Receptor-mediated activation of arachidonic acid release in mouse peritoneal macrophages is linked to extracellular calcium influx

https://doi.org/10.1016/S0006-291X(05)81170-2Get rights and content

The role of external calcium in platelet-activating factor- and zymosan-stimulated arachidonic acid release from mouse macrophages was investigated. Deprivation of external Ca2+ led to strong inhibition of receptor-mediated arachidonic acid release, which was completely restored when Ca2+ was added to the incubation medium. When arachidonic acid release was examined in Ca2+-depleted cells, the response took place only in presence of external Ca2+. Verapamil, a voltage-dependent Ca2+ channel blocker, nearly abolished arachidonic acid release in response to both platelet-activating factor and zymosan. These results suggest that extracellular Ca2+ influx is functionally linked to arachidonic acid release and hence to phospholipase A2 activation in mouse peritoneal macrophages.

References (26)

  • BurgoyneR.D. et al.

    Trends Biochem. Sci.

    (1990)
  • EmilssonA. et al.

    Biochim. Biophys. Acta

    (1985)
  • EmilssonA. et al.

    Biochim. Biophys. Acta

    (1986)
  • GlaserK.B. et al.

    J. Biol. Chem.

    (1990)
  • LokeshB.R. et al.

    Biochim. Biophys. Acta

    (1985)
  • FernándezB. et al.

    FEBS Lett.

    (1990)
  • DiezE. et al.

    Biochim. Biophys. Acta

    (1987)
  • BalsindeJ. et al.

    Biochim. Biophys. Acta

    (1988)
  • BrooksR.C. et al.

    J. Biol. Chem.

    (1989)
  • ChristiansenN.P. et al.

    Blood

    (1988)
  • SlivkaS.R. et al.

    J. Biol. Chem.

    (1988)
  • HallamT.J. et al.

    Trends Pharmacol. Sci.

    (1989)
  • UlevitchR.J. et al.

    J. Biol. Chem.

    (1988)
  • Cited by (18)

    • Cellular Assays for Evaluating Calcium-Dependent Translocation of cPLA<inf>2</inf>α to Membrane

      2017, Methods in Enzymology
      Citation Excerpt :

      cPLA2α is subject to complex mechanisms of regulation that are important for controlling the levels of free arachidonic acid available for metabolism through the cyclooxygenase and lipoxygenase pathways. Initial characterization of cPLA2α showed that it required calcium for activity in vitro consistent with cellular studies showing that calcium-mobilizing agonists induce arachidonic acid release (Clark, Milona, & Knopf, 1990; Fernandez & Balsinde, 1991; Kramer, Roberts, Manetta, & Putnam, 1991; Leslie, Voelker, Channon, Wall, & Zelarney, 1988; Rittenhouse-Simmons & Deykin, 1977; Rzigalinski, Blackmore, & Rosenthal, 1996). Calcium was found to promote the interfacial binding of cPLA2α to phospholipid vesicles in vitro and to cellular membranes (Channon & Leslie, 1990; Clark et al., 1991; Glover et al., 1995; Hirabayashi et al., 1999; Peters-Golden, Song, Marshall, & Brock, 1996; Schievella, Regier, Smith, & Lin, 1995).

    • Involvement of calcium-independent phospholipase A<inf>2</inf> in hydrogen peroxide-induced accumulation of free fatty acids in human U937 cells

      2002, Journal of Biological Chemistry
      Citation Excerpt :

      In the next series of experiments, the cells were depleted of their intracellular Ca2+ by treating them with 40 μm quin2/AM plus 1 mm EGTA in a Ca2+-free medium. This procedure buffers and clamps the intracellular calcium concentration at very low levels (about 10−8m) (32). Under these conditions, the AA response to H2O2 remained unchanged, whereas the ConA response was abolished (Fig. 5).

    • Ethanol inhibits zymosan-stimulated eicosanoid production in mouse peritoneal macrophages

      1994, Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
    View all citing articles on Scopus
    View full text