Premium
The first two N‐terminal immunoglobulin‐like domains of soluble human IL‐1 receptor type II are sufficient to bind and neutralize IL‐1β
Author(s) -
Kollewe Christian,
Neumann Detlef,
Martin Michael U
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02345-0
Subject(s) - receptor , antibody , extracellular , chemistry , dissociation constant , interleukin 1 receptor , recombinant dna , biochemistry , interleukin , immunology , biology , cytokine , gene
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 N‐terminal Ig‐like domains. Both forms bound IL‐1β with a dissociation constant ( K d ) of 200 pM and neutralized IL‐1β in a bioassay. They did not bind or neutralize IL‐1α. This demonstrates that the two Ig‐like domains of shIL‐1RII are sufficient to bind IL‐1β with an affinity comparable to full length shIL‐1RII. This suggests that this short form of shIL‐1RII contributes to the anti‐inflammatory effect of soluble IL‐1 receptors in vivo.