The first two N-terminal immunoglobulin-like domains of soluble human IL-1 receptor type II are sufficient to bind and neutralize IL-1beta.
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-1beta with a dissociation constant (K(d)) of 200 pM and neutralized IL-1beta in a bioassay. They did not bind or neutralize IL-1alpha. This demonstrates that the two Ig-like domains of shIL-1RII are sufficient to bind IL-1beta 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.
Kollewe
C
C
Pharmacology OE 5320, Hannover Medical School, D-30623, Hannover, Germany.
Neumann
D
D
Martin
M U
MU
D001665:Binding Sites; D002460:Cell Line; D003001:Cloning, Molecular; D006801:Humans; D007136:Immunoglobulins / Q000737:chemistry; D007375:Interleukin-1 / Q000378:metabolism*; D007668:Kidney; D007700:Kinetics; D017472:Receptors, Interleukin-1 / Q000737:chemistry* / Q000502:physiology*; D053574:Receptors, Interleukin-1 Type II; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D007136:Immunoglobulins; D007375:Interleukin-1; D017472:Receptors, Interleukin-1; D053574:Receptors, Interleukin-1 Type II; D011994:Recombinant Proteins