Stimulation of ERK2 by taurine with enhanced alkaline phosphatase activity and collagen synthesis in osteoblast-like UMR-106 cells

Biochem Pharmacol. 2001 Oct 15;62(8):1107-11. doi: 10.1016/s0006-2952(01)00741-9.

Abstract

Taurine is present in a variety of tissues and exhibits many important physiological functions in the cell. Even though its functions are well documented in many tissues, its actions on bone cells are largely unknown. Considering a recent finding that taurine is present in the bone, we wished to determine if taurine could have any effects on osteoblast cells. Taurine (10 mM) stimulated alkaline phosphatase activity as well as collagen synthesis. Taurine also stimulated tyrosine phosphorylation of a number of cellular proteins including a 42-kDa protein. The 42-kDa protein was identified as extracellular signal regulated protein kinase 2 (ERK2). A mitogen-activated protein kinase kinase (MEK) inhibitor blocked the taurine-stimulated alkaline phosphatase activity and collagen synthesis. These results suggest that taurine could regulate osteoblast metabolism via ERK2 activation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkaline Phosphatase / metabolism*
  • Animals
  • Cell Survival / drug effects
  • Collagen / biosynthesis*
  • Drug Interactions
  • Enzyme Activation / drug effects
  • Enzyme Inhibitors / pharmacology
  • Mitogen-Activated Protein Kinase 1 / metabolism*
  • Osteoblasts / drug effects
  • Osteoblasts / metabolism
  • Phosphorylation / drug effects
  • Protein-Serine-Threonine Kinases / antagonists & inhibitors
  • Rats
  • Taurine / pharmacology*
  • Tumor Cells, Cultured
  • Tyrosine / metabolism

Substances

  • Enzyme Inhibitors
  • Taurine
  • Tyrosine
  • Collagen
  • Protein-Serine-Threonine Kinases
  • Mitogen-Activated Protein Kinase 1
  • Alkaline Phosphatase