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Depending on their interaction with intracellular proteins, G protein-coupled receptors (GPCR) often display different affinities for agonists at 37°C. Determining the affinity at that temperature is often difficult in intact cells as most GPCRs are internalized after activation. When sequestration of the B 2  bradykinin receptor (B 2 R) was inhibited by either 0.5 M sucrose or phenylarsine oxide (PAO), a shift in the affinity was detected when the incubation temperature was raised from 4°C to 37°C or lowered from 37°C to 4°C. In contrast, binding of the antagonist [ 3 H]NPC 17731 was temperature-independent. B 2 R mutants displayed different affinity shifts allowing conclusions on the role of the involved amino acids. By inhibiting receptor sequestration it was possible to determine also dissociation of [ 3 H]BK and of [ 3 H]NPC 17731 from intact cells at 37°C. Surprisingly, both dissociation rates were markedly enhanced by the addition of unlabeled ligand, most likely via prevention of reassociation of dissociated [ 3 H]ligand. This suggests that dissociated [ 3 H]ligand cannot move freely away from the receptor.

biological chemistry

Inhibition of sequestration of human B 2  bradykinin receptor by phenylarsine oxide or sucrose allows determination of a receptor affinity shift and ligand dissociation in intact cells