Document Detail


Thrombin-induced contraction in alveolar epithelial cells probed by traction microscopy.
MedLine Citation:
PMID:  16675616     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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 microM, 30 min) and inhibition of myosin light chain kinase with ML-7 (10 microM, 30 min) and Rho kinase with Y-27632 (10 microM, 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 actomyosin activation through myosin light chain kinase and Rho kinase signaling pathways. Thrombin-induced contractile tension might further impair alveolar epithelial barrier integrity in the injured lung.
Authors:
Núria Gavara; Raimon Sunyer; Pere Roca-Cusachs; Ramon Farré; Mar Rotger; Daniel Navajas
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-05-04
Journal Detail:
Title:  Journal of applied physiology (Bethesda, Md. : 1985)     Volume:  101     ISSN:  8750-7587     ISO Abbreviation:  J. Appl. Physiol.     Publication Date:  2006 Aug 
Date Detail:
Created Date:  2006-07-19     Completed Date:  2006-09-12     Revised Date:  2013-09-26    
Medline Journal Info:
Nlm Unique ID:  8502536     Medline TA:  J Appl Physiol (1985)     Country:  United States    
Other Details:
Languages:  eng     Pagination:  512-20     Citation Subset:  IM    
Affiliation:
Unitat de Biofísica i Bioenginyeria, Facultat de Medicina-Universitat de Barcelona, Casanova 143, 08036 Barcelona, Spain.
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MeSH Terms
Descriptor/Qualifier:
Actins / drug effects,  physiology,  ultrastructure
Amides / pharmacology
Azepines / pharmacology
Cell Adhesion / physiology*
Cell Line
Cytochalasin D / pharmacology
Cytoskeleton / drug effects,  physiology,  ultrastructure
Humans
Intracellular Signaling Peptides and Proteins
Microscopy, Fluorescence / methods
Myosin-Light-Chain Kinase / antagonists & inhibitors,  physiology
Naphthalenes / pharmacology
Permeability
Protein-Serine-Threonine Kinases / antagonists & inhibitors,  physiology
Pulmonary Alveoli / cytology*
Pyridines / pharmacology
Respiratory Mucosa / cytology*,  physiology*
Signal Transduction / physiology
Thrombin / physiology*
Time Factors
rho-Associated Kinases
Chemical
Reg. No./Substance:
0/Actins; 0/Amides; 0/Azepines; 0/Intracellular Signaling Peptides and Proteins; 0/Naphthalenes; 0/Pyridines; 109376-83-2/ML 7; 138381-45-0/Y 27632; 22144-77-0/Cytochalasin D; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.1/rho-Associated Kinases; EC 2.7.11.18/Myosin-Light-Chain Kinase; EC 3.4.21.5/Thrombin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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