Pasteurella multocida toxin increases endothelial permeability via Rho kinase and myosin light chain phosphatase

Markus Essler, Karin Hermann, Mutsuki Amano, Kozo Kaibuchi, Jürgen Heesemann, Peter C. Weber, Martin Aepfelbacher

研究成果: Article査読

59 被引用数 (Scopus)

抄録

Pasteurella multocida toxin (PMT) has been shown to induce actin reorganization through activation of the GTPase Rho. Here we investigated the involvement of the Rho target proteins Rho kinase and myosin light chain (MLC) phosphatase in the PMT-induced increase in endothelial permeability and the underlying actin reorganization of endothelial cells, stimulation of endothelial layers With PMT enhanced transendothelial permeability > 10- fold, and this was abolished by pretreatment with the specific Rho inactivator C3 transferase from Clostridium botulinum. The PMT-induced increase in endothelial permeability was associated with 1) inactivation of MLC phosphatase, 2) an increase in MLC phosphorylation, and 3) endothelial cell retraction and actin stress fiber formation. PMT-stimulated actin reorganization could be prevented by 1) pretreatment of cells with C3 transferase, 2) microinjection of the Rho binding domain and the pleckstrin homology domain of Rho kinase, and 3) microinjection of constitutively active MLC phosphatase. Together, these results suggest that PMT activates Rho/Rho kinase, which inactivates MLC phosphatase. The resulting increase in MLC phosphorylation causes endothelial cell retraction and a rise in endothelial permeability.

本文言語English
ページ(範囲)5640-5646
ページ数7
ジャーナルJournal of Immunology
161
10
出版ステータスPublished - 15-11-1998
外部発表はい

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Immunology

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