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: Subanesthetic concentrations of drugs inhibit cytochrome P450-mediated metabolism of aniline.
    Author: LaBella FS, Queen G.
    Journal: Eur J Pharmacol; 1995 Oct 06; 293(3):231-5. PubMed ID: 8666040.
    Abstract:
    We reported previously that 18 compounds varying in general anesthetic potency by up to 66 000-fold inhibited, at anesthetic concentrations, the metabolism of arachidonic acid and aminopyrine by cytochrome P450 monooxygenases in rat liver microsomes. Now, we report that P450-mediated para-hydroxylation of aniline is more sensitive to the anesthetics. The Ki values for enzyme inhibition for seven compounds were close to and for seven compounds 5-40 times less than their respective anesthetic potencies. Endogenous substrates with an aniline-like binding mode to P450 include histamine and related imidazoles. Acetone and each of the halogenated compounds, halothane, enflurane, and chloroform, stimulated aniline hydroxylase activity at concentrations well below and above their EC50 values. These potent actions on the universal P450 isoenzymes may contribute to pharmacological effects of the anesthetics associated with levels of drug well below concentrations that effect general anesthesia.
    [Abstract] [Full Text] [Related] [New Search]