Small leucine-rich proteoglycans and matrix metalloproteinase-14: Key partners?
Fiche publication
Date publication
décembre 2017
Journal
Matrix biology : journal of the International Society for Matrix Biology
Auteurs
Membres identifiés du Cancéropôle Est :
Dr BREZILLON Stéphane, Pr DAUCHEZ Manuel, Pr BAUD Stéphanie
Tous les auteurs :
Pietraszek-Gremplewicz K, Karamanou K, Niang A, Dauchez M, Belloy N, Maquart FX, Baud S, Brézillon S
Lien Pubmed
Résumé
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.
Mots clés
Biglycan, Decorin, Fibromodulin, Glycosylation, Lumican, MMP-14, SLRPs, Structure and molecular modeling
Référence
Matrix Biol.. 2017 Dec 15;: