Literature DB >> 29253518

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

Katarzyna Pietraszek-Gremplewicz1, Konstantina Karamanou2, Aïchata Niang3, Manuel Dauchez3, Nicolas Belloy3, François-Xavier Maquart4, Stéphanie Baud3, Stéphane Brézillon5.   

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.
Copyright © 2018. Published by Elsevier B.V.

Entities:  

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

Mesh:

Substances:

Year:  2017        PMID: 29253518     DOI: 10.1016/j.matbio.2017.12.006

Source DB:  PubMed          Journal:  Matrix Biol        ISSN: 0945-053X            Impact factor:   11.583


  21 in total

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