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Table 2 Effect of soluble (GPO)10 on the binding of pro- or actMMP-2 or pro- or actMMP-9 to CIa

From: Hydroxyproline-containing collagen analogs trigger the release and activation of collagen-sequestered proMMP-2 by competition with prodomain-derived peptide P33-42

   Binding to CI
   Without (GPO)10 10× (GPO)10
   Off rate (s-1) K d (μM) Off rate (s-1) K d (μM)
MMP-2 Pro 0.48 0.07 ± 0.03 0.37 0.10 ± 0.04
  Act 0.48 0.17 ± 0.05 0.56 0.21 ± 0.15
MMP-9 Pro 0.32 0.12 ± 0.09 0.22 1.22 ± 0.64
  Act 0.76 0.87 ± 0.39 0.61 1.79 ± 1.81
  1. aMatrix metalloproteinases (MMPs) (100 nM) were passed over collagen type I (CI) immobilized to a sensor chip in the presence or absence of a 10-fold molar excess of Gly-Pro-Hyp triplets (GPO)10. MMP self-activation and activity were prevented by a buffer system consisting of phosphate-buffered saline and 0.05% (vol/vol) Tween 20. K d values and off rates of MMP binding to CI were determined by surface plasmon resonance (SPR) analysis and are shown as mean values ± SD from at least three experiments.