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Lipopolysaccharide-induced granule mobilization and priming of the neutrophil response to Helicobacter pylori peptide Hp(2-20), which activates formyl peptide receptor-like 1

Artikel i vetenskaplig tidskrift
Författare Johan Bylund
Anna Karlsson
F. Boulay
Claes Dahlgren
Publicerad i Infect Immun
Volym 70
Nummer/häfte 6
Sidor 2908-14
Publiceringsår 2002
Publicerad vid Institutionen för invärtesmedicin, Avdelningen för reumatologi och inflammationsforskning
Sidor 2908-14
Språk en
Länkar www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord Amino Acid Sequence, Anti-Bacterial Agents/*immunology, Bacterial Proteins/*immunology, Cells, Cultured, Gelatinases/immunology, Helicobacter pylori/*immunology, Humans, Lipopolysaccharides/*immunology/pharmacology, Macrophage-1 Antigen/immunology, Molecular Sequence Data, Neutrophils/drug effects/*immunology, Organelles, Peptide Fragments/*immunology, Peptides/immunology, Receptors, Complement 3b/immunology, Receptors, Formyl Peptide, Receptors, Immunologic/*immunology, *Receptors, Lipoxin, Receptors, Peptide/*immunology, Subcellular Fractions, Superoxides
Ämneskategorier Medicin och Hälsovetenskap

Sammanfattning

The cecropin-like bactericidal peptide Hp(2-20) from Helicobacter pylori induces activation of the NADPH oxidase in human neutrophils via formyl peptide receptor-like 1 (FPRL1) (J. Bylund, T. Christophe, F. Boulay, T. Nystrom, A. Karlsson, and C. Dahlgren, Antimicrob. Agents Chemother. 45:1700-1704, 2001). Here we investigated the ability of bacterial lipopolysaccharide (LPS) to prime this response. Neutrophils treated with LPS for 30 min at 37 degrees C produced substantially more superoxide anion than control cells upon stimulation with Hp(2-20). Hence, LPS primed the cells for subsequent stimulation through FPRL1. To study the molecular background of this priming phenomenon, we measured the degrees of granule mobilization and concomitant receptor upregulation to the cell surface in LPS-treated cells. Exposure of complement receptors 1 and 3 as well as the formyl peptide receptor (FPR) was markedly increased after LPS treatment. Since approximately 60% of the gelatinase granules were mobilized while the specific granules were retained, we hypothesized that the gelatinase granules were potential stores of FPRL1. The presence of FPRL1 mainly in the gelatinase granules was confirmed by Western blotting of subcellular fractions of resting neutrophils. These results suggest that the mechanism behind the LPS-induced priming of FPRL1-mediated responses lies at the level of granule (receptor) mobilization.

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