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Dextromethorphan O-demethylase activity in rat brain microsomes.

Abstract
CYP2D, a genetically variable isoform of cytochrome P450, has been characterized mainly in the liver and the brain of mammals by measurement of debrisoquine hydroxylase activity. Moreover, 'poor debrisoquine metabolizer' phenotype is significantly increased in Parkinson's disease patients. We present here the first demonstration that the activity of the CYP2D isoform can be characterized in rat brain microsomes by the measurement of dextromethorphan O-demethylase capacity. The cerebral formation of dextrorphan, an antagonist of the N-methyl-D-aspartate receptor, was inhibited by the presence of quinidine and N-methyl-4-phenylpyridinium (MPP+), a dopaminergic neurotoxin inducing a chemical parkinsonism in humans.
AuthorsC Jolivalt, A Minn, M Vincent-Viry, M M Galteau, G Siest
JournalNeuroscience letters (Neurosci Lett) Vol. 187 Issue 1 Pg. 65-8 (Feb 24 1995) ISSN: 0304-3940 [Print] Ireland
PMID7617305 (Publication Type: Journal Article)
Chemical References
  • Pyridines
  • Cytochrome P-450 Enzyme System
  • Oxidoreductases, O-Demethylating
  • dextromethorphan O-demethylase
  • Quinidine
  • pyridine
Topics
  • Animals
  • Brain (enzymology)
  • Cytochrome P-450 Enzyme System (metabolism)
  • Dose-Response Relationship, Drug
  • Kinetics
  • Male
  • Microsomes (physiology)
  • Oxidoreductases, O-Demethylating (metabolism)
  • Pyridines (pharmacology)
  • Quinidine (pharmacology)
  • Rats
  • Rats, Sprague-Dawley

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