Abstract
In vitro treatment of mouse peritoneal cells with 1 micrograms lysophosphatidylcholine (lyso-Pc)/mL in serum free-0.1% egg albumin-supplemented RPMI 1640 medium for 30 min, followed by 3 h cultivation in a medium supplemented with human serum, resulted in a greatly enhanced Fc-receptor-mediated phagocytic activity of macrophages. Vitamin D-binding protein (group-specific component [Gc]) of alpha 2-globulin fraction was shown to be the sole serum glycoprotein required for the generation of a potent macrophage-activating factor. When a mixture of lysophosphatidylcholine (lyso-Pc)-treated nonadherent and adherent cells were cultured in a medium supplemented with a small amount of purified Gc protein (1 ng/mL), a greatly enhanced activation of macrophages was demonstrated. The generation of macrophage-activating factor from purified Gc protein was far more efficient than that from whole serum, indicating that a serum component is inhibitory to the activation process of macrophages. While three other major serum glycoproteins (alpha 2-macroglobulin, alpha 2-HS-glycoprotein and haptoglobin) were neither stimulatory nor inhibitory to lyso-Pc-primed macrophage activation, serum albumin (competitively with Gc protein) appeared to be inhibitory to the process of macrophage activation.
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