Research highlight
Microarray study with the IL-18 responsive cell line discovered a novel cytokine Interleukin-32. Interleukin (IL)-32 has the ability to induce various cytokines including human TNFメ and IL-8 as well as mouse TNFメ and MIP-2. The induction of TNFメ by IL-32 suggests that IL-32 plays an important role in autoimmune/inflammatory diseases since the blockade of TNFメ activity is a highly effective therapeutic approach in rheumatoid arthritis, Crohn¨s Disease, and psoriasis. As with many cytokines, an abnormality of IL-32 regulation may contribute to health and disease.
The identification of the IL-32 receptor components by IL-32 ligand affinity chromatography, functional characterization of the different splice variants by protein expression, and analyzing the variation of IL-32 expression are the objective of research goals to understand a precise role of IL-32 in the network of cytokine biology. We expect IL-32 to have a distinct receptor, since the cytokine does not share sequence homology with other known cytokine families. We will test the hypothesis that an IL-32 receptor exists. How can this IL-32 receptor be identified? Cytokine receptors have been isolated using ligand-affinity columns, for example tumor necrosis factor (TNF)-alpha binding protein, Interferon-alpha/beta receptor (IFNメR2), and IL-18 binding protein. We will use IL-32 ligand affinity column to isolate the putative IL-32 receptor with the use of different protein sources.
In addition, human IL 32 has six splice variants due to mRNA splicing. Recently, we identified the most active IL-32ϒ isoform and developed several dozen monoclonal antibodies by using recombinant IL-32ϒ protein as antigen. We expect that those monoclonal antibodies will be useful for developing IL-32 ELISA kit and immunoprecipitating IL-32 cell surface receptor complex.