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J Biol Chem, Vol. 274, Issue 15, 9918-9922, April 9, 1999
B Activation in Cultured Human
Epithelial Cells
,,
From the The signaling mechanisms utilized by bradykinin
(BK) to activate the transcription factor nuclear factor Department of Molecular and Experimental
Medicine, The Scripps Research Institute, La Jolla, California 92037 and the § Department of Pediatrics, University of California
at San Diego, La Jolla, California 92037
B (NF-B)
are poorly defined. We previously demonstrated that BK-stimulated
NF-B activation requires the small GTPase RhoA. We present
evidence that BK-induced NF-B activation both activates and requires
phosphatidylinositol 3-kinase (PI 3-kinase) in A549 human epithelial
cells. Pre-treatment with the PI 3-kinase-specific inhibitors,
wortmannin, and LY294002 effectively blocked BK-induced PI
3-kinase activity. Wortmannin and LY294002 also abolished
BK-induced NF-B activation, as did transient transfection with a
dominant negative mutant of the p85 subunit. BK-stimulated PI 3-kinase
activity and NF-B activation were sensitive to pertussis but not
cholera toxin, suggesting that the B2 BK receptors transducing the
response were coupled to G
i or Go heterotrimeric G proteins.
Tumor necrosis factor (TNF) also stimulated increased PI
3-kinase activity, however TNF-stimulated NF-B activation was not
affected by the PI 3-kinase inhibitors or the p85 dominant negative
mutant. These findings provide evidence that BK-induced NF-B
activation utilizes a signaling pathway that requires activity of both
RhoA and PI 3-kinase and is distinct from the signaling pathway
utilized by TNF. Furthermore, we show that the p85 regulatory
subunit is required for activation of PI 3-kinase activity by this G
protein-coupled receptor.
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