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Am J Physiol Lung Cell Mol Physiol 275: L911-L916, 1998;
1040-0605/98 $5.00
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Vol. 275, Issue 5, L911-L916, November 1998

Galpha i-2 is required for carbachol-induced stress fiber formation in human airway smooth muscle cells

Carol A. Hirshman1,2, Hideaki Togashi1, Dan Shao1, and Charles W. Emala1

Departments of 1 Anesthesiology and 2 Environmental Health Sciences, The Johns Hopkins Medical Institutions, Baltimore, Maryland 21205

To determine which heterotrimeric G protein couples muscarinic receptors to stress fiber formation [measured by an increase in the filamentous (F)- to monomeric (G)-actin ratio] in human airway smooth muscle (ASM) cells, cultured human ASM cells expressing the M2 muscarinic receptor were grown to confluence. Cells were exposed for 6 days to 10 µM antisense oligonucleotides designed to specifically bind to the mRNA encoding Galpha i-2, Galpha i-3, or Gqalpha . A randomly scrambled oligonucleotide served as a control. F- to G-actin ratios were measured with dual-fluorescence labeling after 5 min of carbachol exposure, which is known to increase the F- to G-actin ratio. Cells in parallel wells were harvested for immunoblot analysis of G protein alpha -subunit expression. Oligonucleotide antisense treatment decreased protein expression of the respective G protein alpha -subunit. Antisense depletion of the Galpha i-2 protein but not of Galpha i-3 or Gqalpha protein blocked the carbachol-induced increase in the F- to G-actin ratio. These results show that the Galpha i-2 protein couples muscarinic receptors to stress fiber formation in ASM.

G protein; fluorescein isothiocyanate-labeled phalloidin; Texas Red-labeled deoxyribonuclease I; antisense oligonucleotide


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