|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
2003-12-3
|
|
pubmed:abstractText |
Recent advances in understanding the molecular basis for mammalian host immune responses to microbial invasion suggest that the first line of defense against microbes is the recognition of pathogen-associated molecular patterns by a set of germline-encoded receptors: the Toll-like receptors (TLRs). TLRs have been identified as being part of a large family of pathogen-recognition receptors that play a decisive role in the induction of both innate and adaptive immunity. Indeed, activation of T lymphocytes depends on their interaction with dendritic cells previously stimulated by TLR agonists such as bacterial lipopolysaccharide (LPS), a TLR-4 ligand. A novel PKC epsilon (epsilon) was recently found to be a critical component of TLR-4 signaling pathway and thereby to play a key role in macrophage and dendritic cell (DC) activation in response to LPS. Thus, controlling the kinase activity of PKC epsilon might represent an efficient strategy to prevent or treat certain inflammatory disorders of microbial origin.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-12,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/PRKCE protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Prkce protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C-epsilon,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/TLR4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptor 4,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptors
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Feb
|
|
pubmed:issn |
1357-2725
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
36
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
183-8
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:14643884-Animals,
pubmed-meshheading:14643884-Catalytic Domain,
pubmed-meshheading:14643884-Dendritic Cells,
pubmed-meshheading:14643884-Humans,
pubmed-meshheading:14643884-Inflammation,
pubmed-meshheading:14643884-Interleukin-12,
pubmed-meshheading:14643884-Ligands,
pubmed-meshheading:14643884-Lipopolysaccharides,
pubmed-meshheading:14643884-Macrophages,
pubmed-meshheading:14643884-Membrane Glycoproteins,
pubmed-meshheading:14643884-Mice,
pubmed-meshheading:14643884-Models, Biological,
pubmed-meshheading:14643884-Protein Kinase C,
pubmed-meshheading:14643884-Protein Kinase C-epsilon,
pubmed-meshheading:14643884-Protein Structure, Tertiary,
pubmed-meshheading:14643884-Receptors, Cell Surface,
pubmed-meshheading:14643884-Th1 Cells,
pubmed-meshheading:14643884-Toll-Like Receptor 4,
pubmed-meshheading:14643884-Toll-Like Receptors
|
|
pubmed:year |
2004
|
|
pubmed:articleTitle |
Protein kinase C epsilon: a new target to control inflammation and immune-mediated disorders.
|
|
pubmed:affiliation |
Laboratory of Experimental Immunology, Université Libre de Bruxelles, B-1070, Brussels, Belgium
|
|
pubmed:publicationType |
Journal Article,
Review
|
