Svenson M, Hansen M B, Kayser L, Rasmussen A K, Reimert C M, Bendtzen K
Department of Medicine TTA, Diseases M, Rigshopitalet University Hospital, Copenhagen, Denmark.
Cytokine. 1992 Mar;4(2):125-33. doi: 10.1016/1043-4666(92)90047-u.
Immunoglobulin G (IgG) antibodies to interleukin 1 alpha (IL-1 alpha) are frequently found in the sera of healthy human individuals. The effects of these autoantibodies on receptor binding and biological activities of human IL-1 were tested. Using the murine T-lymphocyte line NOB-1, human thyrocytes and human foreskin fibroblasts, the antibodies competitively inhibited the biological activity of human recombinant IL-1 alpha (rIL-1 alpha). The degree of inhibition correlated with 125I-rIL-1 alpha binding to IgG in different immunoglobulin preparations and in individual sera. These antibodies also neutralized the IL-1 activity of isolated membrane fragments and lysates of human blood monocytes activated by lipopolysaccharide. In contrast, the supernatant IL-1 activity was not affected. Stronger inhibition of biological activity and cell binding of 125I-rIL-1 alpha was obtained with NOB-1 cells than with human thyrocytes. The antibodies failed to interfere with the biological activity of rIL-1 beta. It is concluded that IgG autoantibodies of IL-1 alpha in the sera of healthy humans selectively inhibit the biological activity of the soluble and membrane-associated forms of IL-1 alpha in vitro, and that the degree of biological inhibition afforded by these antibodies depends upon the target cell.
在健康人体血清中经常发现白细胞介素1α（IL-1α）的免疫球蛋白G（IgG）抗体。测试了这些自身抗体对人IL-1受体结合和生物学活性的影响。使用小鼠T淋巴细胞系NOB-1、人甲状腺细胞和人包皮成纤维细胞，这些抗体竞争性抑制人重组IL-1α（rIL-1α）的生物学活性。抑制程度与不同免疫球蛋白制剂和个体血清中125I-rIL-1α与IgG的结合相关。这些抗体还中和了脂多糖激活的人血单核细胞膜碎片和裂解物的IL-1活性。相反，上清液中的IL-1活性不受影响。与人类甲状腺细胞相比，NOB-1细胞对125I-rIL-1α的生物学活性和细胞结合的抑制作用更强。这些抗体未能干扰rIL-1β的生物学活性。得出的结论是，健康人血清中IL-1α的IgG自身抗体在体外选择性抑制IL-1α可溶性和膜相关形式的生物学活性，并且这些抗体提供的生物学抑制程度取决于靶细胞。
