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• W2034757359 abstract "Both mechanotransduction and extracellular matrix (ECM) proteolytic remodeling are critical during embryonic development and in disease progression. Although mechanical stress is known to profoundly influence ECM remodeling, its effect on ECM degradation by matrix metalloproteinases (MMPs) is largely unexplored. We used a single-molecule magnetic tweezers assay to study the effect of force on collagen proteolysis by MMP-1. We show that the application of ∼10 pN in extensional force (far less than cell traction forces) causes a ∼100-fold increase in proteolysis rates. Our results support a mechanistic model in which the collagen triple helix unwinds prior to proteolysis. The data and resulting model predict that cell-generated traction forces may dramatically increase localized collagen proteolysis, suggesting that cells may use mechanical force to regulate proteolytic ECM remodeling." @default.
• W2034757359 created "2016-06-24" @default.
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• W2034757359 creator A5043484477 @default.
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• W2034757359 date "2011-02-01" @default.
• W2034757359 modified "2023-09-28" @default.
• W2034757359 title "Mechanical Load Induces a 100-Fold Increase in the Rate of Collagen Proteolysis by MMP-1" @default.
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• W2034757359 doi "https://doi.org/10.1016/j.bpj.2010.12.3006" @default.
• W2034757359 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3320677" @default.
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