Biochemical properties and mechanism of action of a vanadyl(IV)-aspirin complex on bone cell lines in culture

Biometals. 2002 Mar;15(1):37-49. doi: 10.1023/a:1013183910203.

Abstract

A recently synthesized vanadyl(IV) complex with aspirin [VO(aspirin)ClH2O]2, has been thoroughly investigated by physicochemical techniques. In order to support the proposed structure, stoichiometry and the coordination sphere of the vanadium center, some studies such as elemental analysis, electronic (diffuse reflectance) and vibrational (infrared) spectroscopies, magnetic susceptibility, as well as the thermal behavior, were carried out. The bioactivity of the vanadium complex (VOAspi) was evaluated on two osteoblast-like cell lines in culture, being its cytotoxic effects stronger than the vanadyl cation as assessed by morphological changes and lipid peroxidation. These effects may be partially explained through the induction of the expression of Erks (Extracellular signal-regulated kinases) and the inhibition of the PTPases (Phosphotyrosine phosphatases) present in the cellular extracts.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Animals
  • Aspirin / analogs & derivatives*
  • Aspirin / chemistry
  • Aspirin / pharmacology
  • Cell Line
  • Chemical Phenomena
  • Chemistry, Physical
  • Enzyme Inhibitors / pharmacology
  • Lipid Peroxidation / drug effects
  • Mice
  • Mitogen-Activated Protein Kinase 1 / metabolism
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinases / metabolism
  • Osteoblasts / cytology
  • Osteoblasts / drug effects*
  • Osteoblasts / metabolism*
  • Protein Tyrosine Phosphatases / antagonists & inhibitors
  • Rats
  • Spectrophotometry, Infrared
  • Vanadates / chemistry
  • Vanadates / pharmacology*

Substances

  • Enzyme Inhibitors
  • Vanadates
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinases
  • Protein Tyrosine Phosphatases
  • Aspirin