The first two N-terminal immunoglobulin-like domains of soluble human IL-1 receptor type II are sufficient to bind and neutralize IL-1 beta - Research portal of Justus Liebig University Giessen:

Journal article

The first two N-terminal immunoglobulin-like domains of soluble human IL-1 receptor type II are sufficient to bind and neutralize IL-1 beta

Authors list: Kollewe, C; Neumann, D; Martin, MU

Publication year: 2000

Pages: 189-193

Journal: FEBS Letters

Volume number: 487

Issue number: 2

ISSN: 0014-5793

DOI Link: https://doi.org/10.1016/S0014-5793(00)02345-0

Publisher: Wiley

Abstract:
Two forms of soluble human type II interleukin (IL)-1 receptor (shIL-1RII) were generated, one consisting of the complete extracellular three immunoglobulin (Ig)-like domains and one containing only the first two IV-terminal Ig-like domains. Both forms bound IL-1 beta with a dissociation constant (K-d) Of 200 pM and neutralized IL-1 beta in a bioassay. They did not bind or neutralize IL-1 alpha. This demonstrates that the two Ig-like domains of shIL-1RII are sufficient to bind IL-1 beta with an affinity comparable to full length shIK-1RII. This suggests that this short form of shIL-1RII contributes to the anti-inflammatory effect of soluble IL-1 receptors in vivo. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

Citation Styles

Harvard Citation style: Kollewe, C., Neumann, D. and Martin, M. (2000) The first two N-terminal immunoglobulin-like domains of soluble human IL-1 receptor type II are sufficient to bind and neutralize IL-1 beta, FEBS Letters, 487(2), pp. 189-193. https://doi.org/10.1016/S0014-5793(00)02345-0

APA Citation style: Kollewe, C., Neumann, D., & Martin, M. (2000). The first two N-terminal immunoglobulin-like domains of soluble human IL-1 receptor type II are sufficient to bind and neutralize IL-1 beta. FEBS Letters. 487(2), 189-193. https://doi.org/10.1016/S0014-5793(00)02345-0