[HTML][HTML] Functional selectivity of G protein signaling by agonist peptides and thrombin for the protease-activated receptor-1
JN McLaughlin, L Shen, M Holinstat, JD Brooks… - Journal of biological …, 2005 - ASBMB
Thrombin activates protease-activated receptor-1 (PAR-1) by cleavage of the amino
terminus to unmask a tethered ligand. Although peptide analogs can activate PAR-1, we
show that the functional responses mediated via PAR-1 differ between the agonists.
Thrombin caused endothelial monolayer permeability and mobilized intracellular calcium
with EC 50 values of 0.1 and 1.7 nm, respectively. The opposite order of activation was
observed for agonist peptide (SFLLRN-CONH 2 or TFLLRNKPDK) activation. The addition …
terminus to unmask a tethered ligand. Although peptide analogs can activate PAR-1, we
show that the functional responses mediated via PAR-1 differ between the agonists.
Thrombin caused endothelial monolayer permeability and mobilized intracellular calcium
with EC 50 values of 0.1 and 1.7 nm, respectively. The opposite order of activation was
observed for agonist peptide (SFLLRN-CONH 2 or TFLLRNKPDK) activation. The addition …