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. 2021 Nov 23;12:754702. doi: 10.3389/fimmu.2021.754702

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Copyright © 2021 Peñaloza, van der Geest, Ybe, Standiford and Lee

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Post-translational processing of human IL-36 cytokines by extracellular proteases. Human IL-36 cytokines are selectively cleaved and potentially activated by proteases. (A) IL-36α is cleaved extracellularly by neutrophil proteases Cathepsin G (CatG) and Neutrophil Elastase (NE). (B) IL-36β has been described to be N-terminally processed by CatG. (C) IL-36γ is selectively cleaved by Proteinase-3 (P3), NE, Cathepsin S (CatS), the Streptococcus pyogenes-derived protease SpeB, the Aspergillus fumigatus-derived protease F13 and the Pseudomonas aeruginosa-derived protease LasB. (D) IL-36Ra is cleaved and potentially activated by NE, CatG and P3. (E) The proteolytic cleavage of IL-36 cytokines can be regulated by the host glycoprotein thrombospondin-1, which has been shown to possess inhibitory properties against the host proteases NE and CatG, and against the bacterial protease LasB.