RECK, a novel matrix metalloproteinase regulator

Histol Histopathol. 2008 Aug;23(8):1003-10. doi: 10.14670/HH-23.1003.

Abstract

Extracellular matrix (ECM) macromolecules are important for creating the cellular environments required during development and morphogenesis of tissues. Matrix metalloproteinases (MMPs) are a family of Zn-dependent endopeptidases that collectively are capable of cleaving virtually all ECM substrates, and play an important role in some physiological and pathological processes. MMP activity can be inhibited by some natural and artificial inhibitors. A newly found membrane-anchored regulator of MMPs, the reversion-inducing-cysteine-rich protein with kazal motifs (RECK), is downregulated when the cells undergo a process of malignant transformation, and is currently the subject of considerable research activity because of its specific structure and function. In this review, we have chosen to concentrate our efforts on the structure, function, regulation, and future prospect of RECK in order to provide a new target for prevention and treatment of tumours.

Publication types

  • Review

MeSH terms

  • Cell Transformation, Neoplastic
  • Cells, Cultured
  • Down-Regulation
  • Extracellular Matrix / metabolism*
  • GPI-Linked Proteins
  • Gene Expression Regulation, Neoplastic
  • Humans
  • Matrix Metalloproteinase Inhibitors
  • Matrix Metalloproteinases / metabolism*
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / physiology*
  • Neoplasms / blood supply
  • Neoplasms / metabolism*
  • Neoplasms / therapy
  • Neovascularization, Pathologic
  • Tissue Inhibitor of Metalloproteinases / metabolism*

Substances

  • GPI-Linked Proteins
  • Matrix Metalloproteinase Inhibitors
  • Membrane Glycoproteins
  • RECK protein, human
  • Tissue Inhibitor of Metalloproteinases
  • Matrix Metalloproteinases