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IL-33 Raises Alarm Immunity Volume 31, Issue 1, Pages 5-7 (July 2009)
Mohamed Lamkanfi, Vishva M. Dixit Immunity Volume 31, Issue 1, Pages 5-7 (July 2009) DOI: /j.immuni Copyright © 2009 Elsevier Inc. Terms and Conditions
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Figure 1 IL-33 Responses in Necrosis and Apoptosis
IL-33 is constitutively expressed in the nucleus of endothelial and epithelial cells, where it may be involved in regulating transcription through its amino-terminal homeodomain-like DNA-binding motif. Tissue damage during trauma or infection triggers secretion of full-length IL-33 from necrotic cells. Extracellular IL-33 engages the IL-1 receptor family member ST2. In association with an IL-1R accessory protein (IL-1RAcP), this leads to NF-κB-mediated secretion of proinflammatory and Th2 cell-associated cytokines from mast cells and other immune cells to alert the immune system and to promote the initiation of healing responses. During apoptosis, the executioner caspase-3 and -7 inactivate IL-33 by cleaving the carboxy-terminal IL-1-like β-trefoil domain. Although processed IL-33 is largely retained inside apoptotic bodies, caspase-mediated processing prevents accidentally released IL-33 from stimulating the ST2 receptor. Immunity , 5-7DOI: ( /j.immuni ) Copyright © 2009 Elsevier Inc. Terms and Conditions
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