme Induction/drug effectsen
dc.subjectGuinea Pigsen
dc.subjectIsoenzymes/biosynthesisen
dc.subjectLiver/drug effects/*enzymologyen
dc.subjectMaleen
dc.subjectMethylcholanthrene/pharmacologyen
dc.subjectMiceen
dc.subjectMice, Inbred C57BLen
dc.subjectMice, Inbred DBAen
dc.subjectPhenobarbital/pharmacologyen
dc.subjectRana ridibundaen
dc.subjectRatsen
dc.subjectRats, Inbred Strainsen
dc.subjectSpecies Specificityen
dc.subjectTriturusen
dc.subjectTrouten
dc.titleInducibility of liver cytosolic aldehyde dehydrogenase activity in various animal speciesen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/2576795-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate1989-
heal.abstract1. The inducibility of hepatic cytosolic aldehyde dehydrogenase activity was studied in rat, mouse, guinea pig, chicken, frog, salamander and rainbow trout, by using two different types of inducers of drug metabolism. 2. Phenobarbital (a type I inducer of drug metabolizing enzymes) increased total liver cytosolic aldehyde dehydrogenase activity (up to 20-fold) in a genetically defined substrain of responsive rats (RR) and only slightly, if at all, in a non-responsive substrain (rr). On the contrary, both types of rats showed a highly induced aldehyde dehydrogenase activity after treatment with methylcholanthrene (a type II inducer). Phenobarbital is affecting mainly an isozyme of aldehyde dehydrogenase which is best measured with propionaldehyde as the substrate and NAD as the coenzyme (P/NAD). 3. Administration of phenobarbital to mice produced only a slight increase (2-fold) in the P/NAD aldehyde dehydrogenase activity. 4. Methylcholanthrene treatment caused a 2-fold increase of the hepatic P/NAD aldehyde dehydrogenase activity in the chicken. 5. In the guinea pig, phenobarbital produced an approximate 3-fold increase of the P/NAD activity. Methylcholanthrene had a similar effect, although to a lesser extent. 6. In the salamander, a 4-fold increase was detected in the enzyme activity measured with benzaldehyde as the substrate and NADP as the coenzyme (B/NADP), after treatment with either phenobarbital or methylcholanthrene. 7. The hepatic aldehyde dehydrogenase activities were found unchanged in the rainbow trout, after treatment with phenobarbital or 2,3,7,8-tetrachlorodibenzo-p-dioxin. 8. The rat model remains the only one examined that shares with human hepatocytes strong inducibility of the B/NADP aldehyde dehydrogenase isozyme upon treatment with polycyclic aromatic hydrocarbons.en
heal.journalNameComp Biochem Physiol Cen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ

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