Distribution and characterization of autoantibodies to interleukin 1 alpha in normal human sera

Scand J Immunol. 1990 Dec;32(6):695-701. doi: 10.1111/j.1365-3083.1990.tb03212.x.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Aged
  • Antibody Affinity
  • Antibody Specificity
  • Autoantibodies / blood*
  • Female
  • Humans
  • Immunoglobulin Fab Fragments / metabolism
  • Immunoglobulin G / analysis
  • Immunoglobulin Isotypes / analysis
  • Interleukin-1 / immunology*
  • Male
  • Middle Aged
  • Recombinant Proteins / immunology


  • Autoantibodies
  • Immunoglobulin Fab Fragments
  • Immunoglobulin G
  • Immunoglobulin Isotypes
  • Interleukin-1
  • Recombinant Proteins