Synthesis and use of a novel N-formyl peptide derivative to isolate a human N-formyl peptide receptor cDNA

Boulay, François; Tardif, Marianne; Brouchon, Laurence; Vignais, Pierre V.

doi:10.1016/0006-291x(90)91143-g

Cited by 241 publications

(132 citation statements)

References 16 publications

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“…Sequence alignment of all available cDNAs and ESTs for the three genes with this BAC contig indicated the presence of two exons for each gene. [14][15][16][17] Although reports that FPR1 and FPRL-1 have three exons were not verified by EST or cDNA data, FPR1 and FPRL-1 were each found to have a single exon ORF as previously reported. 16 The sizes of the exons and intron are given for FPR1 in Figure 1B.…”

Section: Resultsmentioning

confidence: 96%

Evaluation of human leukocyte N-formylpeptide receptor (FPR1) SNPs in aggressive periodontitis patients

et al. 2003

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Polymorphonuclear neutrophils (PMNs) are attracted to sites of infection by N-formylpeptide (fMLP) chemoattractants. The high-affinity fMLP receptor (FPR1) of phagocytic cells interacts with bacterial fMLP and mediates chemotaxis, degranulation, and superoxide production. These cellular functions are disrupted in PMN from aggressive periodontitis (AP) patients. Two FPR1 gene single nucleotide polymorphisms (SNPs), c.329T4C and c.378C4G, have been associated with a localized form of AP in African-American patients. To evaluate the generality of these SNPs in AP patients, we sequenced a 363 bp interval of the FPR1 gene in an ethnically diverse group of patients (n ¼ 111) and controls (n ¼ 115). Neither c.329T4C nor c.378C4G were detected in the 452 alleles sequenced. Six SNPs were identified including two located in the FPR1 second extracellular loop that were significantly associated with the AP phenotype in African-American patients (p.R190W, P ¼ 0.0033; and p.N192K, P ¼ 0.0018). These two SNPs show three predominant haplotypes, each associated with a different disease risk in African-Americans. These data do not support the hypothesis that the FPR1 SNPs c.329T4C and c.378C4G play an etiologic role in aggressive periodontitis, but do suggest that SNPs in the second extracellular loop may be etiologically important.

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Section: Resultsmentioning

confidence: 96%

Evaluation of human leukocyte N-formylpeptide receptor (FPR1) SNPs in aggressive periodontitis patients

et al. 2003

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“…The FPR is a member of the G protein-coupled receptor family (1,2). This class of receptors is typified by the presence of seven membrane-spanning domains.…”

Section: Effects Of Pi3k Inhibitors On Fmlp-induced Rhoa Activation Imentioning

confidence: 99%

“…When exposed to chemoattractants, such as formyl peptide, leukocytes become rapidly activated. The bacterial tripeptide fMet-Leu-Phe (fMLP) 1 is able to activate all major functions of neutrophils and is a prototypical ligand for the N-formyl peptide receptor (FPR), which contains seven putative transmembrane domains characteristic of the G protein-coupled receptor of the rhodopsin family (1,2). fMLP stimulates peripheral blood mononuclear cells to express a defined set of gene products, including IL-1, IL-6, and IL-8.…”

mentioning

confidence: 99%

Chemoattractant-stimulated NF-κB Activation Is Dependent on the Low Molecular Weight GTPase RhoA

Huang¹,

Chen²,

Zuraw³

et al. 2001

Journal of Biological Chemistry

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“…Receptors for N-formylmethionyl peptides (FPR) are among the most thoroughly studied neutrophil receptors and are members of the family of receptors coupled to a guanyl nucleotide-binding protein (G protein). The FPR has recently been cloned (6) and exhibits seven hydrophobic domains, suggesting that this receptor has seven transmembrane segments, analogous to other G protein-coupled receptors (7,8).…”

Section: Lntroductionmentioning

confidence: 99%

Neutrophil chemoattractant receptors and the membrane skeleton

Klotz

Jesaitis

1994

BioEssays

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Signal transduction via receptors for N‐formylmethionyl peptide chemoattractants (FPR) on human neutrophils is a highly regulated process which involves participation of cytoskeletal elements. Evidence exists suggesting that the cytoskeleton and/or the membrane skeleton controls the distribution of FPR in the plane of the plasma membrane, thus controlling the accessibility of FPR to different proteins in functionally distinct domains. In desensitized cells, FPR are restricted to domains which are depleted of G proteins but enriched in cytoskeletal proteins such as actin and fodrin. Thus, the G protein signal transduction partners of FPR become inaccessible to the agonist‐occupied receptor, preventing cell activation. The mechanism of interaction of FPR with the membrane skeleton is poorly understood but evidence is accumulating that suggests a direct binding of FPR (and other receptors) to cytoskeletal proteins such as actin.

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Synthesis and use of a novel N-formyl peptide derivative to isolate a human N-formyl peptide receptor cDNA

Cited by 241 publications

References 16 publications

Evaluation of human leukocyte N-formylpeptide receptor (FPR1) SNPs in aggressive periodontitis patients

Evaluation of human leukocyte N-formylpeptide receptor (FPR1) SNPs in aggressive periodontitis patients

Chemoattractant-stimulated NF-κB Activation Is Dependent on the Low Molecular Weight GTPase RhoA

Neutrophil chemoattractant receptors and the membrane skeleton

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