Acute inactivation of tryptophan hydroxylase by amphetamine analogs involves the oxidation of sulfhydryl sites

Eur J Pharmacol. 1989 Mar 7;172(1):93-7. doi: 10.1016/0922-4106(89)90048-5.

Abstract

The activity of rat hippocampal tryptophan hydroxylase was reduced from 30-60% 3 h after the administration of a 10-15 mg/kg dose of either fenfluramine, methamphetamine or 3,4-methylenedioxymethamphetamine (MDMA). Tryptophan hydroxylase inactivated by these drug treatments could be reconstituted by a prolonged anaerobic incubation in the presence of 5 mM dithiothreitol and 50 microM Fe2+. Drug-inactivated enzyme obtained from rats killed 18 h after multiple doses of either D(+)- or L(-)-MDMA could not be similarly restored. These observations suggest that the rapid decrease in central tryptophan hydroxylase activity induced by amphetamine analogs results from the reversible oxidation of a sulfhydryl site(s) within the enzyme molecule, whereas the irreversible decrease in enzymatic activity measured 18 h after multiple-dose MDMA treatment may reflect serotonergic toxicity.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amphetamines / pharmacology*
  • Anaerobiosis
  • Animals
  • Dithiothreitol / pharmacology
  • Enzyme Activation / drug effects
  • Hippocampus / enzymology
  • Iron / pharmacology
  • Male
  • Oxidation-Reduction
  • Rats
  • Rats, Inbred Strains
  • Sulfhydryl Compounds / analysis*
  • Tryptophan Hydroxylase / antagonists & inhibitors*

Substances

  • Amphetamines
  • Sulfhydryl Compounds
  • Iron
  • Tryptophan Hydroxylase
  • Dithiothreitol