Influence of the Cytosolic Carboxyl Termini of Human B1 and B2 Kinin Receptors on Receptor Sequestration, Ligand Internalization, and Signal Transduction

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-Arg 10 -kallidin and bradykinin (BK), both wild type receptors, as well as truncated B2KRs, a mutated B2KR, and chimeric...

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Bibliographic Details
Published in:The Journal of biological chemistry 1998-01, Vol.273 (5), p.2617-2623
Main Authors: Faussner, A, Proud, D, Towns, M, Bathon, J M
Format: Article
Language:English
Subjects:
Animals
Biological Transport
Cell Compartmentation
Cells, Cultured
CHO Cells
Cricetinae
Cytosol
Fibroblasts - cytology
Humans
Inositol Phosphates - metabolism
Ligands
Lung - cytology
Models, Molecular
Peptide Fragments - genetics
Peptide Fragments - metabolism
Protein Conformation
Receptor, Bradykinin B1
Receptor, Bradykinin B2
Receptors, Bradykinin - genetics
Receptors, Bradykinin - metabolism
Recombinant Fusion Proteins - metabolism
Signal Transduction
Transfection
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Summary: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-Arg 10 -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 [ 3 H]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 3 H-labeled des-Arg 10 -kallidin with cells expressing B1KR resulted in a modest, slow internalization of the ligand (
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.273.5.2617