Extracellular mutations of protease-activated receptor-1 result in differential activation by thrombin and thrombin receptor agonist peptide.

The protease-activated thrombin receptor-1 (PAR-1) can be activated by both the tethered ligand exposed by thrombin cleavage and a synthetic peptide having the tethered ligand sequence (thrombin receptor agonist peptide or TRAP). We conducted a mutational analysis of extracellular residues of the receptor potentially involved in interaction with both the tethered ligand and the soluble peptide agonist. Agonist-stimulated calcium efflux in X.

Expression of protease-activated receptor-2 during embryonic development.

Protease-activated receptor-2 (PAR-2) is the second member of a novel family of G-protein-coupled receptors, activated through proteolytic cleavage within the extracellular domain to reveal a newly formed amino terminus that acts as a tethered ligand causing receptor activation. PAR-2 is expressed in a number of adult tissues, but its distribution during development has not been characterized. Knowledge of the tissue distribution of PAR-2 during development will provide clues as to its function(s) in vivo.

Ligand cross-reactivity within the protease-activated receptor family.

Recently, a second member of the protease-activated receptor (PAR) family, named PAR-2, has been identified. Similar to the thrombin receptor, PAR-2 appears to be activated by proteolytic-mediated exposure of a "tethered ligand" sequence and can also be activated by the corresponding synthetic peptides. Similarities in the amino acid sequence of the receptors' tethered ligand sequences suggest that their respective agonist peptides might not be absolutely specific for their particular receptors.

Characterization of recombinant human apoB-48-containing lipoproteins in rat hepatoma McA-RH7777 cells transfected with apoB-48 cDNA. Overexpression of apoB-48 decreases synthesis of endogenous apoB-100.

We studied the effect of overexpression of apolipoprotein (apo) B-48 on the synthesis and secretion of endogenous apoB-100 in rat hepatoma McA-RH7777 cell lines stably transfected with human apoB-48 cDNA under the control of the cytomegalovirus promoter. Three cell lines that secrete 40 to 60 ng human apoB.mg cell protein-1.

The anion-binding exosite is critical for the high affinity binding of thrombin to the human thrombin receptor.

The thrombin receptor has been shown to be a novel member of the family of G-protein coupled receptors (Vu, T.-K. H.