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

FEBS Letters

Martin, Michael U¹  Neumann, Detlef¹  Kollewe, Christian¹ 

[1] Pharmacology OE 5320, Hannover Medical School, D-30623 Hannover, Germany

关键词: Interleukin-1;    IL-1 receptor;    Soluble receptor;    Regulation of inflammation;    h;    human;    s;    soluble;    r;    recombinant;    R;    receptor;    IL;    interleukin;    Ig;    immunoglobulin;    HA;    hemagglutinin;    mAB;    monoclonal antibody;    PBS;    phosphate-buffered saline pH 7.4;   

DOI  :  10.1016/S0014-5793(00)02345-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown