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Selective coupling of the human anaphylatoxin C5a receptor and α 16 in human kidney 293 cells
Author(s) -
Buhl Anne Mette,
Eisfelder Bartholomew J.,
Worthen G.Scott,
Johnson Gary L.,
Russell Marijane
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81464-b
Subject(s) - anaphylatoxin , c5a receptor , receptor , human kidney , coupling (piping) , microbiology and biotechnology , chemistry , kidney , biophysics , biology , immunology , biochemistry , materials science , endocrinology , complement system , antibody , metallurgy
The peptide C5a which is generated during the complement cascade is an important chemotactic factor involved in the inflammatory response. The C5a receptor (C5aR) primary sequence suggests that it has a serpentine structure of seven transmembrane domains which is typical of classical G‐protein‐coupled receptors. To investigate the signal transduction mechanism of C5a we transiently expressed the C5aR in combination with different G‐protein a subunits in human kidney 293 cells and measured the PLC activity induced upon C5a stimulation. Cotransfection of C5aR and α 16 stimulated PLC while cotransfection of C5aR with either α q or α 12 did not.