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Disruption of the cytoskeleton after apoptosis induction with autoantibodies

Ingrid Böhm1

  • 1Department of Radiology, University of Bonn, Sigmund-Freud Strasse 25, 53105 Bonn, Germany. i.boehm@uni-bonn.de

Autoimmunity
|August 13, 2003
PubMed

Insights

Anti-double-stranded DNA (dsDNA) antibodies induce F-actin disruption and caspase 3 activation in peripheral blood mononuclear cells (PBMC). This leads to less phosphatidylserine (PS) externalization, potentially reducing apoptotic cell clearance and promoting autoantibody production.

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • Autoimmune diseases are often characterized by the presence of autoantibodies.
  • Anti-double-stranded DNA (anti-dsDNA) antibodies are key autoantibodies in systemic lupus erythematosus (SLE).
  • Apoptosis, or programmed cell death, plays a crucial role in maintaining tissue homeostasis and preventing autoimmunity.

Purpose of the Study:

  • To investigate the effects of anti-dsDNA antibodies on F-actin disruption and phosphatidylserine (PS) externalization during apoptosis in peripheral blood mononuclear cells (PBMC).
  • To explore the relationship between F-actin disruption, caspase 3 activation, and PS externalization in anti-dsDNA antibody-treated cells.
  • To understand the implications of these cellular changes for the clearance of apoptotic cells and subsequent autoantibody production.

Main Methods:

  • Peripheral blood mononuclear cells (PBMC) were treated with anti-dsDNA antibodies.
  • F-actin disruption was assessed by FITC-phalloidin staining.
  • Phosphatidylserine (PS) externalization was detected by annexin V binding.
  • Caspase 3 activation was measured within the cytoplasm.

Main Results:

  • Anti-dsDNA antibody treatment significantly induced F-actin disruption in PBMC (p < 0.006).
  • Despite similar F-actin disruption, PS externalization was significantly lower in cells treated with anti-dsDNA antibodies compared to untreated cells (58.4% vs. 81.9%).
  • F-actin disruption correlated strongly with caspase 3 activation (r = -0.92599; p < 8.87 x 10^-10) in both treated and untreated cells.

Conclusions:

  • Anti-dsDNA antibody-induced apoptosis is characterized by more pronounced intracellular changes (F-actin disruption, caspase 3 activation) than cell surface alterations (PS externalization).
  • The diminished PS externalization may lead to reduced phagocytosis of apoptotic cells.
  • Impaired clearance of apoptotic cells could contribute to the perpetuation of autoimmunity by promoting autoantibody production against cellular epitopes exposed during apoptosis.

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