Complex Regulation of the Pericellular Proteolytic Microenvironment during Tumor Progression and Wound Repair: Functional Interactions between the Serine Protease and Matrix Metalloproteinase Cascades

<table>The plasmin/MMP axis in pericellular proteolytic control. uPA, tethered to its receptor (uPAR), converts plasminogen receptor- (PlgR-) bound plasminogen to the broad-spectrum protease plasmin that, in turn, activates several MMP family members. Collectively, plasmin and MMPs regulate the extent, duration, and locale of stromal remodeling.</table>

Biochemistry Research International

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Figure 1

Figure 1: Complex Regulation of the Pericellular Proteolytic Microenvironment during Tumor Progression and Wound Repair: Functional Interactions between the Serine Protease and Matrix Metalloproteinase Cascades 

Figure 1 | Complex Regulation of the Pericellular Proteolytic Microenvironment during Tumor Progression and Wound Repair: Functional Interactions between the Serine Protease and Matrix Metalloproteinase Cascades 