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J. Biol. Chem., Vol. 278, Issue 38, 36537-36546, September 19, 2003

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Matrix Metalloproteinase-9 Silencing by RNA Interference Triggers the Migratory-adhesive Switch in Ewing's Sarcoma Cells^*

Josiane Sancéau , Sandrine Truchet  and Brigitte Bauvois  ¶

From the Unité 365 INSERM, Institut Curie, 75248 Paris cedex 05, France and USM503 MNHN, UMR 8646 CNRS-MNHN, U565 INSERM, Muséum National d'Histoire Naturelle, 75005 Paris, France

Enhanced expression of (pro)matrix metalloproteinase-9 (MMP-9) is associated with human tumor invasion and/or metastasis. COH cells derived from a highly invasive and metastatic Ewing's sarcoma constitutively express proMMP-9. Transfection of a double stranded RNA that targets the MMP-9 mRNA into COH cells depleted the corresponding mRNA and protein as demonstrated by reverse transcriptase-PCR, enzyme-linked immunosorbent assay, and gelatin zymography. proMMP-9 extinction resulted in the following: (i) decreased spreading on extracellular matrix (fibronectin, laminin, collagen IV)-coated surfaces, (ii) inhibition of migration toward fibronectin, and (iii) induced aggregation, which was specifically disrupted by a function-blocking E-cadherin antibody. MMP-9 knockdown concomitantly resulted in increased levels of surface E-cadherin, redistribution at the plasma membrane of -catenin, and its physical association with E-cadherin. Moreover, induction of E-cadherin-mediated adhesion was associated with RhoA activation and changes in paxillin cytoskeleton. Finally, an inhibitor of gelatinolytic activity of pro-MMP9 did not reduce COH cell migration confirming that the enzymatic property of COH MMP-9 was not required for migration toward fibronectin. Overall, our observations define a novel critical role for proMMP-9 in providing a cellular switch between stationary and migratory cell phases.

Received for publication, April 24, 2003 , and in revised form, June 12, 2003.

^* This work was supported by grants from INSERM. 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.

^¶ To whom correspondence should be addressed: Unité 365 INSERM, Institut Curie, 26, rue d'Ulm, 75248 Paris cedex 05, France. Tel.: 33-1-42-34-67-20; Fax: 33-1-44-07-07-85; E-mail: bbauvois{at}curie.fr.

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