Ali, Shafaqat and Nguyen, Dang Quan and Falk, Werner and Martin, Michael Uwe (2010) Caspase 3 inactivates biologically active full length interleukin-33 as a classical cytokine but does not prohibit nuclear translocation. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 391 (3). pp. 1512-1516. ISSN 0006-291X, 1090-2104
Full text not available from this repository. (Request a copy)Abstract
IL-33 is a member of the IL-1 family of cytokines with dual function which either activates cells via the IL-33 receptor in a paracrine fashion or translocates to the nucleus to regulate gene transcription in an intracrine manner. We show that full length murine IL-33 is active as a cytokine and that it is not processed by caspase I to mature IL-33 but instead cleaved by caspase 3 at aa175 to yield two products which are both unable to bind to the IL-33 receptor. Full length IL-33 and its N-terminal caspase 3 breakdown product, however, translocate to the nucleus. Finally, bioactive IL-33 is not released by cells constitutively or after activation. This suggests that IL-33 is not a classical cytokine but exerts its function in the nucleus of intact cells and only activates others cells via its receptor as an alarm mediator after destruction of the producing cell. (c) 2009 Elsevier Inc. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | RECEPTOR ACCESSORY PROTEIN; HUMAN MAST-CELLS; CUTTING EDGE; IL-33; ST2; ACTIVATION; MATURATION; LIGAND; Interleukin-33; Caspase 3; IL-1 Family cytokine; IL-33 Processing |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Innere Medizin I |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 10 Aug 2020 08:28 |
| Last Modified: | 10 Aug 2020 08:28 |
| URI: | https://pred.uni-regensburg.de/id/eprint/25297 |
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