title: Differences in teratogenic and toxic properties of alcohol dehydrogenase inhibitors pyrazole and 4-methylpyrazole in Drosophila melanogaster: II. Adh allozymes in an isogenic background.
abstract: Pyrazole and 4-methylpyrazole (4-MP) are in vivo and in vitro inhibitors of alcohol dehydrogenase activity in mammals. The fruitfly Drosophila melanogaster has been used to demonstrate the influence of genetic variation in alcohol dehydrogenase alleles on the results of larval treatment with pyrazole and 4-MP. Genetic polymorphism of organisms involved in experiments with teratogenic and toxic agents is not often considered. Administration of pyrazole to larvae of isogenic D. melanogaster strains, differing mainly in their Adh alleles, caused large Notch-like teratogenic aberrations, macrochaetae multiplication, and pupal mortality. The level of teratogenicity and developmental-toxicity of pyrazole was both concentration and Adh-genotype-dependent. The strain with the highest ADH activity showed smaller effects after the treatments with the two concentrations used. 4-MP does not cause morphological aberrations, although treatment of larvae with an isogenic background caused a high pupal mortality due to non-differentiated material in the pupal case.
authors.affiliation: Department of Plant Ecology and Evolutionary Biology, Utrecht University, The Netherlands.
authors.forename: K T
authors.initials: KT
authors.lastname: Eisses
mesh_terms: D000014:Abnormalities, Drug-Induced / Q000201:enzymology*; D000426:Alcohol Dehydrogenase / Q000037:antagonists & inhibitors* / Q000235:genetics; D000818:Animals; D002874:Chromosome Mapping; D004331:Drosophila melanogaster / Q000187:drug effects* / Q000201:enzymology / Q000235:genetics; D005260:Female; D000077604:Fomepizole; D014644:Genetic Variation; D007527:Isoenzymes / Q000037:antagonists & inhibitors* / Q000235:genetics; D008297:Male; D011720:Pyrazoles / Q000633:toxicity*
chemical_list: D007527:Isoenzymes; D011720:Pyrazoles; C031280:pyrazole; D000077604:Fomepizole; D000426:Alcohol Dehydrogenase