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IgG antibodies binding to different IFN species have been described in sera of healthy and diseased individuals. Human serum immunoglobulins have also been shown to interfere with IFN bioactivity. To characterize these antibodies, human recombinant IFN-alpha 2A (rIFN-alpha) was radioiodinated, and ligand binding studies were performed in human sera as well as on the human cell line A-549 in the presence of human serum. 125I-rIFN-alpha bound to serum factors of healthy individuals. However, less than 3% of the binding was to IgG and the binding was non-saturable and therefore most likely non-specific. 125I-rIFN-alpha bound to receptors on A-549 cells, and the ligand-receptor complexes appeared to internalize. However, both cell binding and internalization of 125I-rIFN-alpha were independent of the presence of human serum. We conclude that normal human sera do not contain detectable autoantibodies to rIFN-alpha.
M B Hansen, and
M Svenson, and
K Bendtzen
October 1990,
Clinical and experimental immunology,
M B Hansen, and
M Svenson, and
K Bendtzen
February 1981,
Journal of interferon research,
M B Hansen, and
M Svenson, and
K Bendtzen
January 1988,
British journal of haematology,
M B Hansen, and
M Svenson, and
K Bendtzen
July 2008,
Arthritis and rheumatism,
M B Hansen, and
M Svenson, and
K Bendtzen
January 1989,
British journal of haematology,
M B Hansen, and
M Svenson, and
K Bendtzen
May 1995,
Cellular and molecular biology (Noisy-le-Grand, France),
M B Hansen, and
M Svenson, and
K Bendtzen
April 1997,
Internal medicine (Tokyo, Japan),
M B Hansen, and
M Svenson, and
K Bendtzen
July 1979,
The Journal of clinical endocrinology and metabolism,
M B Hansen, and
M Svenson, and
K Bendtzen
January 1987,
Medecine interne,
M B Hansen, and
M Svenson, and
K Bendtzen
October 2008,
Veterinary immunology and immunopathology,
