血小板活化因子对小鼠巨噬细胞受体结合及产生IL-1的探讨

PAF Binding and IL-1 Production of the Thioglycollate Elicited Mouse Macrophages

本文探讨了血小板活化因子对硫乙醇酸钠刺激产生的小鼠腹腔巨噬细胞受体结合及产生白细胞介素1的状况。用PAF对~3H-PAF竞争结合实验,测定出对TG-Mφ膜结合的IC50,在20℃为8.5×10^(-9)M,0℃为9.7×10^(-9)M,两者无明显区别;而对TG-Mφ完整细胞的结合。在20℃为6.5×10^(-9)M,0℃为10.5×10^(-9)M,随温度的增高,IC50减小。NaCl有降低~3H-PAF特异结合的能力,IC50为7.5mM。PAF能够刺激TG-Mφ产生白细胞介素1,在10^(-3)M浓度较为明显,和对照组相比,P<0.05。

By using an in vitro radioligand binding assay for the platelet activating factor(PAF) receptor, we have determined IC50 of PAF for specific H-PAF binding to thioglycollate-elicited mouse macrophages (TG-Mφ) membranes and intact cells at 20℃ and 0℃ . Binding to the membranes, IC50 was 8.5×10^(-9)M at 20℃ and 9.7 ×10^(-9)M at 0℃.Binding to the intact cells, IC50 was 6.5×10^(-9)M at 20℃ and 10×10^(-9)M at 0℃ . The existence of PAF specific binding sites on the TG-Mφ was confirmed by the experiment. The presence of sodium ions inhibited H-PAF binding to the TG-Mφ membranes with an IC50 of 7.5mM. We have also examined the role of PAF on IL-1 production by TG-Mφ. The 10^(-(?))M PAF significantly enhanced IL-1 production.