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Search results 101 to 131 out of 131 for Fpr3

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Type Details Score
Publication
22610094 | -
First Author: Bena S
Year: 2012
Journal: J Biol Chem
Title: Annexin A1 interaction with the FPR2/ALX receptor: identification of distinct domains and downstream associated signaling.
Volume: 287
Issue: 29
Pages: 24690-7
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Publication
1374236 | -
First Author: Ye RD
Year: 1992
Journal: Biochem Biophys Res Commun
Title: Isolation of a cDNA that encodes a novel granulocyte N-formyl peptide receptor.
Volume: 184
Issue: 2
Pages: 582-9
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Publication
16025565 | -
First Author: Rabiet MJ
Year: 2005
Journal: Eur J Immunol
Title: Human mitochondria-derived N-formylated peptides are novel agonists equally active on FPR and FPRL1, while Listeria monocytogenes-derived peptides preferentially activate FPR.
Volume: 35
Issue: 8
Pages: 2486-95
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Publication
21543323 | -
First Author: Rabiet MJ
Year: 2011
Journal: J Biol Chem
Title: N-formyl peptide receptor 3 (FPR3) departs from the homologous FPR2/ALX receptor with regard to the major processes governing chemoattractant receptor regulation, expression at the cell surface, and phosphorylation.
Volume: 286
Issue: 30
Pages: 26718-31
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Publication
23549262 | -
First Author: Cattaneo F
Year: 2013
Journal: Int J Mol Sci
Title: Distinct signaling cascades elicited by different formyl peptide receptor 2 (FPR2) agonists.
Volume: 14
Issue: 4
Pages: 7193-230
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Publication
15888909 | -
First Author: Iribarren P
Year: 2005
Journal: Immunol Res
Title: Role of formyl peptide receptor-like 1 (FPRL1/FPR2) in mononuclear phagocyte responses in Alzheimer disease.
Volume: 31
Issue: 3
Pages: 165-76
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Publication
23454745 | J:197568
First Author: Chen K
Year: 2013
Journal: J Clin Invest
Title: Formylpeptide receptor-2 contributes to colonic epithelial homeostasis, inflammation, and tumorigenesis.
Volume: 123
Issue: 4
Pages: 1694-704
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Publication
23562731 | -
First Author: Forsman H
Year: 2013
Journal: Biochim Biophys Acta
Title: The leukocyte chemotactic receptor FPR2, but not the closely related FPR1, is sensitive to cell-penetrating pepducins with amino acid sequences descending from the third intracellular receptor loop.
Volume: 1833
Issue: 8
Pages: 1914-23
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Protein Domain
IPR027345 | Formyl_pep_1/2_rcpt
Type: Family
Description: Formyl peptide receptors (FPR) are members of the rhodopsin-like G-protein coupled receptor family and are involved in chemotaxis [, ]. They were originally identified by their ability to bind N-formyl peptides (typified by fMet-Leu-Phe (fMLP)), produced by the degradation of either bacterial or host cells [, ]but subsequent ligands have been discovered, containing many microbial agonists derived from both bacteria and viruses [, ].FPRs were initially found on leukocytes, but they are expressed in other cells, for example, immature dendritic cells, platelets, microglial cells, astrocytes, fibroblasts and platelets [, ]. FPRs are expressed at high levels on polymorphonuclear and mononuclear phagocytes. Formyl peptide receptors are not only involved in mediating immune cell response to infection, but also act to suppress the immune system under certain conditions []. The main responses elicited upon ligation of formylated peptides, are those of morphological polarization, locomotion, production of reactive-oxygen species and release of proteolytic enzymes []. There are three formyl peptide receptor subtypes, FPR1, FPR2 and FPR3 [, ]. The sequence similarity between FPR1 and FPR2 is high (69%), and although there is a large sequence similarity also between FPR2 and FPR3 (83%), FPR3 can not bind formylated peptides [, ]. This entry represents formyl peptide receptor 1 (FPR1) and Formyl peptide receptor 2 (FPR2).Formyl peptide receptor 1 (FPR1, also known as fMet-Leu-Phe receptor) plays an important role for host defence. This is shown in mice that are devoid of receptor expression, are unable to respond to an infection by Listeria monocytogenes []. The interaction between formyl-methionyl-leucyl phenylalanine (fMLF) and FPR1 triggers a cascade of multiple second messengers through the activation of phospholipase C, phospholipase D and phospholipase A2. This signalling cascade culminates in cell chemotaxis [], phagocytosis [], production of proinflammatory mediators []and activation of transcription factors []. The characterisation of FPR1 function has focused on cells involved in brain function and disease and research indicates that FPR1 is expressed in highly malignant human glioma cells, and is thought to be responsible for mediating motility, growth and angiogenesis of the glioblastoma [, ]. The number of ligands for FPRs is immense, and includes many microbial agonists derived from both bacteria and viruses [, ]. However, unlike FPR2 and FPR3, ligands for FPR1 include endogenous substances, such as annexin AI peptide (Ac9-25) [], and allergens, such as the house mite allergen [].Formyl peptide receptor 2 (FPR2), also known as formyl peptide receptor-like 1 (FPRL1) []and ALXR [], interacts with formylated peptides at a much lower affinity than FPR1 [, ]. However, FPR2 has been found to be a promiscuous receptor, and binds ligands of great diversity in origin and structure, including both lipids and proteins [, ]. It has also been found that mitochondria-derived formyl peptides are potent agonists for FPR2 [], suggesting that its primary function may be to recognise host-driven mitochondrial peptides or possibly other bacterially derived formyl peptides []. FPR2 is also sensitive to cell-penetrating pepducins, unlike FPR1 [].The characterisation of FPR2 function has focused on cells involved in brain function and disease. Research indicates that peptides derived from the protein amyloid beta, which have been shown to stimulate the release of neurotoxic substances from monocytes, do so via FPR2. This suggests that FPR2 is at least partly responsible for proinflammatory destructive activity in brain tissue during Alzheimer's disease [, ]. FPR2 is also critical in mediating homeostasis, inflammation, and epithelial repair processes in the colon [].
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Protein
P33766
Organism: Mus musculus/domesticus
Length: 364  
Fragment?: false
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Protein
O88536
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
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Protein
O88537
Organism: Mus musculus/domesticus
Length: 343  
Fragment?: false
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Protein
O88416
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
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Protein
A4FUQ5
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: false
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Protein
Q3SXG2
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
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Protein
Q71MR7
Organism: Mus musculus/domesticus
Length: 338  
Fragment?: false
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Protein
D8VER2
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
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Protein
P30993
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
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Protein
Q8BW93
Organism: Mus musculus/domesticus
Length: 344  
Fragment?: false
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Protein
O09047
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
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Protein
P97468
Organism: Mus musculus/domesticus
Length: 371  
Fragment?: false
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Protein
Q5U7A4
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
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Protein
E9QQ21
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: false
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Protein
Q3UCS9
Organism: Mus musculus/domesticus
Length: 301  
Fragment?: true
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Protein
A0A1B0GT01
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: true
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Protein
Q3TYR0
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: true
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Protein
Q8C6R2
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
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Protein
E9Q8N2
Organism: Mus musculus/domesticus
Length: 301  
Fragment?: true
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Protein
Q497D3
Organism: Mus musculus/domesticus
Length: 371  
Fragment?: false
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Protein
Q3U4N3
Organism: Mus musculus/domesticus
Length: 226  
Fragment?: true
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Protein
E9PVQ2
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: false
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