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G α ‐16 complements the signal transduction cascade of chemotactic receptors for complement factor C5a (C5a‐R) and N ‐formylated peptides (fMLF‐R) in Xenopus laevis oocytes: G α ‐16 couples to chemotactic receptors in Xenopus oocytes
Author(s) -
M.P.M. van der Burg,
Ute Raffetseder,
Melanie Grove,
Andreas Klos,
Jörg Köhl,
Wilfried Bautsch
Publication year - 1995
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(95)01379-2
Subject(s) - xenopus , biology , c5a receptor , receptor , chemotaxis , microbiology and biotechnology , signal transduction , complement system , biochemistry , immunology , antibody , gene
The human leukocyte chemoattractant receptors for complement factor C5a (C5a‐R) and N ‐formylated peptides (fMLF‐R) are important members of the superfamily of G‐protein coupled receptors (GPCR). Uniquely among the GPCR, these two receptors cannot be expressed in a functionally active form in the oocytes of the frog Xenopus laevis , but require substitution of total RNA of the myelomonocytic U‐937 or HL‐60 cell lines, respectively. Recently, it was reported that the C5a‐R may couple to the α subunit of G‐16. We have tested this G‐protein for its ability to complement the signal transduction cascade of the C5a‐R and fMLF‐R in Xenopus oocytes. Injection of cRNA for the C5a‐R in combination with G α ‐16 led to expression of a functional C5a‐R as measured by ligand‐induced whole cell current. In contrast to a previous report, the fMLF‐R exhibited some residual functional activity when transiently expressed in Xenopus oocytes the extent of which could, however, substantially be increased by coexpression of G α ‐16. Thus, G α ‐16 complements the signal transduction cascade of both receptors in Xenopus laevis oocytes and is most likely the complementing factor present in the U‐937 and HL‐60 cell lines.