Inhibition of VHR dual-specificity protein tyrosine phosphatase activity by flavonoids isolated from Scutellaria baicalensis: structure-activity relationships

Planta Med. 2002 Dec;68(12):1063-5. doi: 10.1055/s-2002-36351.

Abstract

Three flavonoids: norwogonin, dihydronorwogonin and baicalein, were isolated from the roots of Scutellaria baicalensis, as potential inhibitors of VHR dual-specificity protein tyrosine phosphatase (DS-PTPase). Norwogonin (IC 50 = 1.1 microM), dihydronorwogonin (IC 50 = 2.9 microM) and baicalein (IC 50 = 2.4 microM) showed potent inhibitory activity toward VHR, but had no inhibitory activity against T-cell protein tyrosine phosphatase or serine/threonine protein phosphatase 1. From comparisons to the inhibitory activities of other similar flavonoids, it could be suggested that the presence of a hydroxy group in the B ring of flavonoids interferes with the inhibitory activity toward VHR DS-PTPase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Dose-Response Relationship, Drug
  • Dual Specificity Phosphatase 3
  • Flavanones*
  • Flavones
  • Flavonoids / chemistry
  • Flavonoids / isolation & purification
  • Flavonoids / pharmacology*
  • Molecular Structure
  • Phosphoprotein Phosphatases / antagonists & inhibitors
  • Phytotherapy
  • Plant Extracts / chemistry
  • Plant Extracts / isolation & purification
  • Plant Extracts / pharmacology
  • Plant Roots / chemistry
  • Protein Phosphatase 1
  • Protein Tyrosine Phosphatases / antagonists & inhibitors*
  • Scutellaria baicalensis*
  • Structure-Activity Relationship

Substances

  • Flavanones
  • Flavones
  • Flavonoids
  • Plant Extracts
  • dihydronorwagonin
  • norwogonin
  • baicalein
  • Phosphoprotein Phosphatases
  • Protein Phosphatase 1
  • Dual Specificity Phosphatase 3
  • Protein Tyrosine Phosphatases