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J. Biol. Chem., Vol. 278, Issue 45, 44168-44177, November 7, 2003

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Normal Human Keratinocytes Bind to the 3LG4/5 Domain of Unprocessed Laminin-5 through the Receptor Syndecan-1^*

Osamu Okamoto, Sophie Bachy, Uwe Odenthal¶||, Janine Bernaud**, Dominique Rigal**, Hugues Lortat-Jacob, Neil Smyth¶||, and Patricia Rousselle

From the Institut de Biologie et Chimie des Protéines, Unité Mixte de Recherche 5086, Institut Fédératif de Recherche 128 BioSciences Lyon-Gerland, 7 passage du Vercors, 69367 Lyon, France, the ^¶Center for Biochemistry, Medical Faculty, Joseph-Stelzmann-Str.52, 50931 Cologne, Germany, the ^**Etablissement Français du Sang, 1 rue du Vercors, 69007 Lyon, France, and the Institut de Biologie Structurale, UMR 5075 Commissariat à l'Energie Atomique-CNRS-Université Joseph Fourier, 41 avenue Horowitz, 38027 Grenoble, France

Basal keratinocytes of the epidermis adhere to their underlying basement membrane through a specific interaction with laminin-5, which is composed by the association of 3, 3, and 2 chains. Laminin-5 has the ability to induce either stable cell adhesion or migration depending on specific processing of different parts of the molecule. One event results in the cleavage of the carboxyl-terminal globular domains 4 and 5 (LG4/5) of the 3 chain. In this study, we recombinantly expressed the human 3LG4/5 fragment in mammalian cells, and we show that this fragment induces adhesion of normal human keratinocytes and fibrosarcoma-derived HT1080 cells in a heparan- and chondroitin sulfate-dependent manner. Immunoprecipitation experiments with Na₂ ³⁵SO₄-labeled keratinocyte and HT1080 cell lysates as well as immunoblotting experiments revealed that the major proteoglycan receptor for the 3LG4/5 fragment is syndecan-1. Syndecan-4 from keratinocytes also bound to 3LG4/5. Furthermore we could show for the first time that unprocessed laminin-5 specifically binds syndecan-1, while processed laminin-5 does not. These results demonstrate that the LG4/5 modules within unprocessed laminin-5 permit its cell binding activity through heparan and chondroitin sulfate chains of syndecan-1 and reinforce previous data suggesting specific properties for the precursor molecule.

Received for publication, January 22, 2003 , and in revised form, August 25, 2003.

^* This work was supported by grants from the CNRS, the Association pour la Recherche sur le Cancer (Grant 5977 and Program ARECA), the Ligue Nationale contre le Cancer (Rhône-Alpes, Loire, Drôme), "Program Thématique Prioritaire" Grant 085113 from the Rhône-Alpes region, the Fondation Coloplast Pour la Qualité de la Vie, a Société de Recherche Dermatologique grant, and a Japanese Society for Investigative Dermatology International Fellowship Shiseido Award (to P. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Recipient of a poste rouge fellowship from CNRS European program Groupement de Recherche Européen "Intégrines et Transfert d'Informations" followed by a postdoctoral fellowship from the Fondation pour la Recherche Médicale. Present address: Dept. of Anatomy, Biology and Medicine, Oita Medical University, 1-1 Idaigaoka, Hasamamachi, Oita, 879-5593, Japan.

^|| Funded by Deutsche Forschungsgemeinschaft Grant SM 65/1-2.

To whom correspondence should be addressed: IBCP-UMR 5086, 7 passage du Vercors, 69367 Lyon Cedex 07, France. Tel.: 33-04-72-72-26-39; Fax: 33-04-72-72-26-02; E-mail: p.rousselle{at}ibcp.fr.

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