Protein tyrosine phosphatase 1B inhibitory activity of amentoflavone and its cellular effect on tyrosine phosphorylation of insulin receptors

Biol Pharm Bull. 2007 Feb;30(2):379-81. doi: 10.1248/bpb.30.379.

Abstract

Inhibition of protein tyrosine phosphatase 1B (PTP1B) has been proposed as a strategy for the treatment of type 2 diabetes and obesity. Bioassay-guided fractionation of MeOH extract of Selaginella tamariscina (Selaginellaceae) afforded a PTP1B inhibitory compound, amentoflavone. The compound inhibited PTP1B with an IC50 value of 7.3+/-0.5 microM. Kinetic study suggested that amentoflavone is a non-competitive inhibitor of PTP1B, with a Ki value of 5.2 microM. Treatment of 32D cells overexpressing the insulin receptor (IR) with amentoflavone resulted in a dose-dependent increase in tyrosine phosphorylation of IR. These results indicate that amentoflavone may enhance insulin-induced intracellular signaling possibly through inhibition of PTP1B activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biflavonoids / pharmacology*
  • Dual Specificity Phosphatase 3
  • Phosphoprotein Phosphatases / metabolism
  • Phosphorylation
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1
  • Protein Tyrosine Phosphatases / antagonists & inhibitors*
  • Protein Tyrosine Phosphatases / metabolism
  • Receptor, Insulin / metabolism*
  • Tyrosine / metabolism*

Substances

  • Biflavonoids
  • Tyrosine
  • amentoflavone
  • Receptor, Insulin
  • Phosphoprotein Phosphatases
  • Dual Specificity Phosphatase 3
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1
  • Protein Tyrosine Phosphatases