Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1

J Am Chem Soc. 2011 Feb 16;133(6):1686-9. doi: 10.1021/ja109972p. Epub 2011 Jan 19.

Abstract

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 ∼10 pN in extensional force causes an ∼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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Collagen / chemistry
  • Collagen / metabolism*
  • Kinetics
  • Matrix Metalloproteinase 1 / metabolism*
  • Mechanical Phenomena*
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Protein Multimerization
  • Protein Structure, Quaternary
  • Proteolysis*

Substances

  • Peptide Fragments
  • Collagen
  • Matrix Metalloproteinase 1