Inhibition of the formation of the neurotoxin 5-S-cysteinyl-dopamine by polyphenols

Biochem Biophys Res Commun. 2007 Oct 19;362(2):340-6. doi: 10.1016/j.bbrc.2007.07.153. Epub 2007 Aug 7.

Abstract

The death of nigral neurons in Parkinson's disease is thought to involve the formation of the endogenous neurotoxin, 5-S-cysteinyl-dopamine. In the present study, we show that the polyphenols, (+)-catechin and caffeic acid, which contain a catechol moiety, inhibit tyrosinase-induced formation of 5-S-cysteinyl-dopamine via their capacity to undergo tyrosinase-induced oxidation to yield cysteinyl-polyphenol adducts. In contrast, the inhibition afforded by the flavanone, hesperetin, was not accompanied by the formation of cysteinyl-hesperetin adducts, indicating that it may inhibit via direct interaction with tyrosinase. Whilst the stilbene resveratrol also inhibited 5-S-cysteinyl-dopamine formation, this was accompanied by the formation of dihydrobenzothiazine, a strong neurotoxin. Our data indicate that the inhibitory effects of polyphenols against 5-S-cysteinyl-dopamine formation are structure-dependent and shed further light on the mechanisms by which polyphenols exert protection against neuronal injury relevant to neurodegenerative diseases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromatography, High Pressure Liquid
  • Dopamine / analogs & derivatives*
  • Dopamine / chemistry
  • Dopamine / metabolism
  • Flavonoids / chemistry*
  • Flavonoids / pharmacology
  • Mass Spectrometry
  • Monophenol Monooxygenase / antagonists & inhibitors
  • Monophenol Monooxygenase / chemistry
  • Monophenol Monooxygenase / metabolism
  • Neurotoxins / antagonists & inhibitors
  • Neurotoxins / chemistry*
  • Neurotoxins / metabolism
  • Phenols / chemistry*
  • Phenols / pharmacology
  • Polyphenols

Substances

  • Flavonoids
  • Neurotoxins
  • Phenols
  • Polyphenols
  • 5-S-cysteinyldopamine
  • Monophenol Monooxygenase
  • Dopamine