IL-33, a new member of the IL-1F, is widely expressed throughout the body and can be up-regulated by stimulation with proinflammatory factors. It has been identified as a functional ligand for the plasma membrane receptor complex that is a heterodimer consisting of membrane-bound ST2L, which is a member of the IL-1R family, and IL-1RAcP. IL-33 is crucial for the induction of Th2 immune responses. Additionally, under other circumstances, it can also act as an endogenous danger signal. Recently, many studies have demonstrated that IL-33 may be related to the development and progression of fibrotic diseases. It has proinflammatory effects in some fibrotic diseases but has anti-inflammatory effects in others. In this review, the biologic characteristics of IL-33 and the role of the IL-33/ST2 signaling pathway in various fibrotic diseases will be discussed. We hope this overview will provide new insights for the treatment of these diseases.
Interleukin (IL)-38 is the latest member of the IL-1 cytokine family. However, as a result of lacking efficient method to generate relatively large quantity of IL-38, its precise functions are poorly understood. In the present study, the cloning, expression, purification, and activity analysis of recombinant human IL-38 was described. Human IL-38 cDNA was cloned into the prokaryotic expression vector pET-44. The recombinant IL-38 containing a C-hexahistidine tag was expressed in Escherichia coli BL21 (DE3) which induced by isopropyl-β-D-thiogalactoside. The expressed fusion protein was purified by Ni-NTA affinity chromatography. IL-38 protein was largely found in the soluble fraction. The purified IL-38 appeared a single band on SDS-PAGE, the yield of IL-38 was 4 mg from 1 L of bacterial culture, and the purity was more than 98% with low endotoxin level (<0.1 EU/μg). Western blotting confirmed the identity of the purified protein. Activity analysis showed that IL-38 can inhibit effectively the expression of proinflammatory cytokines, such as tumor necrosis factor-α, IL-1β, IL-17, and monocyte chemoattractant protein-1 in lipopolysaccharide-activated THP-1 cells. The production and characterization of biologically active IL-38 will be beneficial for its potential role in clinical applications.
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