Serum amyloid A mediates human neutrophil production of reactive oxygen species through a receptor independent of formyl peptide receptor like-1

Autor: Claes Dahlgren, Anna Karlsson, Lena Björkman, Jennie Karlsson, Huamei Fu, François Boulay, Marie-Josèphe Rabiet, Johan Bylund
Přispěvatelé: Department of Rheumatology & Inflammation Research, University of Gothenburg (GU), Health Care Research Unit, Sahlgrenska University Hospital [Gothenburg]-University of Gothenburg (GU), Umeå Plant Science Centre, Department of Plant Physiology, Umeå University, Biochimie et biophysique des systèmes intégrés (BBSI), Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), University of Gothenburg (GU)-Sahlgrenska University Hospital [Gothenburg]
Jazyk: angličtina
Rok vydání: 2008
Předmět:
Lipopolysaccharides
Phosphatidylinositol 4
5-Diphosphate
MESH: Signal Transduction
MESH: Serum Amyloid A Protein
Neutrophils
MESH: Receptors
Formyl Peptide
MESH: Receptors
Lipoxin
MESH: Receptors
G-Protein-Coupled
Pharmacology
MESH: Neutrophils
[SDV.IMM.II]Life Sciences [q-bio]/Immunology/Innate immunity
Receptors
G-Protein-Coupled
0302 clinical medicine
Immunology and Allergy
Receptors
Lipoxin
Receptor
MESH: Peptide Fragments
MESH: NADPH Oxidase
Respiratory Burst
0303 health sciences
MESH: Reactive Oxygen Species
Transfection
MESH: Phosphatidylinositol 4
5-Diphosphate
3. Good health
MESH: Respiratory Burst
MESH: Oligopeptides
Oligopeptides
Signal Transduction
medicine.medical_specialty
MESH: Enzyme Activation
Recombinant Fusion Proteins
Immunology
HL-60 Cells
Biology
MESH: Pertussis Toxin
Pertussis toxin
MESH: Calcium Signaling
Proinflammatory cytokine
03 medical and health sciences
MESH: HL-60 Cells
Internal medicine
medicine
MESH: Recombinant Fusion Proteins
Humans
Calcium Signaling
Serum amyloid A
Gelsolin
030304 developmental biology
G protein-coupled receptor
Organelles
Serum Amyloid A Protein
Formyl peptide receptor
MESH: Humans
Tumor Necrosis Factor-alpha
MESH: Transfection
NADPH Oxidases
Chemotaxis
Cell Biology
Receptors
Formyl Peptide
Peptide Fragments
Enzyme Activation
stomatognathic diseases
Endocrinology
MESH: Gelsolin
Pertussis Toxin
MESH: Tumor Necrosis Factor-alpha
MESH: Lipopolysaccharides
Reactive Oxygen Species
030215 immunology
MESH: Organelles
Zdroj: Journal of Leukocyte Biology
Journal of Leukocyte Biology, 2008, 83 (2), pp.245-53. ⟨10.1189/jlb.0607-408⟩
Journal of Leukocyte Biology, Society for Leukocyte Biology, 2008, 83 (2), pp.245-53. ⟨10.1189/jlb.0607-408⟩
ISSN: 0741-5400
DOI: 10.1189/jlb.0607-408⟩
Popis: Serum amyloid A (SAA) is one of the acute-phase reactants, a group of plasma proteins that increases immensely in concentration during microbial infections and inflammatory conditions, and a close relationship between SAA levels and disease activity in rheumatoid arthritis (RA) has been observed. RA is an inflammatory disease, where neutrophils play important roles, and SAA is thought to participate in the inflammatory reaction by being a neutrophil chemoattractant and inducer of proinflammatory cytokines. The biological effects of SAA are reportedly mediated mainly through formyl peptide receptor like-1 (FPRL1), a G protein-coupled receptor (GPCR) belonging to the formyl peptide receptor family. Here, we confirmed the affinity of SAA for FPRL1 by showing that stably transfected HL-60 cells expressing FPRL1 were activated by SAA and that the response was inhibited by the use of the FPRL1-specific antagonist WRWWWW (WRW4). We also show that SAA activates the neutrophil NADPH-oxidase and that a reserve pool of receptors is present in storage organelles mobilized by priming agents such as TNF-α and LPS from Gram-negative bacteria. The induced activity was inhibited by pertussis toxin, indicating the involvement of a GPCR. However, based on FPRL1-specific desensitization and use of FPRL1 antagonist WRW4, we found the SAA-mediated effects in neutrophils to be independent of FPRL1. Based on these findings, we conclude that SAA signaling in neutrophils is mediated through a GPCR, distinct from FPRL1. Future identification and characterization of the SAA receptor could lead to development of novel, therapeutic targets for treatment of RA.
Databáze: OpenAIRE
Externí odkaz: