Abstract
Expression of P450 1A1l 1A2 and 2 B1l 2B2 isoenzymes in rat brain was studied by Western blotting, using polyclonal antibodies raised against hepatic P450 1A1l 1A2 and 2B1l 2B2 isoenzymes. In addition, biochemical characterizations of the catalytic activities, pen toxyresorufin O-dealkylation (PROD) and ethoxyre-sorufin O-deethylation (EROD), selective for P450 2B1l 2B2 (PROD) and P450 1A1l 1A2 (EROD), were performed with rat brain microsomes. Control rat brain microsomes did not crossreact with either of the antibodies, whereas microsomes obtained from 3-methylcholanthrene (MC)-pretreated rats revealed significant immunoreactivity with anti-P450 1A1l 1A2. Similar results were observed with phenobarbital (PB)-pretreated rats, with the brain microsomes exhibiting significant immunoreactivity with anti-P450 2B1l 2B2. The induction in the P450 isoenzymes after PB or MC pretreatment was much less in the brain in comparison to the liver. Enzymatic studies indicated that the activities of PROD and EROD were induced in brain 3—4 fold by PB and MC pretreatment, respectively, and were almost completely inhibited on in vitro addition of anti-P450 2B1l 2B2 and 1A1l 1A2. These data demonstrate the expression of P4501A1l 1A2 and 2B1l 2B2 isoenzymes in the brain and indicate that, as in liver, these isoenzymes catalyze EROD and PROD, respectively, in the rat brain.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
