Vempati, Karagiannis, Popel, 2007

Model Status

This CellML model is known to run in both OpenCell and COR to recreate the results in the published paper. The units have been checked and they are consistent. Please note that many of the figures in the paper are complex and requite special simulation conditions. This particular CellML model represents the basic core model presented in the paper. Initial conditions can be modified to generate more complex results. We thank the model author Prakash Vempati for his assistance in getting this CellML model to run.

Model Structure

ABSTRACT: Matrix metalloproteinases (MMPs) are a class of extracellular and membrane-bound proteases involved in an array of physiological processes including angiogenesis. We present a detailed computational model of MMP9 activation and inhibition. Our model is validated to existing biochemical experimental data. We determine kinetic rate constants for the processes of MMP9 activation by MMP3, MMP10, MMP13, and trypsin, inhibition by the tissue inhibitors of metalloproteinases (TIMPs) TIMP1 and TIMP2, and MMP9 deactivation. This computational approach allows us to investigate discrepancies in our understanding of the MMP9

The original paper reference is cited below:

A Biochemical Model of Matrix Metalloproteinase 9 Activation and Inhibition, Prakash Vempati, Emmanouil D. Karagiannis, and Aleksander S. Popel , 2007, The Journal of Biological Chemistry , 282, 37585-37596. PubMed ID: 17848556

Schematic diagram of the biochemical reaction network for MMP9 activation and inhibition spanning MMP9, MMP3, TIMP1, and TIMP2. pM9, pro-MMP9; M3, MMP3; M9, MMP9; T1, TIMP1; T2, TIMP2; Tr, Trypsin.
Derived from workspace Vempati, Karagiannis, Popel, 2007 at changeset 17c90dc4e1b1.
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