Journal of Applied Physiology
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J Appl Physiol (May 4, 2006). doi:10.1152/japplphysiol.00185.2006
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Submitted on February 13, 2006
Accepted on April 24, 2006

Thrombin-induced contraction in alveolar epithelial cells probed by traction microscopy

Nuria Gavara1, Raimon Sunyer1, Pere Roca-Cusachs1, Ramon Farre1, Mar Rotger1, and Daniel Navajas1*

1 Universitat de Barcelona, Unitat de Biofisica i Bioenginyeria - Facultat de Medicina, Barcelona, Barcelona, Spain

* To whom correspondence should be addressed. E-mail: dnavajas{at}ub.edu.

Contractile tension of alveolar epithelial cells plays a major role in the force balance that regulates the structural integrity of the alveolar barrier. The aim of this work was to study thrombin-induced contractile forces of alveolar epithelial cells. A549 alveolar epithelial cells were challenged with thrombin and time course of contractile forces was measured by traction microscopy. The cells exhibited basal contraction with total force magnitude 55.0 ± 12.0 nN (mean ± SE, n = 12). Traction forces were exerted predominantly at the cell periphery and pointed to the cell center. Thrombin (1 U/ml) induced a fast and sustained 2.5-fold increase in traction forces which maintained peripheral and centripetal distribution. Actin fluorescent staining revealed F-actin polymerization and enhancement of peripheral actin rim. Disruption of actin cytoskeleton with cytochalasin D (5 µM, 30 min) and inhibition of myosin light chain kinase (MLCK) with ML-7 (10 µM, 30 min) and Rho kinase with Y-27632 (10 µM, 30 min) markedly depressed basal contractile tone and abolished thrombin-induced cell contraction. Therefore, the contractile response of alveolar epithelial cells to the inflammatory agonist thrombin was mediated by actin cytoskeleton remodeling and acto-myosin activation through MLCK and Rho kinase signaling pathways. Thrombin-induced contractile tension might further impair alveolar epithelial barrier integrity in the injured lung.




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