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The membrane-anchored MMP inhibitor RECK is a key regulator of extracellular matrix integrity and angiogenesis.

Matrix metalloproteinases (MMPs) are essential for proper extracellular matrix remodeling. We previously found that a membrane-anchored glycoprotein, RECK, negatively regulates MMP-9 and inhibits tumor invasion and metastasis. Here we show that RECK regulates two other MMPs, MMP-2 and MT1-MMP, known to be involved in cancer progression, that mice lacking a functional RECK gene die around E10.5 with defects in collagen fibrils, the basal lamina, and vascular development, and that this phenotype is partially suppressed by MMP-2 null mutation. Also, vascular sprouting is dramatically suppressed in tumors derived from RECK-expressing fibrosarcoma cells grown in nude mice. These results support a role for RECK in the regulation of MMP-2 in vivo and implicate RECK downregulation in tumor angiogenesis.

Pubmed ID: 11747814

Authors

  • Oh J
  • Takahashi R
  • Kondo S
  • Mizoguchi A
  • Adachi E
  • Sasahara RM
  • Nishimura S
  • Imamura Y
  • Kitayama H
  • Alexander DB
  • Ide C
  • Horan TP
  • Arakawa T
  • Yoshida H
  • Nishikawa S
  • Itoh Y
  • Seiki M
  • Itohara S
  • Takahashi C
  • Noda M

Journal

Cell

Publication Data

December 14, 2001

Associated Grants

None

Mesh Terms

  • Animals
  • Cells, Cultured
  • Down-Regulation
  • Embryo, Mammalian
  • Extracellular Matrix
  • GPI-Linked Proteins
  • Gene Targeting
  • Humans
  • Immunohistochemistry
  • Matrix Metalloproteinase 14
  • Matrix Metalloproteinase 2
  • Matrix Metalloproteinase 9
  • Matrix Metalloproteinase Inhibitors
  • Matrix Metalloproteinases
  • Matrix Metalloproteinases, Membrane-Associated
  • Membrane Glycoproteins
  • Metalloendopeptidases
  • Mice
  • Mice, Nude
  • Muscle, Smooth, Vascular
  • Mutation
  • Neoplasm Transplantation
  • Neoplasms, Experimental
  • Neovascularization, Pathologic
  • Neovascularization, Physiologic
  • Transfection
  • Tumor Cells, Cultured