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Interaction of casein with human polymorphonuclear cells.

M Solymossy, Z Nagy, G Tóth

    Biochemical Medicine and Metabolic Biology
    |June 1, 1986
    PubMed
    Summary
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    Iodinated casein (125I-casein) binds to polymorphonuclear (PMN) cells via hydrophobic forces, a process crucial for inducing cell migration. This binding is specific and not inhibited by common cell treatments.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Immunology

    Background:

    • Polymorphonuclear (PMN) cells are crucial immune cells involved in inflammatory responses.
    • Casein is known to attract PMN cells, but the mechanism of its attachment is not fully understood.

    Purpose of the Study:

    • To investigate the binding characteristics of iodinated casein (125I-casein) to PMN cells.
    • To elucidate the forces and mechanisms involved in casein-mediated PMN cell chemotaxis.

    Main Methods:

    • Radiolabeling of casein with iodine-125 (125I-casein) for detection.
    • Incubation of 125I-casein with PMN cells at various temperatures and time points.
    • Assessing binding saturation and stability.
    • Investigating the effect of cell pretreatments (trypsin, butanol) and inhibitors (indomethacin, azide, PMSF) on binding.

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  • Evaluating the role of hydrophobic interactions using leucine.

    • Main Results:

    • Iodination did not impair the chemotactic effect of casein.
    • 125I-casein binding increased over time, reaching a plateau around 45 minutes at 24°C and 37°C.
    • Binding did not show saturation even at high casein concentrations (15 mg/ml).
    • Approximately 40% of bound casein remained attached to PMN cells after 60 minutes in a casein-free medium.
    • Cell pretreatments and inhibitors did not affect casein binding.
    • The hydrophobic amino acid leucine counteracted casein attachment.

    Conclusions:

    • Casein binds specifically to PMN cell membranes at chemotactic concentrations through hydrophobic forces.
    • The binding likely involves the formation of micellar casein-membrane lipid complexes.
    • These complexes may play a role in the induction of PMN cell chemotaxis.