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J. Biol. Chem., Vol. 282, Issue 17, 12484-12491, April 27, 2007

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The Elastin Receptor Complex Transduces Signals through the Catalytic Activity of Its Neu-1 Subunit^*

Laurent Duca, Charlotte Blanchevoye, Benoît Cantarelli, Christelle Ghoneim, Stéphane Dedieu, Frédéric Delacoux, William Hornebeck, Aleksander Hinek, Laurent Martiny, and Laurent Debelle¹

From the Laboratoire de Biochimie, UMR CNRS 6198, Faculté des Sciences, Moulin de la Housse, BP 1039, 51687 Reims Cedex 2, France and the Cardiovascular Research Program, The Hospital for Sick Children, Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario M5G 1X8, Canada

The binding of elastin peptides on the elastin receptor complex leads to the formation of intracellular signals but how this is achieved remains totally unknown. Using pharmacological inhibitors of the enzymatic activities of its subunits, we show here that the elastin peptide-driven ERK1/2 activation and subsequent pro-MMP-1 production, observed in skin fibroblasts when they are cultured in the presence of these peptides, rely on a membrane-bound sialidase activity. As lactose blocked this effect, the elastin receptor sialidase subunit, Neu-1, seemed to be involved. The use of a catalytically inactive form of Neu-1 and the small interfering RNA-mediated decrease of Neu-1 expression strongly support this view. Finally, we report that N-acetyl neuraminic acid can reproduce the effects of elastin peptides on both ERK1/2 activation and pro-MMP-1 production. Altogether, our results indicate that the enzymatic activity of the Neu-1 subunit of the elastin receptor complex is responsible for its signal transduction, presumably through sialic acid generation from undetermined substrates.

Received for publication, October 10, 2006 , and in revised form, February 27, 2007.

^* This work was supported in part by grants from the Ligue contre le Cancer (ComitéDépartemental de l'Aube), Fond National pour la Santé ACI 2004 (Cancéropôle Grand-Est Project), and CNRS. 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.

¹ To whom correspondence should be addressed: Laboratoire de Biochimie, UMR CNRS 6198, IFR 53 Biomolécules, Faculté des Sciences, Moulin de la Housse, BP 1039, 51687 Reims Cedex 2, France. Tel.: 33-326-91-34-35; Fax: 33-326-91-83-66; E-Mail: laurent.debelle{at}univ-reims.fr.

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