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Vol. 273, Issue 3, 1309-1315, January 16, 1998
From INSERM Unité 367, Physiologie et Pathologie
Expérimentale Vasculaires, 17, rue du Fer à Moulin,
75005 Paris, France
A human kidney bradykinin (BK)
B2 receptor cDNA was transfected in CHO-K1 cells
to establish cell lines that express stably and at high density a
receptor exhibiting B2 receptor properties in terms of
coupling to cell signaling effectors, desensitization, and
internalization. A cell line with a density of 1.3 × 106 receptors/cell allowed us to carry out a detailed study
of BK-receptor interaction over a wide range of BK concentrations. A
model assuming that BK binds to two receptor affinity states (depending
on guanine nucleotide-sensitive coupling) was not sufficient to account
for the kinetics of BK binding. Equilibrium kinetic analysis and
studies of the effects of receptor occupancy by agonists or antagonists on the kinetics of BK-receptor complex dissociation revealed features typical of negative cooperative binding. The negative cooperativity phenomenon was also observed in isolated membranes in both the presence
and absence of guanine nucleotide. Thus, following the interaction with
BK, B2 receptor molecules likely interact with each other,
resulting in an acceleration of bound ligand dissociation and a
decrease in the apparent affinity of the receptor for BK. This
phenomenon can participate in the desensitization process.
Negative Cooperativity in the Human Bradykinin B2
Receptor
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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