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Phosphatidylinositol 3-kinase c mediates shear stress-dependent activation of JNK in endothelial cells


, : Phosphatidylinositol 3-kinase c mediates shear stress-dependent activation of JNK in endothelial cells. American Journal of Physiology 275(5): 898-H1904

Shear stress differentially activates extracellular signal-regulated kinase (ERK) and c-Jun NH2-terminal kinase (JNK) by mechanisms involving Gai2 and Gb/c proteins, respectively, in bovine aortic endothelial cells (BAEC). The early events in this signaling mechanism by which G proteins regulate ERK and JNK in response to shear stress have not been defined. Here we show that BAEC endogenously express a G protein-dependent form of phosphatidylinositol 3-kinase, PI3Kc, and its activity is stimulated by shear stress. PI3Kc activity was measured in vitro using BAEC that were transiently transfected with an epitope-tagged PI3Kc (vsv-PI3Kc). Exposure of BAEC to shear stress rapidly and transiently stimulated the activity of vsv-PI3Kc (maximum by 15 s, with a return to basal after 1-min exposure to 5 dyn/cm2 shear stress). Activity of vsv-PI3Kc was stimulated by shear stress intensities as low as 0.5 dyn/cm2. Treatment of BAEC with an inhibitor of PI3K, wortmannin, inhibited shear-dependent activation of JNK but had no effect on that of ERK. Furthermore, expression of a kinase-inactive mutant (PI3KcK799R) in BAEC inhibited the shear-dependent activation of JNK but not ERK. Taken together, these results suggest that PI3Kc selectively regulates the shear-sensitive JNK pathway. This differential and novel signaling pathway may be responsible for coordinating various mechanosensitive events in endothelial cells. Reprinted by permission of the publisher.

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