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Related Experiment Videos

In vitro complement binding on cytoplasmic structures in normal human skin: immunoelectronmicroscopic studies.

G Schuler, H Hintner, K Wolff

    The Journal of Cell Biology
    |November 1, 1982
    PubMed
    Summary
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    Normal human serum (NHS) activates the classical complement pathway via antibody-independent Clq binding to cytoplasmic intermediate-sized filaments (ISF). These ISF are the subcellular site for complement activation across various cell types.

    Area of Science:

    • Immunology
    • Cell Biology
    • Complement System

    Background:

    • Previous studies indicated antibody-independent Clq binding to cytoplasmic structures upon exposure to normal human serum (NHS).
    • This binding leads to classical complement pathway activation, evidenced by cytoplasmic C3 deposition.

    Purpose of the Study:

    • To elucidate the precise nature of cytoplasmic C3 binding structures using immunoelectronmicroscopic methods.
    • To identify the subcellular localization of classical complement pathway activation.

    Main Methods:

    • Cryostat skin sections were incubated with NHS.
    • Immunoelectronmicroscopy was employed using peroxidase-labeled rabbit anti-human C3 serum (HRP-R/Hu C3).
    • Detection of HRP reaction product revealed C3 deposition sites.

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    Main Results:

    • Cytoplasmic C3 deposition was observed in suprabasal keratinocytes, melanocytes, fibroblasts, smooth muscle cells, endothelial cells, pericytes, Schwann cells, and nerve axons.
    • C3 binding was exclusively localized to intermediate-sized filaments (ISF).
    • ISF were not decorated under conditions inhibiting classical complement pathway activation.

    Conclusions:

    • Intermediate-sized filaments (ISF) represent the subcellular site for antibody-independent classical complement pathway activation.
    • The complement-fixing capacity of ISF across different cell types suggests a conserved mechanism involving common alpha-helical domains.
    • This finding provides insights into the interaction between complement components and ISF.