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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2000-8-24
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pubmed:abstractText |
The generation of proinflammatory eicosanoids in response to tumor necrosis factor (TNF) involves the activation of cytosolic phospholipase A(2) (cPLA(2)), presumably by phosphorylation through extracellular signal-regulated kinases (ERK). Earlier results had suggested that a pathway involving the p55 TNF receptor (TNF-R55), neutral sphingomyelinase (N-SMase), and c-Raf-1 activates ERK and cPLA(2). We have previously shown that a cytoplasmic region of TNF-R55 distinct from the death domain regulates the activation of N-SMase through binding of the adapter protein FAN. Analysis of embryonal fibroblasts from FAN knockout mice revealed that TNF-induced activation of both ERK and cPLA(2) occurs without involvement of FAN. Furthermore, we provide evidence that the TNF-dependent activation of ERK and cPLA(2) requires the intact death domain of TNF-R55. Finally, we demonstrate that in murine fibroblasts cPLA(2) is phosphorylated in response to TNF solely by ERK, but not by p38 mitogen-activated protein kinase, suggesting a signaling pathway from TNF-R55 via the death domain to ERK and cPLA(2).
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Arachidonic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Ionophores,
http://linkedlifedata.com/resource/pubmed/chemical/MAP Kinase Kinase Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/MAP3K1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Map3k1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Nsmaf protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor...,
http://linkedlifedata.com/resource/pubmed/chemical/Sphingomyelin Phosphodiesterase,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/p38 Mitogen-Activated Protein...
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2000 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
506-12
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:10913368-Animals,
pubmed-meshheading:10913368-Antigens, CD,
pubmed-meshheading:10913368-Arachidonic Acid,
pubmed-meshheading:10913368-B-Lymphocytes,
pubmed-meshheading:10913368-Cells, Cultured,
pubmed-meshheading:10913368-Cytoplasm,
pubmed-meshheading:10913368-Drug Synergism,
pubmed-meshheading:10913368-Fibroblasts,
pubmed-meshheading:10913368-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:10913368-Ionophores,
pubmed-meshheading:10913368-MAP Kinase Kinase Kinase 1,
pubmed-meshheading:10913368-Mice,
pubmed-meshheading:10913368-Mice, Knockout,
pubmed-meshheading:10913368-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:10913368-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:10913368-Mitogen-Activated Protein Kinases,
pubmed-meshheading:10913368-Phospholipases A,
pubmed-meshheading:10913368-Phosphorylation,
pubmed-meshheading:10913368-Protein Structure, Tertiary,
pubmed-meshheading:10913368-Protein-Serine-Threonine Kinases,
pubmed-meshheading:10913368-Proteins,
pubmed-meshheading:10913368-Receptors, Tumor Necrosis Factor,
pubmed-meshheading:10913368-Receptors, Tumor Necrosis Factor, Type I,
pubmed-meshheading:10913368-Sequence Deletion,
pubmed-meshheading:10913368-Signal Transduction,
pubmed-meshheading:10913368-Sphingomyelin Phosphodiesterase,
pubmed-meshheading:10913368-Tetradecanoylphorbol Acetate,
pubmed-meshheading:10913368-Tumor Necrosis Factor-alpha,
pubmed-meshheading:10913368-p38 Mitogen-Activated Protein Kinases
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pubmed:year |
2000
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pubmed:articleTitle |
Activation of ERK1/2 and cPLA(2) by the p55 TNF receptor occurs independently of FAN.
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pubmed:affiliation |
Institut für Immunologie, Christian-Albrechts-Universität Kiel, Brunswiker Strasse 4, Kiel, 24105, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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