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Related Experiment Videos

Phospholipase D1 regulates phagocyte adhesion.

Shankar S Iyer1, Reitu S Agrawal, Christopher R Thompson

  • 1Inflammation Program, Division of Infectious Diseases, Department of Internal Medicine, University of Iowa Carver College of Medicine, 2501 Crosspark Road, Iowa City, IA 52242, USA.

Journal of Immunology (Baltimore, Md. : 1950)
|March 7, 2006
PubMed
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Phospholipase D (PLD) regulates phagocyte adhesion, a critical cellular response. Inhibiting PLD reduces phagocyte adhesion and actin polymerization, suggesting PLD

Area of Science:

  • Cell Biology
  • Immunology
  • Biochemistry

Background:

  • Cellular adhesion is vital for physiological processes like development and motility, and pathological conditions such as inflammation and metastasis.
  • Phagocyte adhesion modulates crucial antimicrobial and cytotoxic functions, including the respiratory burst, secretion, and apoptosis.
  • Phospholipase D (PLD) is implicated in signaling pathways relevant to cellular adhesion and function.

Purpose of the Study:

  • To investigate the role of Phospholipase D (PLD) in regulating phagocyte adhesion.
  • To determine if PLD activity is stimulated by phagocyte adhesion.
  • To elucidate the specific PLD isoform involved and its mechanism in phagocyte adhesion.

Main Methods:

  • Measured PLD activity in primary human neutrophils and macrophages, and myeloid-macrophage cell lines upon adhesion to various substrates (fibronectin, fibrinogen, collagen, plastic).

Related Experiment Videos

  • Utilized confocal microscopy to assess the localization of PLD1 relative to actin filaments and focal adhesion proteins (paxillin).
  • Employing chemical inhibitors and short-interfering RNA (siRNA) to reduce PLD activity and knockdown PLD1 expression, assessing the impact on phagocyte adhesion and F-actin content.

    • Main Results:

    • Phagocyte adhesion to fibronectin, fibrinogen, collagen, and plastic significantly stimulated PLD activity, which was rapid and sustained.
    • PLD1 was found to partially colocalize with actin filaments at the adherent interface near paxillin.
    • Inhibition or knockdown of PLD1 markedly reduced phagocyte adhesion and decreased total cellular F-actin.

    Conclusions:

    • Adhesion actively stimulates Phospholipase D (PLD) activity in phagocytes.
    • PLD1 plays a regulatory role in the initial stages of phagocyte adhesion.
    • PLD activity may be essential for promoting adhesion-dependent phagocyte effector functions.