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The synthetic pepti...
The synthetic peptide Trp-Lys-Tyr-Met-Val-Met-NH2 specifically activates neutrophils through FPRL1/lipoxin A4 receptors and is an agonist for the orphan monocyte-expressed chemoattractant receptor FPRL2.
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Christophe, T (author)
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- Karlsson, Anna, 1967 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för invärtesmedicin, Avdelningen för reumatologi och inflammationsforskning,Institute of Internal Medicine, Dept of Rheumatology and Inflammation Research
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Dugave, C (author)
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Rabiet, M J (author)
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Boulay, F (author)
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- Dahlgren, Claes, 1949 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för invärtesmedicin, Avdelningen för reumatologi och inflammationsforskning,Institutionen för medicinsk mikrobiologi och immunologi,Institute of Internal Medicine, Dept of Rheumatology and Inflammation Research,Institute of Medical Microbiology/Immunology
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(creator_code:org_t)
- 2001
- 2001
- English.
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In: The Journal of biological chemistry. - 0021-9258. ; 276:24, s. 21585-93
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https://gup.ub.gu.se...
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https://doi.org/10.1...
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Abstract
Subject headings
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- Neutrophils express the G protein-coupled N-formyl peptide receptor (FPR) and its homologue FPRL1, whereas monocytes express FPR, FPRL1, and FPRL2, an orphan receptor sharing 83% amino acid identity with FPRL1. FPRL1 is a promiscuous receptor activated by serum amyloid A and by different synthetic peptides, including the hexapeptide Trp-Lys-Tyr-Met-Val-d-Met-NH(2) (WKYMVm). By measuring calcium flux in HL-60 cells transfected with FPR, FPRL1, or FPRL2, we show that WKYMVm activated all three receptors, whereas the l-conformer WKYMVM activated exclusively FPRL1 and FPRL2. The functionality of FPRL2 was further assessed by the ability of HL-60-FPRL2 cells to migrate toward nanomolar concentrations of hexapeptides. The half-maximal effective concentrations of WKYMVM for calcium mobilization in HL-60-FPRL1 and HL-60-FPRL2 cells were 2 and 80 nm, respectively. Those of WKYMVm were 75 pm and 3 nm. The tritiated peptide WK[3,5-(3)H(2)]YMVM bound to FPRL1 (K(D) approximately 160 nm), but not to FPR. The two conformers similarly inhibited binding of (125)I-labeled WKYMVm to FPRL2-expressing cells (IC(50) approximately 2.5-3 micrometer). Metabolic labeling with orthophosphoric acid revealed that FPRL1 was differentially phosphorylated upon addition of the l- or d-conformer, indicating that it induced different conformational changes. In contrast to FPRL1, FPRL2 was already phosphorylated in the absence of agonist and not evenly distributed in the plasma membrane of unstimulated cells. However, both receptors were internalized upon addition of either of the two conformers. Taken together, the results indicate that neutrophils are activated by WKYMVM through FPRL1 and that FPRL2 is a chemotactic receptor transducing signals in myeloid cells.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Immunologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Immunology in the medical area (hsv//eng)
Keyword
- Animals
- Calcium
- metabolism
- Calcium Signaling
- drug effects
- physiology
- Cell Line
- Chemotaxis
- drug effects
- physiology
- Chemotaxis
- Leukocyte
- drug effects
- physiology
- Endocytosis
- HL-60 Cells
- Humans
- Kinetics
- Monocyte Chemoattractant Proteins
- pharmacology
- NADPH Oxidase
- blood
- Neutrophils
- drug effects
- physiology
- Oligopeptides
- pharmacokinetics
- pharmacology
- Receptors
- Cell Surface
- drug effects
- physiology
- Receptors
- Formyl Peptide
- Receptors
- Immunologic
- agonists
- genetics
- physiology
- Receptors
- Lipoxin
- Receptors
- Peptide
- agonists
- genetics
- physiology
- Recombinant Proteins
- agonists
- metabolism
- Stereoisomerism
- Transfection
- Tritium
Publication and Content Type
- ref (subject category)
- art (subject category)
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