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Originally published as MBC in Press, 10.1091/mbc.E02-11-0729 on February 21, 2003

Vol. 14, Issue 6, 2508-2519, June 2003

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{alpha}-Smooth Muscle Actin Is Crucial for Focal Adhesion Maturation in Myofibroblasts

Boris Hinz * {dagger}, Vera Dugina {ddagger}, Christoph Ballestrem §, Bernhard Wehrle-Haller *, and Christine Chaponnier *

* Department of Pathology, Centre Medical Universitaire, University of Geneva, 1211 Geneva 4, Switzerland; {ddagger} Moscow State University, 119899 Moscow, Russia; and § Department of Molecular Cell Biology, The Weizmann Institute of Science, 76100 Rehovot, Israel

Submitted November 13, 2002; Revised December 23, 2002; Accepted February 5, 2003
Monitoring Editor: Paul T. Matsudaira

Cultured myofibroblasts are characterized by stress fibers, containing {alpha}-smooth muscle actin ({alpha}-SMA) and by supermature focal adhesions (FAs), which are larger than FAs of {alpha}-SMA–negative fibroblasts. We have investigated the role of {alpha}-SMA for myofibroblast adhesion and FA maturation. Inverted centrifugation reveals two phases of initial myofibroblast attachment: during the first 2 h of plating microfilament bundles contain essentially cytoplasmic actin and myofibroblast adhesion is similar to that of {alpha}-SMA–negative fibroblasts. Then, myofibroblasts incorporate {alpha}-SMA in stress fibers, develop mature FAs and their adhesion capacity is significantly increased. When {alpha}-SMA expression is induced in 5 d culture by TGF{beta} or low serum levels, fibroblast adhesion is further increased correlating with a "supermaturation" of FAs. Treatment of myofibroblasts with {alpha}-SMA fusion peptide (SMA-FP), which inhibits {alpha}-SMA–mediated contractile activity, reduces their adhesion to the level of {alpha}-SMA negative fibroblasts. With the use of flexible micropatterned substrates and EGFP-constructs we show that SMA-FP application leads to a decrease of myofibroblast contraction, shortly followed by disassembly of paxillin- and {beta}3 integrin-containing FAs; {alpha}5 integrin distribution is not affected. FRAP of {beta}3 integrin-EGFP demonstrates an increase of FA protein turnover following SMA-FP treatment. We conclude that the formation and stability of supermature FAs depends on a high {alpha}-SMA–mediated contractile activity of myofibroblast stress fibers.

Abbreviations used: {alpha}-SMA, {alpha}-smooth muscle actin; FA, focal adhesion; FN, fibronectin; FP, fusion peptide; LF, lung fibroblast; PFA, paraformaldehyde; SKA, skeletal actin; SM, smooth muscle; TGF{beta}-RII, TGF{beta} soluble receptor type II; Triton X-100, TX-100.

Online version of this article contains video material. Online version is available at www.molbiolcell.org.

{dagger} Corresponding author. E-mail address: boris.hinz{at}epfl.ch.




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