Analysis of proteinase-activated receptor 2 and TLR4 signal transduction: a novel paradigm for receptor cooperativity
Proteinase-activated receptor 2 (PAR 2), a seven-transmembrane G protein-coupled
receptor, is activated at inflammatory sites by proteolytic cleavage of its extracellular N
terminus by trypsin-like enzymes, exposing a tethered, receptor-activating ligand. Synthetic
agonist peptides (AP) that share the tethered ligand sequence also activate PAR 2, often
measured by Ca 2+ release. PAR 2 contributes to inflammation through activation of NF-κB-
regulated genes; however, the mechanism by which this occurs is unknown. Overexpression …
receptor, is activated at inflammatory sites by proteolytic cleavage of its extracellular N
terminus by trypsin-like enzymes, exposing a tethered, receptor-activating ligand. Synthetic
agonist peptides (AP) that share the tethered ligand sequence also activate PAR 2, often
measured by Ca 2+ release. PAR 2 contributes to inflammation through activation of NF-κB-
regulated genes; however, the mechanism by which this occurs is unknown. Overexpression …
