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p38-MAPK signals su...
p38-MAPK signals survival by phosphorylation of caspase-8 and caspase-3 in human neutrophils
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- Alvarado-Kristensson, Maria (författare)
- Lund University,Lunds universitet,Experimentell patologi, Malmö,Forskargrupper vid Lunds universitet,Molekylär patologi, Malmö,Experimental Pathology, Malmö,Lund University Research Groups,Molecular Pathology, Malmö
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- Melander, Fredrik (författare)
- Lund University,Lunds universitet,Experimentell patologi, Malmö,Forskargrupper vid Lunds universitet,Experimental Pathology, Malmö,Lund University Research Groups
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- Leandersson, Karin (författare)
- Lund University,Lunds universitet,Experimentell patologi, Malmö,Forskargrupper vid Lunds universitet,Experimental Pathology, Malmö,Lund University Research Groups
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- Rönnstrand, Lars (författare)
- Lund University,Lunds universitet,Institutionen för translationell medicin,Medicinska fakulteten,Department of Translational Medicine,Faculty of Medicine
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- Wernstedt, Christer (författare)
- Uppsala universitet,Ludwiginstitutet för cancerforskning
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- Andersson, Tommy (författare)
- Lund University,Lunds universitet,Experimentell patologi, Malmö,Forskargrupper vid Lunds universitet,Experimental Pathology, Malmö,Lund University Research Groups
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(creator_code:org_t)
- 2004-02-17
- 2004
- Engelska.
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Ingår i: Journal of Experimental Medicine. - : Rockefeller University Press. - 0022-1007 .- 1540-9538. ; 199:4, s. 449-458
- Relaterad länk:
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http://www.ncbi.nlm....
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http://jem.rupress.o...
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https://portal.resea... (primary) (free)
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http://www.jem.org/c...
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http://dx.doi.org/10...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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https://lup.lub.lu.s...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Klinisk medicin -- Cancer och onkologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Clinical Medicine -- Cancer and Oncology (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Läkemedelskemi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Medicinal Chemistry (hsv//eng)
Nyckelord
- 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
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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