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Involvement of p38MAP kinase in bone morphogenetic protein-4-induced osteoprotegerin in mouse bone-marrow-derived

Michiko Tazoe1, Makio Mogi, Shigemi Goto

  • 1Department of Pharmacology, School of Dentistry, Aichi-Gakuin University, Nagoya 464-8650, Japan.

Archives of Oral Biology
|June 28, 2003
PubMed

Insights

Bone morphogenetic protein (BMP)-4 increases soluble osteoprotegerin (OPG) levels in ST2 cells by activating p38 MAP kinase. This pathway is crucial for BMP-4-induced OPG production, regulating bone resorption.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Osteoprotegerin (OPG) is a cytokine regulating bone mass by inhibiting osteoclastic bone resorption.
  • OPG belongs to the tumor necrosis factor receptor superfamily.

Purpose of the Study:

  • To investigate the effect of bone morphogenetic protein (BMP)-4 on OPG production in ST2 cells.
  • To elucidate the signaling pathway involved in BMP-4-induced OPG production.

Main Methods:

  • Mouse bone-marrow-derived stromal cell line (ST2) treated with BMP-4.
  • Measurement of soluble OPG levels.
  • In vitro immunocomplex kinase assay to assess MAP kinase activation.
  • Inhibition studies using SB203580 (p38 MAP kinase inhibitor) and PD98059 (classic MAP kinase inhibitor).

Main Results:

  • BMP-4 significantly increased soluble OPG levels in ST2 cells.
  • BMP-4 did not affect OPG ligand production.
  • BMP-4 activated p38 MAP kinase.
  • SB203580, but not PD98059, inhibited BMP-4-induced OPG increase.

Conclusions:

  • BMP-4 induces OPG production in ST2 cells.
  • Activation of the p38 MAP kinase pathway is essential for BMP-4-induced OPG induction.
  • This finding provides insight into the molecular mechanisms regulating bone resorption.

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