Use of fluoride ion as a probe for the guanine nucleotide-binding protein involved in the phosphoinositide-dependent neutrophil transduction pathway.
Fluoride activation of neutrophils was found to be associated with phosphoinositide turnover, as monitored by the time-dependent accumulation of inositol phosphates. Unlike phosphoinositide turnover induced by the chemotactic peptide, formylmethionylleucylphenylalanine, that induced by fluoride was not inhibited by pretreatment with pertussis toxin. The translocation of protein kinase C activity from the cytosolic to the membrane compartment was also observed in fluoride-stimulated cells. We have proposed that the mode of action of this halide ion involves interaction with a GTP-binding protein which serves as an intermediary unit between the receptors for inflammatory stimuli and the phosphoinositide-specific phosphodiesterase.
D003994:Bucladesine / Q000494:pharmacology; D019204:GTP-Binding Proteins / Q000097:blood*; D006801:Humans; D007700:Kinetics; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000494:pharmacology; D009504:Neutrophils / Q000187:drug effects / Q000378:metabolism*; D037342:Pertussis Toxin; D010716:Phosphatidylinositols / Q000097:blood*; D011493:Protein Kinase C / Q000097:blood; D012969:Sodium Fluoride / Q000494:pharmacology*; D010566:Virulence Factors, Bordetella / Q000494:pharmacology
D010716:Phosphatidylinositols; D010566:Virulence Factors, Bordetella; D009240:N-Formylmethionine Leucyl-Phenylalanine; D003994:Bucladesine; D012969:Sodium Fluoride; D037342:Pertussis Toxin; D011493:Protein Kinase C; D019204:GTP-Binding Proteins