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Research Article Free access | 10.1172/JCI116862

Binding of cytokines to pharmaceutically prepared human immunoglobulin.

M Svenson, M B Hansen, and K Bendtzen

Laboratory of Medical Immunology, Rigshospitalet University Hospital, Copenhagen, Denmark.

Find articles by Svenson, M. in: JCI | PubMed | Google Scholar

Laboratory of Medical Immunology, Rigshospitalet University Hospital, Copenhagen, Denmark.

Find articles by Hansen, M. in: JCI | PubMed | Google Scholar

Laboratory of Medical Immunology, Rigshospitalet University Hospital, Copenhagen, Denmark.

Find articles by Bendtzen, K. in: JCI | PubMed | Google Scholar

Published November 1, 1993 - More info

Published in Volume 92, Issue 5 on November 1, 1993
J Clin Invest. 1993;92(5):2533–2539. https://doi.org/10.1172/JCI116862.
© 1993 The American Society for Clinical Investigation
Published November 1, 1993 - Version history
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Abstract

Pharmaceutically prepared IgG, pooled from sera of over 2,000 normal individuals, contained both monomeric and dimeric IgG. Each type of IgG bound 125I-labeled interleukin (IL)-1 alpha, IL-1 beta, IL-6, and tumor necrosis factor (TNF)-alpha. Increased binding to IgG was observed if 125I-IL-1 beta was denatured by heating to 39 degrees C. However, the binding of both nondenatured and denatured 125I-IL-1 beta was not inhibited by unlabeled IL-1 beta. In contrast, binding of 125I-IL-1 alpha, 125I-IL-6, and 125I-TNF alpha was inhibited by the corresponding unlabeled cytokine. Papain-digestion of IgG abolished binding of 125I-TNF alpha but failed to influence the displaceable binding of 125I-IL-1 alpha and 125I-IL-6. 125I-TNF alpha was a mixture of trimeric and monomeric forms, the latter being the predominant form at lower concentrations. The apparent saturability of 125I-TNF alpha was explained by a higher nonspecific binding of monomeric than of trimeric 125I-TNF alpha to IgG. The amounts of cytokine antibodies in IgG preparations would contribute approximately 2 micrograms anti-IL-1 alpha IgG and 1 microgram anti-IL-6 IgG per kg body wt during high dose immune globulin therapy. In conclusion, pharmaceutical preparations of human IgG contain specific and neutralizing, high affinity antibodies against IL-1 alpha and IL-6, but not against TNF alpha or IL-1 beta. There are significant methodological pitfalls that hamper detection of IgG autoantibodies against cytokines.

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