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Vol. 15, Issue 9, 4310-4320, September 2004
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* Laboratory of Cell Biophysics, Swiss Federal Institute of Technology, 1015 Lausanne, Switzerland;
Department of Pathology and Immunology, Centre Medical Universitaire, University of Geneva, 1211 Geneva 4, Switzerland
Submitted May 11, 2004;
Revised June 25, 2004;
Accepted June 29, 2004
Monitoring Editor: Paul Matsudaira
Myofibroblasts of wound granulation tissue, in contrast to dermal fibroblasts, join stress fibers at sites of cadherin-type intercellular adherens junctions (AJs). However, the function of myofibroblast AJs, their molecular composition, and the mechanisms of their formation are largely unknown. We demonstrate that fibroblasts change cadherin expression from N-cadherin in early wounds to OB-cadherin in contractile wounds, populated with 
-smooth muscle actin (-SMA)-positive myofibroblasts. A similar shift occurs during myofibroblast differentiation in culture and seems to be responsible for the homotypic segregation of -SMA-positive and -negative fibroblasts in suspension. AJs of plated myofibroblasts are reinforced by -SMA–mediated contractile activity, resulting in high mechanical resistance as demonstrated by subjecting cell pairs to hydrodynamic forces in a flow chamber. A peptide that inhibits -SMA–mediated contractile force causes the reorganization of large stripe-like AJs to belt-like contacts as shown for enhanced green fluorescent protein-–catenin-transfected cells and is associated with a reduced mechanical resistance. Anti-OB-cadherin but not anti-N-cadherin peptides reduce the contraction of myofibroblast-populated collagen gels, suggesting that AJs are instrumental for myofibroblast contractile activity.
Abbreviations used: AJ, adherens junction; -SMA, -smooth muscle actin; EMT, epithelial-to-mesenchymal transition; FA, focal adhesion; FP, fusion peptide; LF, lung fibroblast; LPA, lysophosphatic acid; PFA, paraformaldehyde; SCF, subcutaneous fibroblast; SKA, skeletal actin; SMC, smooth muscle cell; TGF
, transforming growth factor-; TGF-sRII, recombinant soluble TGF receptor type II; TX-100, Triton X-100.
Online version of this article contains supporting material. On-line version is available at www.molbiolcell.org.
Corresponding author. E-mail address: boris.hinz{at}epfl.ch.
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