Source:http://linkedlifedata.com/resource/pubmed/id/21472666
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2011-6-9
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pubmed:abstractText |
Proinflammatory cell activation via the receptor for advanced glycation end products (RAGE) pathway may play a central pathogenetic role in atherosclerosis. Since S100A8/A9 was recently identified as ligand of RAGE, we determined the effects of proinflammatory cytokines on RAGE-mediated induction of gene expression of S100A8 and S100A9. mRNA levels of S100A8 and S100A9 were upregulated following cytokine stimulation with IL-6 (1, 10, 100?ng/ml) or TNF? (10?ng/ml) in human THP-1 cells. Preincubation of cells with 2000?ng/ml AGE (advanced glycation end products) before cytokine stimulation resulted in upregulation of RAGE. Pretreatment of THP-1 with AGE followed by stimulation with IL-6 (10?ng/ml) or TNF? (10?ng/ml) further increased S100A8 and S100A9?mRNA expression and S100A8/A9 release into cell culture supernatant, as compared to pretreatment with non-glycated albumin as control. Binding of AGE to RAGE was blocked with a neutralizing anti-RAGE antibody. Normal mouse IgG served as control. Cytokine-stimulated induction of S100A8 and S100A9?mRNA levels as well as of S100A8/A9 release after preincubation of cells with AGE were significantly suppressed by RAGE blockade, indicating a RAGE-dependent pathway of AGE-mediated S100A8/A9 expression.The cytokine-induced potentiated S100A8 and S100A9 expression under conditions with a high AGE burden is able to aggravate proinflammatory conditions via activation of the RAGE pathway.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calgranulin A,
http://linkedlifedata.com/resource/pubmed/chemical/Calgranulin B,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-6,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/advanced glycosylation end-product...
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1439-3646
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pubmed:author | |
pubmed:copyrightInfo |
© J. A. Barth Verlag in Georg Thieme Verlag KG Stuttgart · New York.
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pubmed:issnType |
Electronic
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pubmed:volume |
119
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
353-7
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pubmed:meshHeading |
pubmed-meshheading:21472666-Animals,
pubmed-meshheading:21472666-Calcium-Binding Proteins,
pubmed-meshheading:21472666-Calgranulin A,
pubmed-meshheading:21472666-Calgranulin B,
pubmed-meshheading:21472666-Cell Line, Tumor,
pubmed-meshheading:21472666-Dose-Response Relationship, Drug,
pubmed-meshheading:21472666-Gene Expression Regulation, Leukemic,
pubmed-meshheading:21472666-Humans,
pubmed-meshheading:21472666-Interleukin-6,
pubmed-meshheading:21472666-Leukemia,
pubmed-meshheading:21472666-Mice,
pubmed-meshheading:21472666-Receptors, Immunologic,
pubmed-meshheading:21472666-Signal Transduction,
pubmed-meshheading:21472666-Tumor Necrosis Factor-alpha
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pubmed:year |
2011
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pubmed:articleTitle |
RAGE-dependent regulation of calcium-binding proteins S100A8 and S100A9 in human THP-1.
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pubmed:affiliation |
Medizinische Klinik mit Schwerpunkt Kardiologie und Angiologie, Charité - Universitätsmedizin Berlin, Campus Mitte, Germany. kai.eggers@charite.de
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pubmed:publicationType |
Journal Article
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