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Activation of MMP-2 by Clostridium difficile toxin B in bovine smooth muscle cells

T Koike1, M Kuzuya, T Asai

  • 1Department of Geriatrics, Nagoya University Graduate School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya, 466-8550, Japan.

Biochemical and Biophysical Research Communications
|October 12, 2000
PubMed

Insights

Rho family GTPases regulate cell migration by controlling actin reorganization and matrix metalloproteinase-2 (MMP-2) activation. Clostridium difficile toxin B activated MMP-2, suggesting a role for these GTPases in MMP-2 regulation.

Area of Science:

  • Cell Biology
  • Biochemistry

Background:

  • Matrix metalloproteinase-2 (MMP-2) is crucial for cell migration via extracellular matrix degradation.
  • Rho family GTPases are key regulators of dynamic actin reorganization during cell movement.

Purpose of the Study:

  • To investigate the relationship between Rho family GTPase activity and the regulation of MMP-2.
  • To understand the specific roles of Rho, Rho-kinase, and their downstream effectors in MMP-2 activation.

Main Methods:

  • Utilized inhibitors of Rho family GTPases, including Clostridium difficile toxin B, C3 transferase, and Y-27632, on smooth muscle cells.
  • Monitored MMP-2 activation, actin reorganization, cell morphology, and expression/processing of MT1-MMP.

Main Results:

  • Clostridium difficile toxin B inactivated Rho family GTPases and activated MMP-2.
  • C3 transferase and Y-27632 did not induce MMP-2 activation but altered cell morphology by inhibiting actin stress fibers.
  • Toxin B treatment led to increased expression and processing of MT1-MMP, a known MMP-2 activator.

Conclusions:

  • Rho family GTPases are involved in MMP-2 activation.
  • Complete inhibition of Rho or Rho-kinase is insufficient for MMP-2 activation.
  • MMP-2 activation is mediated through the expression and activation of MT1-MMP, influenced by Rho family GTPases.

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