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  • Title: Characterization of formylmethionyl-leucyl-phenylalanine stimulation of inositol trisphosphate accumulation in rabbit neutrophils.
    Author: Bradford PG, Rubin RP.
    Journal: Mol Pharmacol; 1985 Jan; 27(1):74-8. PubMed ID: 2981403.
    Abstract:
    Inositol trisphosphate (IP3) formed by phospholipase C-mediated breakdown of triphosphoinositide (PIP2) may be a ubiquitous second messenger for a number of Ca2+-mobilizing receptor agonists. Using [3H]inositol-labeled rabbit peritoneal neutrophils, we report that radiolabeled inositol phosphates are generated in response to the chemotactic peptide, formylmethionyl-leucyl-phenylalanine (fMet-Leu-Phe). fMet-Leu-Phe-stimulated formation of [3H]IP3 occurs with a rapid time course and a concentration dependence which closely parallels that of stimulated lysosomal enzyme secretion. The synthetic peptide methionyl-leucyl-phenylalanine, which is unable to promote secretion, failed to elevate [3H]IP3 accumulation, and the competitive antagonist t-butyloxycarbonyl-Phe-Leu-Phe-Leu-Phe depressed the stimulant action of fMet-Leu-Phe on [3H]IP3 levels and secretion. The Ca2+ ionophore ionomycin, which promotes secretion, was unable to enhance IP3 levels, confirming that polyphosphoinositide hydrolysis is a specific receptor-mediated event that precedes calcium mobilization during neutrophil activation. The ability of leukotriene B4 to also promote a rapid accumulation of [3H]IP3 suggests that there exists in the neutrophil an interaction between phospholipase A2 and C-mediated events. These findings support the hypothesis that IP3 may be a pivotal messenger for signal transfer by Ca2+-mobilizing receptor agonists.
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