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[Interaction between fibronectin and aggregated IgG].

E J Menzel, W Borth, B Kaik

    Wiener Klinische Wochenschrift
    |December 23, 1983
    PubMed
    Summary
    This summary is machine-generated.

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    Plasma fibronectin binds to aggregated human IgG, forming immune complexes that precipitate. This interaction impacts immune complex assay reliability, with fibronectin interfering with conglutinin binding assays.

    Area of Science:

    • Biochemistry
    • Immunology

    Context:

    • Immune complexes play a role in various autoimmune diseases.
    • Accurate detection of immune complexes is crucial for diagnosis and monitoring.
    • Plasma fibronectin is a protein involved in immune responses and tissue repair.

    Purpose:

    • To investigate the interaction between plasma fibronectin and aggregated human IgG (a model for immune complexes).
    • To evaluate the reliability of two common immune complex assays in the presence of fibronectin.

    Summary:

    • Plasma fibronectin forms complexes with aggregated human IgG, leading to precipitation in buffered saline.
    • No significant interaction was observed in serum or synovial fluid.
    • The C1q solid phase assay demonstrated low susceptibility to fibronectin interference.

    Related Experiment Videos

  • The conglutinin binding assay showed increased immune complex values when pathological concentrations of fibronectin were present.

    • Impact:

    • Findings highlight the potential for fibronectin to interfere with specific immune complex detection methods.
    • Suggests the need for assay validation in the presence of fibronectin, particularly for the conglutinin binding assay.
    • Informs the interpretation of immune complex assay results in clinical settings where fibronectin levels may be altered.