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AJP - Lung Cellular and Molecular Physiology, Vol 273, Issue 5 1020-L1028, Copyright © 1997 by American Physiological Society
ARTICLES |
Y. Amrani, V. Krymskaya, C. Maki and R. A. Panettieri Jr
Department of Medicine, University of Pennsylvania Medical Center, Philadelphia 19104, USA.
We have previously shown that tumor necrosis factor (TNF)-alpha, a cytokine involved in asthma, enhances Ca2+ responsiveness to bronchoconstrictor agents in cultured human airway smooth muscle (ASM) cells. In the present study, we investigated the potential mechanism(s) by which TNF-alpha modulates ASM cell responsiveness to such agents. In human ASM cells loaded with fura 2, TNF-alpha and interleukin (IL)-1 beta significantly enhanced thrombin- and bradykinin-evoked elevations of intracellular Ca2+. In TNF-alpha-treated cells. Ca2+ responses to thrombin and bradykinin were 350 +/- 14 and 573 +/- 93 nM vs. 130 +/- 17 and 247 +/- 48 nM in nontreated cells, respectively (P < 0.0001). In IL-1 beta-treated cells, the Ca2+ response to bradykinin was 350 +/- 21 vs. 127 +/- 12 nM in nontreated cells (P < 0.0001). The time course for TNF-alpha potentiation of agonist-induced Ca2+ responses requires a minimum of 6 h and was maximum after 12 h of incubation. In addition, cycloheximide, a protein synthesis inhibitor, completely blocked the potentiating effect of TNF-alpha on Ca2+ signals. We also found that TNF-alpha significantly enhanced increases in phosphoinositide (PI) accumulation induced by bradykinin. The percentage of change in PI accumulation over control was 115 +/- 8 to 210 +/- 15% in control cells vs. 128 +/- 10 to 437 +/- 92% in TNF-alpha-treated cells for 3 x 10(-9) to 3 x 10(-6) M bradykinin. The PI turnover to 10 mM NaF, a direct activator of G proteins, was also found to be enhanced by TNF-alpha. The percentage of change in PI accumulation over control increased from 280 +/- 35% in control cells to 437 +/- 92% in TNF-alpha-treated cells. Taken together, these results show that TNF-alpha can potently regulate G protein-mediated signal transduction in ASM cells by activating pathways dependent on protein synthesis. Our study demonstrates one potential mechanism underlying the enhanced Ca2+ response to bronchoconstrictor agents induced by cytokines in human ASM cells.
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