The in vitro effect of Helichrysi flos on microsomal lipid peroxidation

J Ethnopharmacol. 2001 Sep;77(1):31-5. doi: 10.1016/s0378-8741(01)00258-6.

Abstract

Helichrysum arenarium (L.) Moench has long been known as a medicinal plant in Europe for its cholagogue, choleretic, hepatoprotective and detoxifying activities. Antioxidant properties of its main phenolics, flavonoids may be supposed to be responsible for these effects. The aim of this study was to verify the antioxidant properties of lyophilized water extracts with different polyphenol and flavonoid contents from inflorescences. The effects of natural extracts on microsomal fraction of rat liver were examined. Enzymatically induced lipid peroxidation and NADPH cytochrome c reductase activity in liver microsomes were measured by spectrophotometric methods. Results were compared with the activity of silibinin flavonoid, the main agent of well-known milk thistle (Silybum marianum L.). The natural plant extracts diminish the enzymatically induced lipid peroxidation in a concentration-dependent manner and reduce the cytochrome c dose dependently. The sample with higher polyphenol and flavonoid contents showed more stimulation of NADPH cytochrome c reductase. The lyophilized Helichrysi flos extracts proved to be more effective compared to silibinin in examined concentrations.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antioxidants / pharmacology*
  • Asteraceae / chemistry*
  • Cytochrome c Group / drug effects
  • Flavonoids / analysis
  • Lipid Peroxidation / drug effects
  • Microsomes, Liver / drug effects
  • Microsomes, Liver / metabolism
  • NADPH-Ferrihemoprotein Reductase / metabolism
  • Phenols / analysis
  • Plant Extracts / pharmacology*
  • Plant Stems
  • Plants, Medicinal
  • Rats
  • Silybum marianum / chemistry
  • Silymarin / pharmacology

Substances

  • Antioxidants
  • Cytochrome c Group
  • Flavonoids
  • Phenols
  • Plant Extracts
  • Silymarin
  • NADPH-Ferrihemoprotein Reductase