4.6 Article

Small leucine-rich proteoglycans and matrix metalloproteinase-14: Key partners?

Journal

MATRIX BIOLOGY
Volume 75-76, Issue -, Pages 271-285

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.matbio.2017.12.006

Keywords

SLRPs; Lumican; Fibromodulin; Decorin; Biglycan; MMP-14; Structure and molecular modeling; Glycosylation

Funding

  1. CNRS
  2. Universite de Reims-Champagne-Ardenne
  3. Ligue Nationale Contre le Cancer
  4. Conference de Coordination Inter Regionale du Grand Est (CCIR-GE) [30036506-UMR7369]
  5. Ligue contre le Cancer (CCIR-GE) [30036506-UMR7369]
  6. Multiscale Molecular Modeling Platform
  7. Eiffel Scholarship of Excellence [870731F]
  8. EU H2020 project GLYCANC [645756]

Ask authors/readers for more resources

Small leucine-rich proteoglycans (SLRPs) are important regulators of extracellular matrix assembly and cell signaling. They are a family of proteoglycans that are present in extracellular matrix and that share in common multiple repeats of a leucine-rich structural motif. SLRPs have been identified as inhibitors of cancer progression by affecting MMPs, especially MMP-14 activity. Lumican, a member of the SLRPs family, and its derived peptides were shown to possess anti-tumor activity. Interestingly, it was demonstrated recently that lumican interacts directly with the catalytic domain of MMP-14 and inhibits its activity. The aim of this review was to summarize the interactions between SLRPs and MMPs with a special interest to lumican. (C) 2018 The Authors. Published by Elsevier Ltd.

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