Distribution and Characterization of Autoantibodies to Interleukin 1α in Normal Human Sera

Publisher Website
Google Scholar
Abstract
Antibodies against IL‐1α were detected in sera of apparently healthy individuals. The immunoglobulins belonged to the IgG and class, particularly IgG1. IgG2. and IgG4. [125I]rIL‐1α bound to Tab fragments of IgG. and IgG immune complexes of molecular weights from 160 to 700 kDa were formed in the sera by [125I]rIL‐1α. The occurrence of detectable anti‐IL‐1α IgG in sera of 32 male and 32 female donors was 25 and 22% respectively. As judged by Scatchard analysis of the binding data, the capacity and avidity of binding were greaser in the male than in the female sera (mean capacity to bind [l25I]rIL‐1α 10 [0.7 ‐27] versus 3.3 [0.5‐7.3] ng/ml; and mean Kd:5.5 [5‐7] versus 11 [4 16] PM). The antibodies did not cross‐bind human recombinant IL‐1β, IL‐2, 1L‐6. or tumour necrosis factor alpha (TNF‐α). It is concluded that native IL‐1α seems lo trigger production of specific, high‐avidity IgG antibodies in a relatively large number of normal individuals. These autoantibodies may regulate immunoinflammatory processes involving IL‐1α.