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RECK Negatively Regulates Matrix Metalloproteinase-9 Transcription

¹ Antibiotics Laboratory and Chemical Biology Department, Advanced Science Institute, RIKEN and ² Graduate School of Science and Engineering, Saitama University, Saitama, Japan

Requests for reprints: Siro Simizu, Antibiotics Laboratory and Chemical Biology Department, Advanced Science Institute, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. Phone: 81-48-467-9541; Fax: 81-48-462-4669; E-mail: simizu{at}riken.jp.

Key Words: RECK • invasion • matrix metalloproteinase-9 • glycosylphosphatidylinositol-anchored protein • Fra-1

RECK, a glycosylphosphatidylinositol-anchored glycoprotein, inhibits the enzymatic activities of some matrix metalloproteinases (MMP), thereby suppressing tumor cell metastasis; however, the detailed mechanism is still obscure. In this study, we compared the gene expression profiles between mock- and RECK-transfected HT1080 cells and showed that RECK decreases MMP-9 mRNA levels but not other MMP mRNA levels. Moreover, treatment with RECK-specific siRNA increased MMP-9 mRNA in RECK-expressing cells. The promoter assay showed that MMP-9 promoter activity was suppressed by RECK and that RECK-mediated suppression of MMP-9 promoter activity requires 12-O-tetradecanoylphorbol-13-acetate–responsive element (TRE) and B sites. Moreover, the binding ability of Fra-1 and c-Jun to TRE within the MMP-9 promoter region was suppressed by RECK. Thus, these results show that RECK is a negative regulator of MMP-9 transcription. [Cancer Res 2009;69(4):1502–8]