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Am J Physiol Lung Cell Mol Physiol 277: L653-L661, 1999;
1040-0605/99 $5.00
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Vol. 277, Issue 3, L653-L661, September 1999

Actin reorganization in airway smooth muscle cells involves Gq and Gi-2 activation of Rho

Carol A. Hirshman and Charles W. Emala

Department of Anesthesiology, College of Physicians and Surgeons of Columbia University, New York, New York 10032

Extracellular stimuli induce cytoskeleton reorganization (stress-fiber formation) in cells and Ca2+ sensitization in intact smooth muscle preparations by activating signaling pathways that involve Rho proteins, a subfamily of the Ras superfamily of monomeric G proteins. In airway smooth muscle, the agonists responsible for cytoskeletal reorganization via actin polymerization are poorly understood. Carbachol-, lysophosphatidic acid (LPA)-, and endothelin-1-induced increases in filamentous actin staining are indicative of actin reorganization (filamentous-to-globular actin ratios of 2.4 ± 0.3 in control cells, 6.7 ± 0.8 with carbachol, 7.2 ± 0.8 with LPA, and 7.4 ± 0.9 with endothelin-1; P < 0.001; n = 14 experiments). Although the effect of all agonists was blocked by C3 exoenzyme (inactivator of Rho), only carbachol was blocked by pertussis toxin. Although carbachol-induced actin reorganization was blocked in cells pretreated with antisense oligonucleotides directed against Galpha i-2 alone, LPA- and endothelin-1-induced actin reorganization were only blocked when both Galpha i-2 and Gqalpha were depleted. These data indicate that in human airway smooth muscle cells, carbachol induces actin reorganization via a Galpha i-2 pathway, whereas LPA or endothelin-1 induce actin reorganization via either a Galpha i-2 or a Gqalpha pathway.

G protein; endothelin-1; carbachol; lysophosphatidic acid; antisense oligonucleotide; Galpha i-2; cell culture


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