title: Distribution and characterization of autoantibodies to interleukin 1 alpha in normal human sera.
abstract: Antibodies against IL-1 alpha were detected in sera of apparently healthy individuals. The immunoglobulins belonged to the IgG class, particularly IgG1, IgG2, and IgG4. [125I]rIL-1 alpha bound to Fab fragments of IgG, and IgG immune complexes of molecular weights from 160 to 700 kDa were formed in the sera by [125I]rIL-1 alpha. The occurrence of detectable anti-IL-1 alpha 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 greater in the male than in the female sera (mean capacity to bind [125I]rIL-1 alpha: 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-1 beta, IL-2, IL-6, or tumour necrosis factor alpha (TNF-alpha). It is concluded that native IL-1 alpha seems to trigger production of specific, high-avidity IgG antibodies in a relatively large number of normal individuals. These autoantibodies may regulate immunoinflammatory processes involving IL-1 alpha.
authors: Department of infectious diseases M, Rigshospitalet University Hospital, Copenhagen, Denmark.
authors: M
authors: M
authors: Svenson
authors: M
authors: M
authors: Bagge Hansen
authors: K
authors: K
authors: Bendtzen
mesh_terms: D000328:Adult; D000368:Aged; D000915:Antibody Affinity; D000918:Antibody Specificity; D001323:Autoantibodies / Q000097:blood*; D005260:Female; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000378:metabolism; D007074:Immunoglobulin G / Q000032:analysis; D007132:Immunoglobulin Isotypes / Q000032:analysis; D007375:Interleukin-1 / Q000276:immunology*; D008297:Male; D008875:Middle Aged; D011994:Recombinant Proteins / Q000276:immunology
chemical_list: D001323:Autoantibodies; D007140:Immunoglobulin Fab Fragments; D007074:Immunoglobulin G; D007132:Immunoglobulin Isotypes; D007375:Interleukin-1; D011994:Recombinant Proteins