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Interleukin-18 binding protein (IL-18BP) is a constitutively secreted glycoprotein that acts as a natural antagonist for interleukin-18 (IL-18) by preventing interaction between IL-18 and its receptors. Through this binding, IL-18BP neutralizes the proinflammatory role of IL-18 in cell-mediated immune responses, resulting in reduced IFN-gamma production by T helper type I cells and inhibition of allospecific cytotoxic T lymphocyte (CTL) activity through augmented natural killer (NK) cell cytotoxicity. As an inhibitor of IL-18 and an essential component of skin homeostasis, IL-18BP has been linked to a variety of diseases, including eczema, asthma, and the autoimmune condition, Crohn's disease. The upregulation of IL-18BP by keratinocytes expressing the human papillomavirus (HPV) E7 oncoprotein has been shown to decrease IL-18-induced IFN-gamma production and IL-18-mediated T cell activation. Elevated levels of IL-18 and IL-18BP, as well as proinflammatory cytokines IFN-gamma, TNF-alpha, IL-1beta and IL-8, have been linked to chronic inflammation and observed in macrophages (including Kupffer cells) isolated from lesions and intestinal tissues of Crohn's disease patients. As a member of the immunoglobulin-like class of receptors, IL-18BP contains a single immunoglobulin (Ig) domain; although two (b and d) of the four identified human isoforms (a-d) contain incomplete domains that greatly reduce their binding affinity.
Igifbp; Il18bp; IL-18BP; IL18BPa; interferon gamma inducing factor binding protein; interferon gamma-inducing factor-binding protein; interleukin 18 binding protein; interleukin-18 binding protein; interleukin-18-binding protein; MC51L-53L-54L homolog gene product; MC54L; Tadekinig-alfa
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