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rdf:type |
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lifeskim:mentions |
umls-concept:C0023810,
umls-concept:C0024432,
umls-concept:C0031669,
umls-concept:C0205263,
umls-concept:C0205314,
umls-concept:C0256813,
umls-concept:C0679622,
umls-concept:C1314939,
umls-concept:C1366537,
umls-concept:C1367731,
umls-concept:C1704259,
umls-concept:C1705294,
umls-concept:C1705987,
umls-concept:C1879547
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pubmed:issue |
7
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pubmed:dateCreated |
2000-10-10
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pubmed:abstractText |
The activation of kinases of the mitogen-activated protein kinase superfamily initiated by lipopolysaccharide (LPS) plays an important role in transducing inflammatory signals. The pathway leading to the induction of stress-activated protein kinases in macrophages stimulated with LPS was investigated. The activation of Jun N-terminal kinases (JNK) by LPS is herbimycin sensitive. Using specific inhibitors, it was shown that the pathway involves the activation of phosphoinositide 3-kinase (PI 3-K). However, in contrast to previous reports, the small GTPases Cdc42 and Rac are not required downstream of PI 3-K for JNK activation. Instead, the phosphoinositides produced by PI 3-K stimulate protein kinase C (PKC) zeta activation through PDK1. In turn, activation of this atypical PKC leads to the stimulation of phosphatidylcholine phospholipase C (PC-PLC) and acidic sphingomyelinase (ASMase). It is therefore proposed that PKCzeta regulates the PC-PLC/ASMase pathway, and it is hypothesized that the resultant ceramide accumulation mediates the activation of the SEK/JNK module by LPS.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Androstadienes,
http://linkedlifedata.com/resource/pubmed/chemical/Benzoquinones,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/JNK Mitogen-Activated Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Lactams, Macrocyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/MAP Kinase Kinase 4,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Quinones,
http://linkedlifedata.com/resource/pubmed/chemical/Sphingomyelin Phosphodiesterase,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/cdc42 GTP-Binding Protein,
http://linkedlifedata.com/resource/pubmed/chemical/herbimycin,
http://linkedlifedata.com/resource/pubmed/chemical/phosphatidylcholine-specific...,
http://linkedlifedata.com/resource/pubmed/chemical/wortmannin
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-4971
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
96
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2592-8
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:11001916-Androstadienes,
pubmed-meshheading:11001916-Benzoquinones,
pubmed-meshheading:11001916-Cell Line,
pubmed-meshheading:11001916-Enzyme Activation,
pubmed-meshheading:11001916-Enzyme Inhibitors,
pubmed-meshheading:11001916-Isoenzymes,
pubmed-meshheading:11001916-JNK Mitogen-Activated Protein Kinases,
pubmed-meshheading:11001916-Lactams, Macrocyclic,
pubmed-meshheading:11001916-Lipopolysaccharides,
pubmed-meshheading:11001916-MAP Kinase Kinase 4,
pubmed-meshheading:11001916-Macrophages,
pubmed-meshheading:11001916-Mitogen-Activated Protein Kinase Kinases,
pubmed-meshheading:11001916-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:11001916-Protein Kinase C,
pubmed-meshheading:11001916-Quinones,
pubmed-meshheading:11001916-Signal Transduction,
pubmed-meshheading:11001916-Sphingomyelin Phosphodiesterase,
pubmed-meshheading:11001916-Type C Phospholipases,
pubmed-meshheading:11001916-cdc42 GTP-Binding Protein
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pubmed:year |
2000
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pubmed:articleTitle |
Lipopolysaccharide induces jun N-terminal kinase activation in macrophages by a novel Cdc42/Rac-independent pathway involving sequential activation of protein kinase C zeta and phosphatidylcholine-dependent phospholipase C.
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pubmed:affiliation |
Section of Cell Biology and Microbiology, Institute of Microbiology and Genetics, Vienna Biocenter, Vienna, Austria.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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