These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Dissociation of cytochrome P-450 inactivation and induction.
    Author: Ortiz de Montellano PR, Costa AK.
    Journal: Arch Biochem Biophys; 1986 Dec; 251(2):514-24. PubMed ID: 3800382.
    Abstract:
    Polycyclic aromatic hydrocarbons bind to a cytosolic receptor that translocates into the nucleus and induces the synthesis of mRNA for a subset of cytochrome P-450 isozymes. The failure to detect a "phenobarbital" receptor, however, suggests that the induction of P-450b/e, the isozymes induced by phenobarbital, is mediated by a less direct mechanism. One attractive alternative is that a receptor exists for an endogenous substance that is specifically turned over by the trace amounts of P-450b/e present in uninduced liver. Changes in the concentration of this substance caused by agents that inhibit P-450b/e would then trigger the induction response. We report here that suppressing the catalytic activities of P-450b/e for prolonged periods with 1-aminobenzotriazole, a mechanism-based irreversible inhibitor, neither induces P-450b/e nor interferes with induction of these isozymes at the level of transcription by phenobarbital. The results argue against mechanisms for the induction of P-450b/e keyed to the effective catalytic availability of these isozymes.
    [Abstract] [Full Text] [Related] [New Search]