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1 Department of Pharmacology, University of South Alabama College of Medicine, Mobile, Alabama 36688; and 2 Department of Internal Medicine, University of Iowa Health Sciences Center, Iowa City, Iowa 52242
The present study evaluated the necessity of store-operated Ca2+ entry in mediating thrombin-induced 20-kDa myosin light chain (MLC20) phosphorylation and increased permeability in bovine pulmonary artery endothelial cells (BPAECs). Thrombin (7 U/ml) and thapsigargin (1 µM) activated Ca2+ entry through a common pathway in confluent BPAECs. Similar increases in MLC20 phosphorylation were observed 5 min after thrombin and thapsigargin challenge, although thrombin produced a sustained increase in MLC20 phosphorylation that was not observed in response to thapsigargin. Neither agonist increased MLC20 phosphorylation when Ca2+ influx was inhibited. Thrombin and thapsigargin induced inter-endothelial cell gap formation and increased FITC-dextran (molecular radii 23 Å) transfer across confluent BPAEC monolayers. Activation of store-operated Ca2+ entry was required for thapsigargin and thrombin receptor-activating peptide to increase permeability, demonstrating that activation of store-operated Ca2+ entry is coupled with MLC20 phosphorylation and is associated with intercellular gap formation and increased barrier transport of macromolecules. Unlike thrombin receptor-activating peptide, thrombin increased permeability without activation of store-operated Ca2+ entry, suggesting that it partly disrupts the endothelial barrier through a proteolytic mechanism independent of Ca2+ signaling.
thapsigargin; thrombin; myosin light chain kinase; receptor-operated calcium channels; lung
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