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Complement factor adsorption on solid surfaces--an ellipsometric method for investigation of quantitative aspects.

H Elwing, C Dahlgren, R Harrison

    Journal of Immunological Methods
    |July 6, 1984
    PubMed
    Summary
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    Ellipsometry quantifies adsorbed proteins on surfaces. This study shows IgG adsorption impacts complement C3 binding and human polymorphonuclear leucocyte (PMNL) migration, revealing key interactions.

    Area of Science:

    • Biophysical Chemistry
    • Immunology
    • Surface Science

    Background:

    • Quantifying biomolecular interactions on surfaces is crucial for understanding biological processes.
    • Antibody-mediated immune responses involve complex interactions between proteins and cells.

    Purpose of the Study:

    • To quantify organic material adsorption from human sera onto antibody-coated surfaces using ellipsometry.
    • To investigate the relationship between immunoglobulin G (IgG) adsorption levels and complement factor binding (C3).
    • To measure the effect of IgG adsorption on human polymorphonuclear leucocyte (PMNL) migration inhibition.

    Main Methods:

    • Ellipsometry was employed to measure the adsorption of organic material from human sera onto antibody-coated surfaces.
    • Complement component C3 deposition was assessed on surfaces with varying IgG adsorption.

    Related Experiment Videos

  • A modified ellipsometry method quantified the inhibition of PMNL locomotion.
  • Main Results:

    • Maximal adsorption of organic material occurred at approximately 0.5 µg/cm² of IgG.
    • Complement component C3 was detected on antibody surfaces, but not C5, C8, or C9.
    • PMNL migration inhibition was observed within a narrow IgG adsorption range of 0.2 to 0.5 µg/cm².

    Conclusions:

    • IgG adsorbed on surfaces may lack binding sites for complement factors beyond C3.
    • The study highlights quantitative relationships between antibody-dependent complement activation and cellular responses like PMNL migration.
    • Ellipsometry provides a valuable tool for studying these complex immunological interactions.