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Am J Physiol Lung Cell Mol Physiol 282: L1305-L1313, 2002. First published January 4, 2002; doi:10.1152/ajplung.00304.2001
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Vol. 282, Issue 6, L1305-L1313, June 2002

Src modulates serotonin-induced calcium signaling by regulating phosphatidylinositol 4,5-bisphosphate

Barbara Tolloczko, Petra Turkewitsch, Sofia Choudry, Sandra Bisotto, Elizabeth D. Fixman, and James G. Martin

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

We tested the hypothesis that, in airway smooth muscle cells, stimulation of G-protein-coupled receptors by contractile agonists activates Src kinase and that this kinase modulates cell contractility and Ca2+ signaling by affecting the levels of the phospholipase C substrate phosphatidylinositol 4,5-bisphosphate (PIP2). Stimulation of cultured rat tracheal smooth muscle cells with serotonin (5-HT) induced an increase in Src activity, Ca2+ mobilization, and contraction (decrease in cell area). 5-HT-evoked cell contraction was reduced by a specific inhibitor of Src family kinases, 4-amino-5(4-methylphenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine (PP1). Peak Ca2+ responses to 5-HT were attenuated by PP1 and an anti-Src-blocking antibody and augmented by expression of constitutively activated Y529F Src. Sustained phases of Ca2+ responses to 5-HT and Ca2+ influx resulting from emptying of Ca2+ stores in the endoplasmic reticulum by thapsigargin were also decreased after PP1 treatment. PP1 significantly reduced the turnover of inositol phosphates produced on 5-HT stimulation and the amount of PIP2 in the Triton X-100-insoluble lipid fraction. Overall, these data demonstrate that, in rat tracheal smooth muscle cells, Src kinase modulates 5-HT-evoked cell contractility and Ca2+ signaling by regulating PIP2 levels and Ca2+ influx.

phospholipase C; smooth muscle contraction; phosphoinositides


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