| Literature DB >> 29253518 |
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.Entities:
Keywords: Biglycan; Decorin; Fibromodulin; Glycosylation; Lumican; MMP-14; SLRPs; Structure and molecular modeling
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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