Alpha-viniferin: a prostaglandin H2 synthase inhibitor from root of Carex humilis

Planta Med. 1998 Apr;64(3):204-7. doi: 10.1055/s-2006-957409.

Abstract

An inhibitor on cyclooxygenase activity of prostaglandin H2 synthase was purified from the root of Carex humilis Leyss (Cyperaceae) by a variety of column chromatographic methods. As a result of the structure analysis by FAB-mass, 1H-NMR, and 13C-NMR spectral data, the active compound was identified as (+)-alpha-viniferin, an oligomeric stilbene characterized originally from Caragana chamlagu Lamarck (Leguminosae). (+)-alpha-Viniferin exhibited a dose-dependent inhibition on cyclooxygenase activity, where 50% of inhibition (IC50) was shown at a final concentration of about 7 microM. Resveratrol, a putative building block of oligomeric stilbenes, also inhibited the cyclooxygenase activity. The inhibitory potency of (+)-alpha-viniferin was about 3- to 4-fold stronger than that of resveratrol on cyclooxygenase activity of prostaglandin H2 synthase partially purified from sheep seminal vesicles.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anti-Inflammatory Agents, Non-Steroidal / pharmacology*
  • Benzofurans / pharmacology*
  • Cyclooxygenase Inhibitors / pharmacology*
  • In Vitro Techniques
  • Male
  • Microsomes / drug effects
  • Microsomes / enzymology
  • Plant Extracts / pharmacology*
  • Plant Roots
  • Poaceae / chemistry
  • Prostaglandin-Endoperoxide Synthases / metabolism*
  • Seminal Vesicles / drug effects
  • Seminal Vesicles / enzymology
  • Sheep

Substances

  • Anti-Inflammatory Agents, Non-Steroidal
  • Benzofurans
  • Cyclooxygenase Inhibitors
  • Plant Extracts
  • alpha-viniferin
  • Prostaglandin-Endoperoxide Synthases