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rdf:type |
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lifeskim:mentions |
umls-concept:C0022702,
umls-concept:C0023810,
umls-concept:C0024426,
umls-concept:C0056695,
umls-concept:C0079784,
umls-concept:C0085828,
umls-concept:C0175697,
umls-concept:C0205263,
umls-concept:C0287531,
umls-concept:C0851285,
umls-concept:C1333257,
umls-concept:C1514485,
umls-concept:C1705047,
umls-concept:C1879547,
umls-concept:C2697656
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pubmed:issue |
7
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pubmed:dateCreated |
2009-7-14
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pubmed:abstractText |
MAPK phosphatase-1 (MKP-1) is a protein phosphatase that plays a crucial role in innate immunity. This phosphatase inactivates ERK1/2, which are involved in two opposite functional activities of the macrophage, namely proliferation and activation. Here we found that although macrophage proliferation and activation induce MKP-1 with different kinetics, gene expression is mediated by the proximal promoter sequences localized between -380 and -180 bp. Mutagenesis experiments of the proximal element determined that CRE/AP-1 is required for LPS- or M-CSF-induced activation of the MKP-1 gene. Moreover, the results from gel shift analysis and chromatin immunoprecipitation indicated that c-Jun and CREB bind to the CRE/AP-1 box. The distinct kinetics shown by M-CSF and LPS correlates with the induction of JNK and c-jun, as well as the requirement for Raf-1. The signal transduction pathways that activate the induction of MKP-1 correlate kinetically with induction by M-CSF and LPS.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1521-4141
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
39
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1902-13
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:19585511-Animals,
pubmed-meshheading:19585511-Binding Sites,
pubmed-meshheading:19585511-Blotting, Western,
pubmed-meshheading:19585511-Bone Marrow Cells,
pubmed-meshheading:19585511-Cell Proliferation,
pubmed-meshheading:19585511-Chromatin Immunoprecipitation,
pubmed-meshheading:19585511-Cyclic AMP Response Element-Binding Protein,
pubmed-meshheading:19585511-Dual Specificity Phosphatase 1,
pubmed-meshheading:19585511-Electrophoretic Mobility Shift Assay,
pubmed-meshheading:19585511-Gene Expression,
pubmed-meshheading:19585511-JNK Mitogen-Activated Protein Kinases,
pubmed-meshheading:19585511-Kinetics,
pubmed-meshheading:19585511-Lipopolysaccharides,
pubmed-meshheading:19585511-Macrophage Activation,
pubmed-meshheading:19585511-Macrophage Colony-Stimulating Factor,
pubmed-meshheading:19585511-Macrophages,
pubmed-meshheading:19585511-Mice,
pubmed-meshheading:19585511-Mice, Inbred BALB C,
pubmed-meshheading:19585511-Protein Binding,
pubmed-meshheading:19585511-Proto-Oncogene Proteins c-jun,
pubmed-meshheading:19585511-Proto-Oncogene Proteins c-raf,
pubmed-meshheading:19585511-RNA, Small Interfering,
pubmed-meshheading:19585511-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:19585511-Transcription Factor AP-1,
pubmed-meshheading:19585511-Transfection
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pubmed:year |
2009
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pubmed:articleTitle |
CREB and AP-1 activation regulates MKP-1 induction by LPS or M-CSF and their kinetics correlate with macrophage activation versus proliferation.
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pubmed:affiliation |
Institute for Research in Biomedicine, University of Barcelona, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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