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Originally published In Press as doi:10.1074/jbc.M104871200 on July 19, 2001

J. Biol. Chem., Vol. 276, Issue 38, 35818-35825, September 21, 2001
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The Ca2+-binding Proteins S100A8 and S100A9 Are Encoded by Novel Injury-regulated Genes*

Irmgard S. ThoreyDagger , Johannes Roth§, Johannes Regenbogen, Jörn-Peter Halle, Michaela Bittner, Thomas Vogl§, Susanne KaeslerDagger , Philippe BugnonDagger , Birgit Reitmaier, Silke DurkaDagger , Anja Graf, Mandy Wöckner, Norman Rieger||, Alexander Konstantinow**, Eckhard Wolf||, Andreas Goppelt, and Sabine WernerDagger Dagger Dagger

From the Dagger  Institute of Cell Biology, ETH Zürich, Hönggerberg, CH-8093 Zürich, Switzerland, § Institute of Experimental Dermatology, University of Münster, Von-Esmarch-Str. 56, D-48129 Münster,  SWITCH BIOTECH AG, Fraunhoferstr. 10, D-82152 Martinsried, || Institut für Molekulare Tierzucht und Biotechnologie der Ludwig-Maximilians-Universität München, Feodor-Lynen-Str. 25, D-81377 München, and ** Klinik für Dermatologie und Allergologie der Technischen Universität München am Biederstein, Biedersteiner Str. 29, D-80802 München, Germany

To gain insight into the molecular mechanisms underlying cutaneous wound repair, we performed a large scale screen to identify novel injury-regulated genes. Here we show a strong up-regulation of the RNA and protein levels of the two Ca2+-binding proteins S100A8 and S100A9 in the hyperthickened epidermis of acute murine and human wounds and of human ulcers. Furthermore, both genes were expressed by inflammatory cells in the wound. The increased expression of S100A8 and S100A9 in wound keratinocytes is most likely related to the activated state of the keratinocytes and not secondary to the inflammation of the skin, since we also found up-regulation of S100A8 and S100A9 in the epidermis of activin-overexpressing mice, which develop a hyperproliferative and abnormally differentiated epidermis in the absence of inflammation. Furthermore, S100A8 and S100A9 expression was found to be associated with partially differentiated keratinocytes in vitro. Using confocal microscopy, both proteins were shown to be at least partially associated with the keratin cytoskeleton. In addition, cultured keratinocytes efficiently secreted the S100A8/A9 dimer. These results together with previously published data suggest that S100A8 and S100A9 are novel players in wound repair, where they might be involved in the reorganization of the keratin cytoskeleton in the wounded epidermis, in the chemoattraction of inflammatory cells, and/or in the defense against microorganisms.

* This work was supported by a grant from the Bundesministerium für Bildung und Forschung (BMBF) (to S. W., A. G., and E. W.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Dagger To whom correspondence should be addressed: Institute of Cell Biology, HPM D42, ETH Zürich, Hönggerberg, CH-8093 Zürich, Switzerland. Tel.: 0041 1 6333941; Fax: 0041 1 6331174; E-mail: sabine.werner@cell.biol.ethz.ch.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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