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Table 1 Experimentally derived parameter values for the MMP model

From: Control and inhibition analysis of complex formation processes

Parameters

Values

Remarks

[MT 1] T

100nM

From Karagiannis 2004 [18]& Hoshino 2012 [16]

[T 2] T

50-100nM

From Karagiannis 2004 [18] & Hoshino 2012 [16]

[M 2] T

100nM

From Karagiannis 2004 [18] & Hoshino 2012 [16]

k a(MT 1−MT 1)

2/μM/s

From Hoshino 2012 [16]

k d(MT 1−MT 1)

0.01/s

From Hoshino 2012 [16]

k a(MT 1−T 2)

2.74/μM/s

From Toth 2000 [19]

k d(MT 1−T 2)

0.0001/s

From Toth 2000 [19]

k a(T 2−M 2)

0.14/μM/s

From Olson 1997 [20]

k d(T 2−M 2)

0.0047/s

From Olson 1997 [20]

  1. The parameters ka(MT 1−MT 1) and kd(MT 1−MT 1) are association and dissociation rate constants of the MT1-MMP dimer formation, respectively. The parameterska(MT 1−T 2) and kd(MT 1−T 2) are association and dissociation rate constants of the MT1-MMP and TIMP2 binding reaction, respectively. The parameters ka(T 2−M 2) and kd(T 2−M 2) are association and dissociation rate constants of the TIMP2 and MMP2 binding reaction, respectively.
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Theoretical Biology and Medical Modelling

ISSN: 1742-4682