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

Table 3 Effect of thermostability and Hyp content of collagen analogs on the binding kinetics of pro- or actMMP-2 to CI^a

	K_dfor binding to CI (in nM) in the presence of 10-fold molar excess
	-	(GPP)₁₀	(POG)₅	(GPO)₁₀
ProMMP-2	7.1 ± 0.1	42.1 ± 39.1	155.5 ± 40.3	155.5 ± 50.2
ActMMP-2	250.0 ± 30.0	n.d.	n.d.	2,710.0 ± 90.0

^aPro- or actMMP-2 (100 nM) was passed over collagen type I (CI) immobilized to a sensor chip in the presence or absence of 10-fold molar excesses of (GPP)₁₀, (POG)₅, or (GPO)₁₀. Reagents were dissolved in matrix metalloproteinase (MMP) activity buffer, and MMP-2 activity was specifically blocked by 1 μM Ro 28-2653. K_d values of MMP-2 binding to CI were determined by surface plasmon resonance (SPR) analysis and are shown as mean values ± SD from at least three experiments. Hyp, hydroxyproline; GPP, Gly-Pro-Pro; GPO, Gly-Pro-Hyp triplets; n.d., not determined.

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