Recombinant HBsAg, an apoptotic-like lipoprotein, interferes with the LPS-induced activation of ERK-1/2 and JNK-1/2 in monocytes
Autor: | Annelies Roobrouck, Peter Vanlandschoot, Geert Leroux-Roels, Freya Van Houtte |
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Rok vydání: | 2002 |
Předmět: |
MAPK/ERK pathway
Lipopolysaccharides Transcription Genetic p38 mitogen-activated protein kinases CD14 Biophysics Apoptosis Biology Biochemistry Peripheral blood mononuclear cell Monocytes Humans Mitogen-Activated Protein Kinase 9 Mitogen-Activated Protein Kinase 8 RNA Messenger Phosphorylation Molecular Biology Mitogen-Activated Protein Kinase 1 Hepatitis B Surface Antigens Mitogen-Activated Protein Kinase 3 Kinase Tumor Necrosis Factor-alpha NF-kappa B Cell Biology Molecular biology Recombinant Proteins Enzyme Activation Mitogen-activated protein kinase biology.protein Cytokines lipids (amino acids peptides and proteins) Tumor necrosis factor alpha Mitogen-Activated Protein Kinases Interleukin-1 |
Zdroj: | Biochemical and biophysical research communications. 297(3) |
ISSN: | 0006-291X |
Popis: | Yeast expressed Hepatitis B surface antigen (rHBsAg) binds to monocytes through interaction with the LPS binding protein (LBP) and the LPS receptor CD14. Charged phospholipids of rHBsAg determine the interaction with these proteins. Although attachment of rHBsAg resembles the pro-inflammatory binding of LPS to CD14, rHBsAg does not activate monocytes and even reduces the expression of pro-inflammatory cytokines by LPS-stimulated monocytes. It is reported here that addition of rHBsAg to LPS-stimulated PBMC often results in increased secretion of IL-10, suggesting a similarity between the interaction of monocytes with apoptotic cells and rHBsAg. Using THP-1 cells, it is shown that IL-10 is not necessary to reduce TNFalpha protein levels. Addition of rHBsAg to LPS-stimulated cells reduces TNFalpha mRNA levels, but does not affect phosphorylation of p65 NF-kappaB and p38 MAP kinase. Instead, a reduced phosphorylation of ERK-1/2 and JNK-1/2 MAP kinases is observed. |
Databáze: | OpenAIRE |
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