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i-2 is required for
carbachol-induced stress fiber formation in human airway smooth
muscle cells
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
G
i-2,
Gi-3, or
Gq. 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
-subunit expression. Oligonucleotide antisense treatment decreased
protein expression of the respective G protein -subunit. Antisense
depletion of the Gi-2 protein
but not of Gi-3 or
Gq protein blocked the
carbachol-induced increase in the F- to G-actin ratio. These results
show that the Gi-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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