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p38-MAPK signals survival by phosphorylation of caspase-8 and caspase-3 in human neutrophils
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2004 (English)In: Journal of Experimental Medicine, ISSN 0022-1007, E-ISSN 1540-9538, Vol. 199, no 4, 449-458 p.Article in journal (Refereed) Published
Abstract [en]

Neutrophil apoptosis occurs both in the bloodstream and in the tissue and is considered essential for the resolution of an inflammatory process. Here, we show that p38-mitogen-activated protein kinase (MAPK) associates to caspase-8 and caspase-3 during neutrophil apoptosis and that p38-MAPK activity, previously shown to be a survival signal in these primary cells, correlates with the levels of caspase-8 and caspase-3 phosphorylation. In in vitro experiments, immunoprecipitated active p38-MAPK phosphorylated and inhibited the activity of the active p20 subunits of caspase-8 and caspase-3. Phosphopeptide mapping revealed that these phosphorylations occurred on serine-364 and serine-150, respectively. Introduction of mutated (S150A), but not wild-type, TAT-tagged caspase-3 into primary neutrophils made the Fas-induced apoptotic response insensitive to p38-MAPK inhibition. Consequently, p38-MAPK can directly phosphorylate and inhibit the activities of caspase-8 and caspase-3 and thereby hinder neutrophil apoptosis, and, in so doing, regulate the inflammatory response.

Place, publisher, year, edition, pages
2004. Vol. 199, no 4, 449-458 p.
Keyword [en]
Apoptosis, Caspases/antagonists & inhibitors/*blood, Cell Survival/physiology, Humans, Inflammation/blood, Mitogen-Activated Protein Kinases/*blood, Neutrophils/cytology/*enzymology, Phosphorylation, Research Support; Non-U.S. Gov't, Signal Transduction/physiology, p38 Mitogen-Activated Protein Kinases
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Medical and Health Sciences
Identifiers
URN: urn:nbn:se:uu:diva-72995DOI: 10.1084/jem.20031771PubMedID: 14970175OAI: oai:DiVA.org:uu-72995DiVA: diva2:100906
Available from: 2005-05-31 Created: 2005-05-31 Last updated: 2017-12-14Bibliographically approved

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Wernstedt, Christer

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