The novel PAR2 ligand C391 blocks multiple PAR2 signalling pathways in vitro and in vivo.

ABSTRACT:

Background and purpose

Proteinase-activated receptor-2 (PAR2) is a GPCR linked to diverse pathologies, including acute and chronic pain. PAR2 is one of the four PARs that are activated by proteolytic cleavage of the extracellular amino terminus, resulting in an exposed, tethered peptide agonist. Several peptide and peptidomimetic agonists, with high potency and efficacy, have been developed to probe the functions of PAR2, in vitro and in vivo. However, few similarly potent and effective antagonists have been described.

Experimental approach

We modified the peptidomimetic PAR2 agonist, 2-furoyl-LIGRLO-NH₂ , to create a novel PAR2 peptidomimetic ligand, C391. C391 was evaluated for PAR2 agonist/antagonist activity to PAR2 across G_q signalling pathways usi

SUBMITTER: Boitano S 

PROVIDER: S-EPMC4562513 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature