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4 results

  • 5 - Predictability of metabolic antiepileptic drug interactions

  • from Part II - Pharmacokinetic interactions
    • By Edoardo Spina, Section of Pharmacology, Department of Clinical and Experimental Medicine and Pharmacology, University of Messina, Messina, Italy, Emilio Perucca, Clinical Pharmacology Unit, University of Pavia, Pavia, Italy, Rene Levy, Department of Pharmaceutics, University of Washington, Seattle, WA, USA
  • Edited by Jerzy Majkowski, Blaise F. D. Bourgeois, Harvard University, Massachusetts, Philip N. Patsalos, Institute of Neurology, London, Richard H. Mattson, Yale University, Connecticut
  • Book:
    Antiepileptic Drugs
    Published online:
    07 September 2009
    Print publication:
    26 May 2005, pp 57-92

  • Summary

    Knowledge of the main enzyme systems involved in the biotransformation of antiepileptic drugs (AEDs) is essential for understanding the principles and mechanisms of metabolically based drug interactions involving these drugs. In recent years, the major cytochrome P450 (CYP) isoenzymes have been characterized at the molecular level and their different substrates, inhibitors and inducers have been identified. Drug interactions involving CYP isoforms and other drug-metabolizing enzymes may result from one of two processes, enzyme induction or inhibition. The potential for metabolic drug interactions is an important aspect to be considered during the development of new drugs. Initially, the simplest approach to the in vitro study of drug metabolism was through use of purified enzymes. Prediction of interactions that may affect the test drug requires knowledge of the enzyme systems and knowledge of the influence of other drugs on such enzyme systems.

  • 7 - Interactions between antiepileptic drugs

  • from Part II - Pharmacokinetic interactions
  • Edited by Jerzy Majkowski, Blaise F. D. Bourgeois, Harvard University, Massachusetts, Philip N. Patsalos, Institute of Neurology, London, Richard H. Mattson, Yale University, Connecticut
  • Book:
    Antiepileptic Drugs
    Published online:
    07 September 2009
    Print publication:
    26 May 2005, pp 111-138

  • Summary

    Old and new antiepileptic drugs (AEDs) are associated with a wide range of pharmacokinetic drug-drug interactions. Classical pharmacokinetic interactions are enzyme induction, enzyme inhibition and displacement from protein binding. Numerous studies have been performed showing that phenobarbital (PB) decreases concentrations of other concomitantly given AEDs. The interaction of phenytoin (PHT) with valproic acid (VPA) is somewhat complex as it primarily concerns protein binding. In the last decade, a series of new AEDs have become available for the treatment of epileptic patients. The experience of several decades with the classic AEDs has shown that interactions may have severe clinical consequences. Reports on AED interactions usually focus on the increase or decrease of serum concentrations. Most interactions correspond to the pharmacokinetic properties of the compounds, but it should be borne in mind that rare interactions may also play an important role in the individual.

  • Effect of dietary supplementation with carotenoids on xenobiotic metabolizing enzymes in the liver, lung, kidney and small intestine of the rat

  • Christopher Jewell, Nora M. O'Brien
  • Journal:
    British Journal of Nutrition / Volume 81 / Issue 3 / March 1999
    Published online by Cambridge University Press:
    09 March 2007, pp. 235-242
    Print publication:
    March 1999
    • Article
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  • The effect of 16 d intake of 300 mg carotenoids/kg diet (β-carotene (βC), bixin (BX), lycopene (LY), lutein (LU), canthaxanthin (CX) or astaxanthin (AX)) on xenobiotic metabolizing enzymes in the liver, lung, kidney and small intestine of male Wistar rats was assessed. A control group received the basal diet (AIN-76) without carotenoids and a positive control group for enzyme induction received 3-methylcholanthrene (3-MC) at 666 mg/kg diet. Cytochrome P450 activity was assessed using the substrates ethoxyresorufin for P450 1A1, methoxyresorufin for P450 1A2, pentoxyresorufin for P450 2B1/2 and benzyloxyresorufin for P450 types 1A1/2, 2B1/2 and 3A. Glutathione-S-transferase (EC 2.5.1.18) and reduced glutathione status were assessed. Carotenoid uptake by the tissues was also determined. 3-MC and the carotenoids BX, CX and AX led to significant increases compared with control in liver, lung and kidney ethoxyresorufin-O-deethylation. Methoxyresorufin-O-demethylation activity was significantly increased in liver and lung by BX, CX and AX but only CX and AX significantly increased activity in kidney. Pentoxyresorufin-O-depentylation and benzyloxyresorufin-O-dearylation increased in liver of 3-MC-, BX-, CX- and AX-treated rats, but to a much lesser degree than for the other two substrates. Benzyloxyresorufin-O-dearylation in lung was significantly decreased by all carotenoids. Activities of any of the measured enzymes in the small intestine were undetectable in all treatment groups except the 3-MC group. Glutathione status was unaffected by any of the treatments. This is the first study identifying the carotenoids BX, CX and AX as inducers of rat lung and kidney xenobiotic metabolizing enzymes.