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Tumor cell growth and migration begin with the secretion of proteolytic enzymes that degrade the extracellular matrix (ECM) followed by an invasion of the tumor vasculature leading to initiation of metastasis. Matrix Metalloproteases (MMPs) and their endogenous inhibitors (TIMPs) are key components of extracellular proteolysis and regulators of the tumor microenvironment (TME). Identification of ways to inhibit early matrix proteolysis would enhance our ability to target early tumor development and prevent metastatic potential. Studies have suggested that MMP/TIMP balance is shifted towards MMP activation during cancer progression.
Our laboratory investigates molecular mechanisms of MMPs and TIMPs regulation in the extracellular space that impact homeostasis and cancer progression. Current research includes: (1) Post-translational regulation of TIMP-2 with focus on tyrosine phosphorylation, (2) Identification of novel TIMP-2 extracellular protein interactions involved in tumor cell migration and invasion, (3) Targeting extracellular signaling for the development of novel cancer therapeutics.