PTP1B inhibitory activity of kaurane diterpenes isolated from Siegesbeckia glabrescens

J Enzyme Inhib Med Chem. 2006 Aug;21(4):379-83. doi: 10.1080/14756360600741560.

Abstract

Protein tyrosine phosphatase 1B (PTP1B) is considered as a therapeutic target for the treatment of diabetes and obesity. In our preliminary screening study, a MeOH extract of the aerial part of Siegesbeckia glabrescens was found to inhibit PTP1B activity at 30 microg/mL. Bioassay-guided fractionation led to the isolation of two active diterpenes, ent-16betaH, 17-isobutyryloxy-kauran-19-oic acid (1) and ent-16betaH, 17-acetoxy-18-isobutyryloxy-kauran-19-oic acid (2), along with ent- 16betaH, 17-hydroxykauran-19-oic acid (3). Compounds 1 and 2 inhibited the PTP1B activity with IC50 values of 8.7 +/- 0.9 and 30.6 +/- 2.1 microM, respectively. Kinetic studies suggest that both 1 and 2 are non-competitive inhibitors of PTP1B. However, compound 3 substituted with a hydroxyl group at C-17 in kaurane-type showed no inhibitory effects towards PTP1B.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Asteraceae / metabolism*
  • Diterpenes, Kaurane / chemistry*
  • Diterpenes, Kaurane / pharmacology
  • Dose-Response Relationship, Drug
  • Drug Evaluation, Preclinical*
  • Enzyme Inhibitors / pharmacology*
  • Humans
  • Inhibitory Concentration 50
  • Kinetics
  • Models, Chemical
  • Plant Extracts / metabolism
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1
  • Protein Tyrosine Phosphatases / antagonists & inhibitors*
  • Protein Tyrosine Phosphatases / chemistry
  • Recombinant Proteins / chemistry

Substances

  • Diterpenes, Kaurane
  • Enzyme Inhibitors
  • Plant Extracts
  • Recombinant Proteins
  • PTPN1 protein, human
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1
  • Protein Tyrosine Phosphatases