title: Drug metabolizing enzyme systems in the houbara bustard (Chlamydotis undulata).
abstract: This study compared catalytic and immunochemical properties of drug metabolizing phase I and II enzyme systems in houbara bustard (Chlamydotis undulata) liver and kidney and rat liver. P450 content in bustard liver (0.34 +/- 0.03 nmol mg-1 protein) was 50% lower than that of rat liver (0.70 +/- 0.02 nmol mg-1 protein). With the exception of aniline hydroxylase activity, monooxygenase activities using aminopyrine, ethoxyresorufin and ethoxycoumarin as substrates were all significantly lower than corresponding rat liver enzymes. As found in mammalian systems the P450 activities in the bird liver were higher than in the kidney. Immunohistochemical analysis of microsomes using antibodies to rat hepatic P450 demonstrated that bustard liver and kidney express P4502C11 homologous protein; no appreciable cross-reactivity was observed in bustards using antibodies to P4502E1, 1A1 or 1A2 isoenzymes. Glutathione content and glutathione S-transferase (GST) activity in bustard liver were comparable with those of rat liver. GST activity in the kidney was 65% lower than the liver. Western blotting of liver and kidney cytosol with human GST isoenzyme-specific antibodies revealed that the expression of alpha-class of antibodies exceeds mu in the bustard. In contrast, the pi-class of GST was not detected in the bustard liver. This data demonstrates that hepatic and renal microsomes from the bustard have multiple forms of phase I and phase II enzymes. The multiplicity and tissue specific expression of xenobiotic metabolizing enzymes in bustards may play a significant role in determining the pharmacokinetics of drugs and susceptibility of the birds to various environmental pollutants and toxic insults.
authors.affiliation: Veterinary Science Department, Environmental Research and Wildlife Development Agency, Abu Dhabi, United Arab Emirates.
authors.forename: T A
authors.initials: TA
authors.lastname: Bailey
authors.forename: A
authors.initials: A
authors.lastname: John
authors.forename: E P
authors.initials: EP
authors.lastname: Mensah-Brown
authors.forename: A
authors.initials: A
authors.lastname: Garner
authors.forename: J
authors.initials: J
authors.lastname: Samour
authors.forename: H
authors.initials: H
authors.lastname: Raza
mesh_terms: D000818:Animals; D001189:Aryl Hydrocarbon Hydroxylases; D001717:Birds / Q000378:metabolism*; D019363:Cytochrome P-450 CYP1A1 / Q000032:analysis; D019388:Cytochrome P-450 CYP1A2 / Q000032:analysis; D003577:Cytochrome P-450 Enzyme System / Q000032:analysis* / Q000737:chemistry; D003580:Cytochromes; D003600:Cytosol / Q000201:enzymology; D005982:Glutathione Transferase / Q000032:analysis* / Q000737:chemistry; D007150:Immunohistochemistry; D007527:Isoenzymes / Q000032:analysis* / Q000737:chemistry; D007668:Kidney / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D008861:Microsomes / Q000201:enzymology; D051381:Rats; D013045:Species Specificity; D039181:Steroid 16-alpha-Hydroxylase; D013250:Steroid Hydroxylases / Q000032:analysis
chemical_list: D003580:Cytochromes; D007527:Isoenzymes; D003577:Cytochrome P-450 Enzyme System; D013250:Steroid Hydroxylases; D001189:Aryl Hydrocarbon Hydroxylases; C017170:Cyp1a2 protein, rat; D019363:Cytochrome P-450 CYP1A1; D019388:Cytochrome P-450 CYP1A2; D039181:Steroid 16-alpha-Hydroxylase; D005982:Glutathione Transferase