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Related Experiment Videos

DNA hydrolyzing autoantibodies.

A M Shuster1, G V Gololobov, O A Kvashuk

  • 1V.A. Engelhardt Institute of Molecular Biology, Academy of Sciences of Russia, Moscow.

Science (New York, N.Y.)
|May 1, 1992
PubMed
Summary
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Autoantibodies in patients with autoimmune diseases exhibit DNA-nicking activity. This DNA-hydrolyzing activity, identified as immunoglobulin M (IgM) and immunoglobulin G (IgG), differs from standard deoxyribonuclease (DNase).

Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Patients with autoimmune pathologies can exhibit unique serum activities.
  • Autoantibodies are key players in autoimmune diseases.
  • The enzymatic activity of autoantibodies is not fully characterized.

Purpose of the Study:

  • To investigate the presence and nature of DNA-nicking activity in the sera of patients with autoimmune diseases.
  • To characterize the autoantibodies responsible for DNA hydrolysis.
  • To compare the DNA degradation pattern with known deoxyribonucleases (DNases).

Main Methods:

  • Serum samples from patients with autoimmune pathologies were analyzed for DNA-nicking activity.
  • Affinity and high-performance liquid chromatography were used for purification.

Related Experiment Videos

  • Immunoglobulin M (IgM) and immunoglobulin G (IgG) were identified as the active components.
  • Acid shock stability and DNA degradation patterns were assessed.

    • Main Results:

    • A DNA-nicking activity was detected in patient sera and attributed to autoantibodies.
    • The purified activity corresponded to IgM and IgG, reacting with anti-human IgG antibodies.
    • These DNA-hydrolyzing autoantibodies demonstrated stability to acid shock.
    • The DNA degradation pattern produced by these autoantibodies was distinct from DNase I and blood DNase.

    Conclusions:

    • Autoantibodies in autoimmune diseases can possess DNA-hydrolyzing capabilities.
    • The identified autoantibodies are immunoglobulins (IgM and IgG) with nuclease-like activity.
    • This activity is distinct from endogenous DNases and exhibits unique stability properties.