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Distribution and Characterization of Autoantibodies to Interleukin 1α in Normal Human Sera
Author(s) -
SVENSON M.,
HANSEN M. BAGGE,
BENDTZEN K.
Publication year - 1990
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1990.tb03212.x
Subject(s) - avidity , antibody , autoantibody , immunology , recombinant dna , alpha (finance) , immune system , microbiology and biotechnology , biology , immunoglobulin g , chemistry , medicine , biochemistry , gene , construct validity , nursing , patient satisfaction
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. [ 125 I]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 [ 125 I]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 [ l25 I]rIL‐1α 10 [0.7 ‐27] versus 3.3 [0.5‐7.3] ng/ml; and mean K d :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.