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Protease-activated receptors (PARs) transmit and amplify important inflammatory signals under situations of injury or infection. However, these signals can also promote pathological conditions in certain disease states. We have discovered that a new class of drugs acting at PAR1 can redirect this signal to give protective, ANTI-inflammatory responses.

Modulators of protease-activated receptors (PARs)

Protease-activated receptors (PARs) are a unique family of G protein-coupled receptors (GPCRs) that are activated by the cleavage of their N-terminal ends by proteases such as thrombin and trypsin. They play critical roles in platelet activation and clot formation, immune response, inflammation, and potentially cell proliferation and migration. 

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Work from the lab of SAB member Dr. Robert Flaumenhaft and the founder's lab (Dr. Chris Dockendorff) led to the identification of small molecules that can selectively inhibit and activate specific signaling pathways governed by the receptor PAR1. This can result in the inhibition of platelet activation (and resulting thrombus formation), but additionally it leads to the inhibition of inflammatory responses in several cell types, particularly the endothelial cells that comprise the barrier of blood vessels. These molecules, called parmodulins, can also promote protective effects in response to inflammatory signals involving the enzyme thrombin (“thromboinflammation”), making them promising for the treatment of numerous conditions including sepsis and kidney disease (see "Projects" section).

Collaborating Labs and Consultants

Building upon several long-term academic collaborations, Function Therapeutics has partnered with a diverse group of world leaders in chemistry, biology, and medicine. All are dedicated to the study of PAR ligands for the treatment of diseases for which therapies are urgently needed.

Publications & Presentations

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Photo Credit: Dan Johnson

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