Interleukins (IL) are immunomodulatory proteins that elicit a wide array of responses in cells and tissues. Interleukin 37 (IL-37, IL-1 F7) is a member of the IL-1 family. There are five isoforms of IL-37 (a-e) of which transcript IL-37b is known to be functional (Sharma et al. 2008). This isoform is represented in UniProt as the canonical form of IL-37 and in Reactome as the full length, unprocessed form of IL-37. Like several other IL-1 family members, IL-37 is synthesized as a precursor that requires processing (primarily by caspase 1) to attain full receptor agonist or antagonist function. The putative caspase 1 cleavage site is at aspartic acid 20 (Kumar et al. 2002). Both full length and cleaved IL-37 can be secreted from the cytosol to the extracellular space via a mechanism dependent on caspase 1 cleavage of IL-37 (Bulau A M et al. 2014).
Dinarello, CA, Bufler, P, Li, S, Rubartelli, A, Fink, M, Bulau, AM, Schwerd, T, Mansell, A, Nold, MF, Hong, J, Nold-Petry, CA
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