Retention of ligand binding activity by the extracellular domain of the IL-1 receptor.
The IL-1R on murine T cells is an 80-kDa cell surface glycoprotein which binds both IL-1 alpha and IL-1 beta. We have recently isolated a cDNA clone encoding this molecule. From the primary sequence mature receptor is predicted to be a 557 residue integral membrane protein with a 319 residue carbohydrate-rich extracellular region. We have constructed a cDNA clone encoding this region of the protein (residues 1 to 316). Expression of this cDNA in HeLa cells leads to secretion of a soluble IL-1 alpha binding protein into the culture medium. Quantitative binding experiments with the truncated receptor show that it possesses IL-1 binding properties which are indistinguishable from those of full length IL-1R. Gel filtration chromatography experiments show that a complex can be formed between a single truncated receptor molecule and a single IL-1 alpha molecule.
Dower
S K
SK
Immunex Corporation, Seattle, WA 98101.
Wignall
J M
JM
Schooley
K
K
McMahan
C J
CJ
Jackson
J L
JL
Prickett
K S
KS
Lupton
S
S
Cosman
D
D
Sims
J E
JE
D000818:Animals; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005109:Extracellular Matrix / Q000032:analysis / Q000378:metabolism*; D006801:Humans; D007375:Interleukin-1 / Q000378:metabolism*; D051379:Mice; D008970:Molecular Weight; D011869:Radioligand Assay; D011971:Receptors, Immunologic / Q000032:analysis / Q000378:metabolism*; D017472:Receptors, Interleukin-1; D011994:Recombinant Proteins / Q000032:analysis / Q000378:metabolism; D012995:Solubility
D007375:Interleukin-1; D011971:Receptors, Immunologic; D017472:Receptors, Interleukin-1; D011994:Recombinant Proteins