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Related Experiment Videos

Fibronectin binds to the C1q component of complement

D H Bing, S Almeda, H Isliker

    Proceedings of the National Academy of Sciences of the United States of America
    |July 1, 1982
    PubMed
    Summary

    Fibronectin binds complement component C1q through its collagen-like tail region, similar to gelatin binding. This interaction suggests fibronectin may aid in clearing C1q-coated debris and immune complexes.

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    Area of Science:

    • Biochemistry
    • Immunology
    • Cell Biology

    Background:

    • Fibronectin is a key extracellular matrix protein involved in cell adhesion and clearance mechanisms.
    • Complement component C1q initiates the classical complement pathway and binds to immune complexes and cellular debris.

    Purpose of the Study:

    • To investigate the binding interaction between fibronectin and C1q.
    • To identify the specific regions of C1q involved in fibronectin binding.
    • To explore the functional implications of this interaction in biological clearance processes.

    Main Methods:

    • Immobilization of fibronectin to plastic tubes and C1q to Sepharose beads for binding assays.
    • Determination of binding affinity (Kd) and inhibition constants (Ki) under varying ionic conditions.

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  • Competitive binding assays using fragments of C1q.

    • Main Results:

    • Fibronectin binds soluble C1q with a dissociation constant (Kd) of 82 ± 2.6 nM.
    • Binding is sensitive to ionic conditions but not significantly affected by pH.
    • The collagenous tail regions of C1q, but not the globular heads, competitively inhibit binding (Ki = 59 nM).
    • Gelatin also binds fibronectin (Kd = 131 nM), indicating a similar binding mechanism.

    Conclusions:

    • Fibronectin binds C1q via its collagen-like tail region, analogous to gelatin binding.
    • This interaction suggests a potential role for fibronectin in the clearance of C1q-opsonized materials, such as immune complexes and cellular debris, through mechanisms like endocytosis.