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

Matrix Biol. 2019 Jan:75-76:271-285. doi: 10.1016/j.matbio.2017.12.006. Epub 2017 Dec 15.

Abstract

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.

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

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Catalytic Domain / genetics
  • Disease Progression
  • Extracellular Matrix / genetics
  • Extracellular Matrix / metabolism
  • Humans
  • Lumican / genetics*
  • Matrix Metalloproteinase 14 / genetics*
  • Matrix Metalloproteinase 14 / metabolism
  • Neoplasms / genetics*
  • Neoplasms / pathology
  • Signal Transduction / genetics
  • Small Leucine-Rich Proteoglycans / genetics*

Substances

  • LUM protein, human
  • Lumican
  • Small Leucine-Rich Proteoglycans
  • MMP14 protein, human
  • Matrix Metalloproteinase 14