Retention of ligand binding activity by the extracellular domain of the IL-1 receptor |
| |
Authors: | S K Dower J M Wignall K Schooley C J McMahan J L Jackson K S Prickett S Lupton D Cosman J E Sims |
| |
Affiliation: | Immunex Corporation, Seattle, WA 98101. |
| |
Abstract: | 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. |
| |
Keywords: | |
|