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Table 1 Binding of pro- or actMMP-2 or pro- or actMMP-9 to native collagens, single chains of CI, chain fragments and synthetic peptidesa

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

   Binding of [125I]-MMPs (% of maximum control)
   ActMMP-2 ActMMP-9 ProMMP-2 ProMMP-9
Wells coated with     
  CI 11.1 ± 1.8 3.1 ± 0.5 24.0 ± 5.6 30.9 ± 3.1
  CIII 14.3 ± 5.8 5.0 ± 0.4 40.0 ± 5.0 45.0 ± 2.0
  CVI 4.8 ± 0.6 2.4 ± 0.1 14.1 ± 1.8 12.3 ± 0.8
  α1(I) 19.0 ± 3.0 4.7 ± 0.3 36.0 ± 4.0 37.6 ± 0.9
  α2(I) 10.7 ± 1.8 2.6 ± 0.2 30.2 ± 2.3 21.8 ± 1.1
  α1CB3 7.4 ± 0.3 1.8 ± 0.2 13.2 ± 7.9 7.4 ± 1.2
  α1CB6 4.9 ± 1.5 2.4 ± 0.2 12.8 ± 2.6 19.3 ± 0.4
  α1CB7 6.8 ± 0.6 2.1 ± 0.3 18.2 ± 3.7 20.4 ± 1.3
  α1CB8 4.4 ± 1.7 2.8 ± 0.4 14.0 ± 4.5 31.6 ± 0.9
  (GPO)10 6.2 ± 3.1 5.4 ± 0.6 13.0 ± 3.5 36.1 ± 1.7
  (GPP)10 2.1 ± 0.7 0.9 ± 0.4 3.6 ± 2.0 4.9 ± 0.7
  GAP 1.5 ± 0.7 0.7 ± 0.2 1.7 ± 1.0 1.3 ± 0.2
  1. aProteins and peptides were immobilized to the wells of polystyrene microtiter plates before 2 ng/well [125I]-MMPs were added. Wells were washed thoroughly, and bound MMPs were determined as residual radioactivity. Binding efficiency was calculated in comparison to the amount of the respective radiolabeled MMPs initially added (100%). Results are mean values ± SD of at least five independent experiments performed in triplicate. activated form of MMP (actMMP); proMMPs, inactive latent proform of MMPs; MMP, matrix metalloproteinase; CI, collagen type I; α1(I), α1 chain of collagen type I (α1(I)); α1CB3, α1CB3, cyanogen bromide peptide 3 of the α1 chain of collagen type I;; GPO, Gly-Pro-Hyp triplets; GPP, Gly-Pro-Pro; GAP, Gly-Ala-Pro.