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Am J Physiol Lung Cell Mol Physiol 274: L803-L809, 1998;
1040-0605/98 $5.00
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Vol. 274, Issue 5, L803-L809, May 1998

Carbachol-induced actin reorganization involves Gi activation of Rho in human airway smooth muscle cells

Hideaki Togashi1, Charles W. Emala1, Ian P. Hall2, and Carol A. Hirshman1,3

Departments of 1 Anesthesiology and 3 Environmental Health Sciences, The Johns Hopkins Medical Institutions, Baltimore, Maryland 21205; and 2 Department of Medicine, University Hospital, Queen's Medical Center, Nottingham N67 2UH, United Kingdom

To determine whether M2 muscarinic receptors are linked to the monomeric G protein Rho, we studied the effect of carbachol on actin reorganization (stress fiber formation) in cultured human airway smooth muscle cells that expressed mainly M2 muscarinic receptors by dual- fluorescence labeling of filamentous (F) and monomeric (G) actin. F-actin was labeled with FITC-labeled phalloidin, and G-actin was labeled with Texas Red-labeled DNase I. Carbachol stimulation induced stress fiber formation (increased F-actin staining) in the cells and increased the F- to G-actin ratio 3.6 ± 0.4-fold (mean ± SE; n = 5 experiments). Preincubation with pertussis toxin, Clostridium C3 exoenzyme, or tyrosine kinase inhibitors reduced the carbachol-induced increase in stress fiber formation and significantly decreased the F- to G-actin ratio, whereas a mitogen-activated protein kinase inhibitor, a phosphatidylinositol 3-kinase inhibitor, and a protein kinase C inhibitor were without effect. This study demonstrates that in cultured human airway smooth muscle cells, muscarinic-receptor activation induces stress fiber formation via a pathway involving a pertussis-sensitive G protein, Rho proteins, and tyrosine phosphorylation.

M2 muscarinic receptor; fluoroscein isothiocyanate-labeled phalloidin; Texas Red-labeled deoxyribonuclease; Gi proteins; Rho proteins; stress fiber formation


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