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Two distinct chemotactic factor inactivators in human serum.

G Till, P A Ward

    Journal of Immunology (Baltimore, Md. : 1950)
    |February 1, 1975
    PubMed
    Summary
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    Two human serum chemotactic factor inactivators (CFI) were isolated: a 7S beta-globulin inactivating C3 fragments and a 4S alpha-globulin inactivating C5 fragments. Both are crucial for regulating chemotaxis.

    Area of Science:

    • Immunology and Biochemistry
    • Complement System and Chemotaxis

    Background:

    • Chemotactic factors, particularly fragments of C3 and C5, play a vital role in immune cell recruitment.
    • The regulation of these chemotactic activities is essential for controlling inflammatory responses and preventing tissue damage.
    • The existence and nature of specific inhibitors for these chemotactic factors in human serum were previously unclear.

    Purpose of the Study:

    • To isolate and characterize the factor responsible for inactivating chemotactic activity in human serum.
    • To determine the specificities of different serum components towards various chemotactic fragments.
    • To elucidate the biochemical properties and optimal conditions for the activity of these inactivators.

    Main Methods:

    • Isolation of chemotactic factor inactivator (CFI) from whole human serum using salt precipitation, anionic exchange, and gel filtration chromatography.

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  • Characterization of isolated fractions based on sedimentation velocity (ultracentrifugation).
  • Assay of inactivator specificity against C3 and C5 chemotactic fragments.

    • Main Results:

    • Two distinct CFI fractions were isolated: a 7S beta-globulin and a 4S alpha-globulin.
    • The 7S beta-globulin specifically inactivated chemotactic activity associated with C3 fragments.
    • The 4S alpha-globulin specifically inactivated the C5 chemotactic fragment. Crude CFI demonstrated heat lability and dependence on time, temperature, and pH (optimal 7.2-7.4).

    Conclusions:

    • Human serum contains distinct alpha- and beta-globulin inhibitors targeting specific complement-derived chemotactic fragments (C3 and C5).
    • These findings reveal a regulatory mechanism for chemotaxis mediated by specific inactivators.
    • The characterized properties (heat lability, pH optimum) provide insights into the stability and function of these immune regulators.