Abstract
Interleukin-37 (IL-37) is an IL-1 family cytokine discovered in recent years and has 5 different isoforms. As an immunosuppressive factor, IL-37 can suppress excessive immune response. IL-37 plays a role in protecting the body against endotoxin shock, ischemia-reperfusion injury, autoimmune diseases, and cardiovascular diseases. In addition, IL-37 has a potential antitumor effect. IL-37 and its receptors may serve as novel targets for the study, diagnosis, and treatment of immune-related diseases and tumors.
Highlights
Interleukin-37 (IL-37) was first discovered and identified through computational sequence analysis by Kumar et al [1] in 2000
IL-37 forms complex with Smad3 to achieve nuclear translocation, which in turn regulates gene transcription, cell metabolism, cell proliferation, and cytokine expression and inhibits the activity of Dendritic cells (DCs)
IL-37 acts as an immunosuppressive agent by binding to IL18Rα to form complex with IL-18BP, so as to achieve the role of immune suppression by inhibiting the synthesis of IFN-γ and suppressing signal transduction after Toll-like receptor (TLR)
Summary
Interleukin-37 (IL-37) was first discovered and identified through computational sequence analysis by Kumar et al [1] in 2000. IL-37d (exons 1, 4, 5, and 6) encodes the 12β-strand-containing protein structure, suggesting that these two subtypes have biological functions [4, 11]. IL-37c (exons 1, 2, 5, and 6) and IL-37e (exons 1, 5, and 6) do not encode β-clover secondary structure due to lack of exon 4, so they may do not have biological functions [4, 11]. IL-37c shares a common N-terminal sequence with IL37b and IL-37d and competes with IL-37b and IL-37d precursors for the same cleavage enzyme target; whereas IL-37c has no biological function, production of precursor IL-37c is recognized as a mechanism of downregulation of IL-37b and IL-37d [4].
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