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. Author manuscript; available in PMC: 2020 Oct 15.
Published in final edited form as: Cell Mol Bioeng. 2014 Jul 6;7(3):446–459. doi: 10.1007/s12195-014-0344-9

TABLE 3.

List of parameter values.

Parameter Description Value (h−1) Source
k1f Rate of β1 integrin adhesion and activation 23 Estimated from Ref. 49
k1r Rate of β1 integrin deactivation 0.567 Estimated from Ref. 49
k2f Rate of β3 integrin adhesion and activation 23 Estimated from Ref. 49
k2f Rate of β3 integrin deactivation 0.567 Estimated from Ref. 49
k3f Rate of TGF-β1 ligand attachment to TBR2 receptor 60 Ref. 44
k3r Rate of TGF-β1 disassociation 15 Estimated from Ref. 44
kIpF Rate of β1 integrin activation of FAK 0.454 Estimated from Refs. 13,49
kIpS Rate of β3 integrin activation of Src 20.15 Estimated from Refs. 1,49
kTpS Rate of TGFβ receptor activation of Src 120 Estimated from Refs. 14,15,21
kSpF Rate of Src association with FAK and activation of secondary phosphorylation sites 29 Estimated from Refs. 7,41,49
KmSF Michaelis–Menten constant for Src activation of FAK 0.1 Estimated from Ref. 7
kFAKpE Rate of FAK activation of ERK 48 Estimated from Refs. 46,49
kFGFpFAK Rate of FGF activation of FAK [2.2–8.4] Estimated from Refs. 17,29 and optimized
kFGFpERK* Rate of FGF activation of ERK [5.5–16.6] Estimated from Refs. 17,29 and optimized
kSpT Rate of Src phosphorylation of TBR2 40 Estimated from Refs. 14,15
KmST Michaelis–Menten constant for Src activation of TBR2 0.1 Estimated from Refs. 14,15
kSpP Rate of Src phosphorylation of p38 10 Estimated from Refs. 7,41,49
kTpP* Rate of TGF-β1 activation of pp38 [13.3–371] Estimated from Refs. 14,15
kIpP* Rate of β1 integrin activation of p38 5 Estimated from Refs. 24,33
kPr Rate of p38 dephosphorylation 580 Ref. 30
kEr Rate of ERK dephosphorylation 210 Estimated from Ref. 49
kSr Rate of Src dephosphorylation 432 Estimated from Ref. 49
kFr Rate of FAK dephosphorylation 48 Estimated from Ref. 49
kTr Rate of ligand induced TBR2 deactivation 15 Ref. 44
kE Intrinsic rate of ERK activation 2 Estimated and optimized
kαSMAf* Rate of p38 promotion of αSMA 0.5 Estimated and optimized for each model
kαSMAr Rate of αSMA degradation 0.515 Estimated from Ref. 20

Initial estimates of values were calculated from literature and varied to find the optimal parameter set.

Parameters that were optimized to calibration data set indicated by *.