Hansen M B, Svenson M, Bendtzen K
Department of Infectious Diseases M, Rigshospitalet University Hospital, Copenhagen, Denmark.
Clin Exp Immunol. 1992 Jun;88(3):559-62. doi: 10.1111/j.1365-2249.1992.tb06487.x.
IgG antibodies binding to different IFN species have been described in sera of healthy and diseased individuals. Human serum immunoglobulins have also been shown to interfere with IFN bioactivity. To characterize these antibodies, human recombinant IFN-alpha 2A (rIFN-alpha) was radioiodinated, and ligand binding studies were performed in human sera as well as on the human cell line A-549 in the presence of human serum. 125I-rIFN-alpha bound to serum factors of healthy individuals. However, less than 3% of the binding was to IgG and the binding was non-saturable and therefore most likely non-specific. 125I-rIFN-alpha bound to receptors on A-549 cells, and the ligand-receptor complexes appeared to internalize. However, both cell binding and internalization of 125I-rIFN-alpha were independent of the presence of human serum. We conclude that normal human sera do not contain detectable autoantibodies to rIFN-alpha.
在健康个体和患病个体的血清中，已发现存在与不同干扰素种类结合的IgG抗体。人血清免疫球蛋白也已被证明会干扰干扰素的生物活性。为了表征这些抗体，对人重组干扰素α 2A（rIFN-α）进行了放射性碘化，并在人血清以及存在人血清的情况下，在人细胞系A-549上进行了配体结合研究。125I-rIFN-α与健康个体的血清因子结合。然而，不到3%的结合是与IgG的结合，且这种结合不饱和，因此很可能是非特异性的。125I-rIFN-α与A-549细胞上的受体结合，并且配体-受体复合物似乎发生了内化。然而，125I-rIFN-α的细胞结合和内化均与人血清的存在无关。我们得出结论，正常人血清中不含有可检测到的针对rIFN-α的自身抗体。
