Interleukin‐1 receptor accessory protein interacts with the type II interleukin‐1 receptor

FEBS Letters

Malinowsky, David¹  Bartfai, Tamas¹  Lundkvist, Johan¹  Layé, Sophie¹ 

[1] Department of Neurochemistry and Neurotoxicology, The Arrhenius Laboratories for Natural Sciences, Stockholm University, S-106 91 Stockholm, Sweden

关键词: Interleukin-1;    IL-1 receptor type II;    IL-1 receptor accessory protein;    Interaction;   

DOI  :  10.1016/S0014-5793(98)00467-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Stably transfected HEK-293 cells express on their surface the murine type II IL-1 receptor (mIL-1RII) as demonstrated by FACS analysis using the mAb 4E2, however binding of [¹²⁵I]-hrIL-1β to these cells is nearly absent. Saturable high affinity binding of [¹²⁵I]-hrIL-1β is observed when the murine IL-1 receptor accessory protein (mIL-1RAcP) is coexpressed with mIL-1RII. Binding of [¹²⁵I]-hrIL-1β to mIL-1RII-mIL-1RAcP complex can be inhibited either with antibodies to mIL-1RII (mAb 4E2), or by antibodies to mIL-1RAcP (mAb 4C5). The number of high affinity binding sites in cells stably transfected with the cDNA for mIL-1RII is dependent on the dose of cDNA for mIL-1RAcP used to transfect the cells. The high affinity complex between mIL-1RII and mIL-1RAcP is not preformed by interaction between the intracellular domains of these two transmembrane proteins, rather it appears to require the extracellular portions of mIL-1RII and mIL-1RAcP and the presence of a ligand. We suggest that in addition to its earlier described decoy receptor role, IL-1RII may modulate the responsiveness of cells to IL-1 by binding the IL-1RAcP in unproductive/non-signalling complexes and thus reducing the number of signalling IL-1RI-IL-1RAcP-agonist complexes when IL-1 is bound.

【 授权许可】

Unknown