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J Biol Chem, Vol. 273, Issue 5, 2617-2623, January 30, 1998
From The Johns Hopkins University School of Medicine, To determine the role of the cytoplasmic carboxyl
termini of human B1 and B2 kinin receptors (B1KR and B2KR,
respectively) in the internalization of their respective ligands,
des-Arg10-kallidin and bradykinin (BK), both wild
type receptors, as well as truncated B2KRs, a mutated B2KR, and
chimeric receptors were stably expressed in Chinese hamster ovary
cells. Incubation of [3H]BK at 37 °C with cells
expressing wild type B2KR resulted in pronounced and rapid ligand
internalization (~80% after 10 min). By contrast, incubation of
3H-labeled des-Arg10-kallidin with cells
expressing B1KR resulted in a modest, slow internalization of the
ligand (<20% after 10 min). Replacement, from Cys324, of
the cytoplasmic carboxyl terminus of the B2KR with that of the B1KR
from Cys330 (both Cys residues are putative palmitoylation
sites) greatly reduced ligand internalization (~40% after 10 min)
without significantly altering Kd or ligand-induced
signal activation. By marked contrast, the corresponding replacement,
of the sequence from Cys330 of the cytoplasmic carboxyl
terminus of the B1KR with the segment of the B2KR, led to a striking
increase of ligand internalization (~75% within 10 min) without
altering Kd or ligand-induced signal activation.
Truncation of the B2KR to within three amino acids of
Cys324 (truncation at Gly327) led to strongly
reduced ligand internalization (~40% after 10 min). Truncation of
the B2KR up to Lys315 almost completely abolished
internalization of [3H]BK (10% after 10 min). This
additional reduction is apparently not caused by the loss of the
potential palmitoylation site at Cys324, since a B2KR with
a point mutation of Cys324 to Ala internalized
[3H]BK as rapidly as the wild type B2KR.
From these results we conclude that the cytoplasmic carboxyl terminus
of the human B2KR contains sequences that are necessary and sufficient
to permit rapid ligand-induced sequestration of human kinin receptors
and internalization of their agonists.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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