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

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

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Free article
Review

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

Katarzyna Pietraszek-Gremplewicz et al. Matrix Biol. 2019 Jan.
Free article

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.

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