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- W2093778832 abstract "IL-18 is a proinflammatory cytokine that is important for host defense, but is also involved in the pathogenesis of a number of disease processes, ranging from autoimmune disorders to atherosclerosis . IL-18 binding protein (IL-18BP) is a constitutively expressed glycoprotein that specifically neutralizes the effects of IL-18, resulting in decreased production of IFN-γ and reduction in Th1 immune responses. In this study we cloned and sequenced a full-length cDNA of the rhesus IL-18BP (RhIL-18BP) from the spleen of rhesus macaques (Macaca mulatta) and compared its nucleotide and amino acid sequences to the functional murine and human IL-18BP orthologues. In addition, we fused RhIL-18BP to the Fc portion of human IgG1 to make recombinant RhIL-18BP·Fcγ1 in order to facilitate its detection by Western blot analysis and determined the approximate molecular weight of RhIL-18BP·Fcγ1 to be 66 kD. With this fusion protein , we showed that RhIL-18BP was functional and could significantly reduce murine IL-18 and LPS-induced IFN-γ production by murine splenocytes . Furthermore, we demonstrated the expression of IL-18BP in atherosclerotic lesions in a rhesus model of atherosclerosis, underscoring the need to fully understand the role of this protein as a primary negative regulator of IL-18 in multiple disease processes." @default.
- W2093778832 created "2016-06-24" @default.
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- W2093778832 date "2010-09-01" @default.
- W2093778832 modified "2023-10-14" @default.
- W2093778832 title "Cloning and characterization of rhesus IL-18 binding protein, a natural antagonist to IL-18" @default.
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- W2093778832 doi "https://doi.org/10.1016/j.cyto.2010.05.010" @default.
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