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Published online April 9, 2007
doi:10.1083/jcb.200606043
The Journal of Cell Biology, Vol. 177, No. 1, 163-172
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Wixler et al.
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Article

Deficiency in the LIM-only protein Fhl2 impairs skin wound healing



Viktor Wixler1, Stephanie Hirner3, Judith M. Müller4, Lucia Gullotti3, Carola Will1, Jutta Kirfel3, Thomas Günther4, Holm Schneider5, Anja Bosserhoff6, Hubert Schorle2, Jung Park7, Roland Schüle4, and Reinhard Buettner3

1 Institute of Molecular Virology, Münster University Hospital Medical School, D-48149 Münster, Germany
2 Department of Developmental Pathology, 3 Institute of Pathology, University Hospital Medical School, D-53127 Bonn, Germany
4 Center for Clinical Research, University of Freiburg, D-79106 Freiburg, Germany
5 Experimental Neonatology, Department of Pediatrics, Medical University of Innsbruck, Innrain 66, A-6020 Innsbruck, Austria
6 Institute of Pathology, University Hospital Regensburg, D-93042 Regensburg, Germany
7 Department of Experimental Medicine I, University of Erlangen-Nürnberg, D-91054 Erlangen, Germany

Correspondence to Reinhard Buettner: Reinhard.Buettner{at}ukb.uni-bonn.de

After skin wounding, the repair process is initiated by the release of growth factors, cytokines, and bioactive lipids from injured vessels and coagulated platelets. These signal molecules induce synthesis and deposition of a provisional extracellular matrix, as well as fibroblast invasion into and contraction of the wounded area. We previously showed that sphingosine-1-phosphate (S1P) triggers a signal transduction cascade mediating nuclear translocation of the LIM-only protein Fhl2 in response to activation of the RhoA GTPase (Muller, J.M., U. Isele, E. Metzger, A. Rempel, M. Moser, A. Pscherer, T. Breyer, C. Holubarsch, R. Buettner, and R. Schule. 2000. EMBO J. 19:359–369; Muller, J.M., E. Metzger, H. Greschik, A.K. Bosserhoff, L. Mercep, R. Buettner, and R. Schule. 2002. EMBO J. 21:736–748.). We demonstrate impaired cutaneous wound healing in Fhl2-deficient mice rescued by transgenic expression of Fhl2. Furthermore, collagen contraction and cell migration are severely impaired in Fhl2-deficient cells. Consequently, we show that the expression of {alpha}-smooth muscle actin, which is regulated by Fhl2, is reduced and delayed in wounds of Fhl2-deficient mice and that the expression of p130Cas, which is essential for cell migration, is reduced in Fhl2-deficient cells. In summary, our data demonstrate a function of Fhl2 as a lipid-triggered signaling molecule in mesenchymal cells regulating their migration and contraction during cutaneous wound healing.

V. Wixler, S. Hirner, J.M. Müller, and L. Gullotti contributed equally to this paper.

Abbreviations used in this paper: HEK, human embryonic kidney; S1P, sphingosine-1-phosphate; SMA, smooth muscle actin; SRF, serum response factor.


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