Receptor‐mediated ADP‐ribosylation of a phospholipase C‐stimulating G protein
Authors:
- 16 November 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 224 (1) , 219-223
Abstract
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.Keywords
This publication has 27 references indexed in Scilit:
- A novel cholera toxin‐sensitive G‐protein (Gc) regulating receptor‐mediated phosphoinositide signalling in human pituitary clonal cellsFEBS Letters, 1987
- G PROTEINS: TRANSDUCERS OF RECEPTOR-GENERATED SIGNALSAnnual Review of Biochemistry, 1987
- Which G protein subunits are the active mediators in signal transduction?Trends in Pharmacological Sciences, 1987
- Purification and immunochemical characterization of the major pertussis‐toxin‐sensitive guanine‐nucleotide‐binding protein of bovine‐neutrophil membranesEuropean Journal of Biochemistry, 1987
- Polyphosphoinositide phosphodiesterase: regulation by a novel guanine nucleotide binding protein, GpTrends in Biochemical Sciences, 1987
- A pertussis/choleratoxin-sensitive N protein may mediate chemoattractant receptor signal transductionBiochemical and Biophysical Research Communications, 1986
- Role of guanine nucleotide binding protein in the activation of polyphosphoinositide phosphodiesteraseNature, 1985
- Inhibition of receptor-mediated release of arachidonic acid by pertussis toxinCell, 1984
- Interaction of Polymorphonuclear Neutrophils with Escherichia ColiJournal of Clinical Investigation, 1978
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976