Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 133, Issue 6, Pages 1686-1689Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja109972p
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Funding
- Burroughs Wellcome Career Award at the Scientific Interface
- National Institutes of Health [1-DP2-OD007078]
- William Bowes Jr. Stanford Graduate Fellowship
- Stanford Cardiovascular Institute
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Although mechanical stress is known to profoundly influence the composition and structure of the extracellular matrix (ECM), the mechanisms by which this regulation occurs remain poorly understood. We used a single-molecule magnetic tweezers assay to study the effect of force on collagen proteolysis by matrix metalloproteinase-1 (MMP-1). Here we show that the application of similar to 10 pN in extensional force causes an similar to 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 biologically relevant forces may increase localized ECM proteolysis, suggesting a possible role for mechanical force in the regulation of ECM remodeling.
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