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A DNA sequence encoding the signal peptide and extracellular domain of human Interleukin 10 receptor alpha (IL-10 R alpha) (aa 1-232) was fused to the Fc region of human IgG1 (aa 93-330). The chimeric protein was expressed in modified human 293 cells.

Interleukin 10 (IL-10) is a pleiotropic cytokine that regulates multiple immune responses through actions on T cells, B cells, macrophage/monocytes and antigen presenting cells (APC) and generally skews the immune response from TH1 to TH2. IL-10 may suppress immune responses by inhibiting expression of IL-1a, IL-1b, IL-6, IL-8, TNF-a, GM-CSF and G-CSF in activated monocytes and activated macrophages. IL-10 also suppresses IFN-g production by NK cells. The biological effects of IL-10 are mediated through binding to the IL-10 receptor (IL-10 R) complex, which belongs to the class II cytokine receptor family. The IL-10R complex is a heterodimer comprising of the IL-10 R alpha chain (IL-10 Ra) and the interleukin 10 receptor beta chain (IL-10 Rb), which is shared by cytokine receptors for IL-22, IL-28 and IL-29. The IL-10 R is expressed on the majority of leukocytes including T cells, NK cells, macrophage/monocytes, B cells, neutrophils and dendritic cells. For a recent review on IL-10 and the IL-10 receptor, please refer to Mocellin et al., (2004) Cytokine Growth Factor Rev. 15(1): 61-76.