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Receptor‐mediated ADP‐ribosylation of a phospholipase C‐stimulating G protein
Author(s) -
Gierschik Peter,
Jakobs Karl H.
Publication year - 1987
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(87)80451-9
Subject(s) - pertussis toxin , cholera toxin , adp ribosylation , g protein , phospholipase c , phospholipase , toxin , gtp' , peptide , biochemistry , receptor , phospholipase d , chemistry , nad+ kinase , microbiology and biotechnology , biology , signal transduction , enzyme
In membranes of myeloid differentiated HL 60 cells, the chemotactic peptide FMLP stimulates phospholipase C via a pertussis toxin‐sensitive G protein. FMLP markedly stimulates the cholera toxin‐dependent ADP‐ribosylation of a 40 kDa protein in these membranes. This effect of FMLP is inhibited by GTP and GTP[S], and is almost completely abolished in membranes of pertussis toxin‐pretreated HL 60 cells. Treatment of HL 60 membranes with cholera toxin and NAD markedly inhibits FMLP‐stimulated high affinity GTPase. These results suggest that a 40 kDa G protein sensitive to both pertussis and cholera toxin functionally interacts with the formyl peptide receptor of HL 60 cells and, thus, very likely is the G protein that stimulates phospholipase C in this system.