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June 1, 1983The Journal of Immunology

Role of Ca2+ in phosphatidylinositol response and arachidonic acid release in formylated tripeptide- or Ca2+ ionophore A23187-stimulated guinea pig neutrophils.

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Authors

TTT TakenawaUniversity of TsukubaYHYoshimi HommaFukushima Medical UniversityYNYuki NagaiKobe Children's Hospital

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Implication

In vitro experiment demonstrates distinct calcium dependencies of phospholipase activation in stimulated guinea pig neutrophils, indicating differential regulatory pathways for lipid signaling.

Key Points

  • To investigate the regulatory role of calcium in phospholipid turnover and arachidonic acid release in guinea pig neutrophils stimulated by fMLP or calcium ionophore A23187.
  • Stimulated guinea pig neutrophils with the chemotactic peptide fMLP or Ca2+ ionophore A23187 in Ca2+-sufficient and Ca2+-depleted environments using EGTA.
  • Tracked phospholipid remodeling, enzymatic breakdown, and de novo lipid synthesis using radiolabeling with [32P]Pi, [3H]arachidonic acid, and [3H]glycerol.
  • fMLP sequentially activated phosphatidylinositol-specific phospholipase C prior to phospholipase A2; phospholipase C remained active during severe Ca2+ deprivation, whereas arachidonic acid release was completely inhibited.
  • Ca2+ ionophore A23187 directly activated phospholipase A2 to release arachidonic acid across multiple phospholipids and stimulated de novo synthesis of phosphatidylinositol and phosphatidic acid.

Cite This Study

Takenawa et al. (1983) studied this question.

synapsesocial.com/papers/6a86acafc27ad527967cacefhttps://doi.org/10.4049/jimmunol.130.6.2849
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