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

• DOI: 10.1074/jbc.m609505200
• Publication Date: 2007-02-28T02:54:48Z
• Authors: Laurent Duca; Charlotte Blanche...; Benoît Cantarelli; Christelle Ghoneim; Stéphane Dedieu; Frédéric Delacoux; William Hornebeck; Aleksander Hinek; Laurent Martiny; Laurent Debelle
• Keywords: Mitogen-Activated Protein Kinase 1; 0303 health sciences; Mitogen-Activated Protein Kinase 3; MAP Kinase Signaling System; Neuraminidase; Lactose; Receptors, Cell Surface; Fibroblasts; Gene Expression Regulation, Enzymologic; N-Acetylneuraminic Acid; Elastin; Enzyme Activation; Protein Subunits; 03 medical and health sciences; Humans; Matrix Metalloproteinase 1; Peptides; Cells, Cultured

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