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Am J Physiol Lung Cell Mol Physiol 278: L1138-L1145, 2000;
1040-0605/00 $5.00
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Vol. 278, Issue 6, L1138-L1145, June 2000

Tyrosine kinase-dependent calcium signaling in airway smooth muscle cells

Barbara Tolloczko, Florence C. Tao, Mary E. Zacour, and James G. Martin

Seymour Heisler Laboratory of the Montreal Chest Institute Research Centre and Meakins-Christie Laboratories, Department of Medicine, McGill University, Montreal, Quebec, Canada H2X 2P2

Contractile agonists may stimulate mitogenic responses in airway smooth muscle by mechanisms that involve tyrosine kinases. The role of contractile agonist-evoked activation of tyrosine kinases in contractile signaling is not clear. We addressed this issue using cultured rat airway smooth muscle cells. In these cells, serotonin (5-HT, 1 µM) caused contraction (quantitated by a decrease in cell area), which was blocked by the tyrosine kinase inhibitor genistein (40 µM). Genistein and tyrphostin 23 (40 and 10 µM, respectively) significantly decreased 5-HT-evoked peak Ca2+ responses, and the effect of genistein could be observed in the absence of extracellular Ca2+. The specific inhibitor of mitogen-activated protein kinase kinase PD-98059 (30 µM) had no significant effect on peak Ca2+ levels. Western analysis of cell extracts revealed that 5-HT caused a significant increase in tyrosine phosphorylation of proteins with molecular masses of ~70 kDa within 10 s of stimulation but no measurable tyrosine phosphorylation of the gamma  isoform of phospholipase C (PLC-gamma ). Tyrosine phosphorylation was inhibited by genistein. Furthermore, genistein (40 µM) significantly attenuated 5-HT-induced inositol phosphate production. We conclude that in airway smooth muscle contractile agonists acting on G protein-coupled receptors may activate tyrosine kinase(s), which in turn modulate calcium signaling by affecting, directly or indirectly, PLC-beta activity. It is unlikely that PLC-gamma or the mitogen-activated protein kinase pathway is involved in Ca2+ signaling to 5-HT.

cell culture; mitogen-activated protein kinase; phospholipase C


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