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Regulation of matrix metalloproteinase-9 and inhibition of tumor invasion by the membrane-anchored glycoprotein RECK

  • Chiaki Takahashi
  • Zeqi Sheng
  • Thomas P. Horan
  • Hitoshi Kitayama
  • Masatoshi Maki
  • Kiyotaka Hitomi
  • Yasuyuki Kitaura
  • Setsuo Takai
  • Regina M. Sasahara
  • Aki Horimoto
  • Yoji Ikawa
  • Barry J. Ratzkin
  • Tsutomu Arakawa
  • Makoto Noda
The National Academy of Sciences
Publication Date
Oct 27, 1998
  • Biology
  • Medicine


A human fibroblast cDNA expression library was screened for cDNA clones giving rise to flat colonies when transfected into v-Ki-ras-transformed NIH 3T3 cells. One such gene, RECK, encodes a membrane-anchored glycoprotein of about 110 kDa with multiple epidermal growth factor-like repeats and serine-protease inhibitor-like domains. While RECK mRNA is expressed in various human tissues and untransformed cells, it is undetectable in tumor-derived cell lines and oncogenically transformed cells. Restored expression of RECK in malignant cells resulted in suppression of invasive activity with concomitant decrease in the secretion of matrix metalloproteinase-9 (MMP-9), a key enzyme involved in tumor invasion and metastasis. Moreover, purified RECK protein was found to bind to, and inhibit the proteolytic activity of, MMP-9. Thus, RECK may link oncogenic signals to tumor invasion and metastasis.

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