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PMID: 1830582 Published · ppublish English Journal Article

Interleukin-1 receptor antagonist competitively inhibits the binding of interleukin-1 to the type II interleukin-1 receptor.

The Journal of biological chemistry ·Vol. 266 ·No. 22 ·1991-08-05 ·Pages 14147-50

Granowitz EV, Clark BD, Mancilla J, Dinarello CA

Abstract

The interleukin-1 receptor antagonist (IL-1ra) inhibits the binding of interleukin-1 (IL-1) to T-cell lines possessing the type I IL-1 receptor; evidence has been published (Carter, D. B., Deibel, M. R. J., Dunn, C. J., Tomich, C. S., Laborde, A. L., Slightom, J. L., Berger, A. E., Bienkowski, M. J., Sun, F. F., McEwan, R. N., Harris, P. K. W., Yem, A. W., Waszak, G. A., Chosay, J. G., Sieu, L. C., Hardee, M. M., Zurcher-Neely, H. A., Reardon, I. M., Heinrickson, R. L., Truesdell, S. E., Shelly, J. A., Eessalu, T. E., Taylor, B. M., and Tracey, D. E. (1990) Nature 344, 633-638; Hannum, C. H., Wilcox, C. J., Arend, W. P., Joslin, F. G., Dripps, D. J., Heimdal, P. L., Armes, L. G., Sommer, A., Eisenberg, S. P., and Thompson, R. C. (1990) Nature 343, 336-340) that IL-Ira does not bind to the type II IL-1 receptor (IL-1RtII). In this study we examined the ability of human recombinant IL-1ra to block the binding of IL-1 to the IL-1RtII on human polymorphonuclear leukocytes (PMN) and Raji human B-lymphoma cells. The binding of 125I-IL-1 beta to PMN was competively inhibited by IL-1ra. IL-1 beta was more potent in inhibiting the binding of 125I-IL-1 beta than IL-1ra. Incubating PMN with 125I-IL-1ra in the presence of increasing concentrations of IL-1 beta or IL-1ra showed that IL-1 beta was an approximately 40-fold more potent inhibitor of binding of 125I-IL-1ra than unlabeled IL-1ra. The IL-1ra was approximately 500-fold less potent in inhibiting the binding of 125I-IL-1 alpha than IL-1 alpha. IL-1ra was also able to competitively inhibit binding of 125I-IL-1 beta to Raji cells. PMN or Raji cells were also incubated with 125I-IL-1 in the absence or presence of IL-1 or IL-1ra. After cross-linking of IL-1 to cells followed by specific immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed a band at 85 kDa corresponding to the 68-kDa IL-1RtII. However, in the presence of an excess of either unlabeled IL-1 or IL-1ra, the 85-kDa IL-1.IL-1RtII complex was not present. These findings demonstrate that the IL-1ra recognizes and blocks IL-1 binding to the IL-1RtII.

MeSH Terms
Binding, Competitive Cross-Linking Reagents Electrophoresis, Polyacrylamide Gel Humans Interleukin-1/antagonists & inhibitors,metabolism Lymphoma, B-Cell/metabolism,pathology Neutrophils/metabolism Precipitin Tests Receptors, Immunologic/antagonists & inhibitors,metabolism Receptors, Interleukin-1 Recombinant Proteins/antagonists & inhibitors,metabolism Tumor Cells, Cultured
Chemicals
Cross-Linking Reagents Interleukin-1 Receptors, Immunologic Receptors, Interleukin-1 Recombinant Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Granowitz E V
Department of Medicine, New England Medical Center Hospitals, Boston, Massachusetts 02111.
Clark B D
Mancilla J
Dinarello C A
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1991-08-05
Pages
14147-50
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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