Open AccessJournal Article
The isolation and partial characterization of neutrophil chemotactic factors from Escherichia coli.
Elliott Schiffmann,Henry V. Showell,Barbara A. Corcoran,Peter A. Ward,Eric P. Smith,Elmer L. Becker +5 more
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Heat-stable, chemotactically active peptides have been obtained from Escherichia coli culture filtrates and a highly purified, not completely characterized, fraction was found to contain aspartic acid, serine, glutamic acid, alanine, and glycine.Abstract:
Heat-stable, chemotactically active peptides have been obtained from Escherichia coli culture filtrates. They range in size between 150 and 1500 daltons and are anionic at neutral pH. Free carboxyl groups but not free amino groups appear to be required for activity. The N-terminal group may be blocked. There do not appear to be internal aromatic or basic residues in the chemotactically active fractions. A highly purified, not completely characterized, fraction was found to contain aspartic acid, serine, glutamic acid, alanine, and glycine.read more
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International Union of Basic and Clinical Pharmacology. LXXIII. Nomenclature for the formyl peptide receptor (FPR) family.
Richard D. Ye,François Boulay,Ji Ming Wang,Claes Dahlgren,Craig Gerard,Marc Parmentier,Charles N. Serhan,Philip M. Murphy +7 more
TL;DR: An International Union of Basic and Clinical Pharmacology (IUPHAR)-recommended nomenclature is introduced and unmet challenges are discussed, including the mechanisms used by these receptors to bind diverse ligands and mediate different biological functions.
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The structure-activity relations of synthetic peptides as chemotactic factors and inducers of lysosomal secretion for neutrophils.
TL;DR: The high activity and the specificity and nature of the structural requirements strongly suggest that the primary interaction of peptide and neutrophil leading to either chemotaxis or lysosomal enzyme release is a binding of the peptide with a stereospecific receptor on the neutrophIL surface.
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Formyl-peptide receptors revisited
TL;DR: This work has shown that the formyl-peptide receptor and its variant FPRL1 (FPR-like 1) are involved in host defense against bacterial infection and in the clearance of damaged cells, and suggests that these receptors contribute to disease pathogenesis and host defense.
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Purification and identification of formyl-methionyl-leucyl-phenylalanine as the major peptide neutrophil chemotactic factor produced by Escherichia coli.
Wayne A. Marasco,Sem H. Phan,H Krutzsch,H.J. Showell,Douglas Feltner,Roderick Nairn,Elmer L. Becker,Peter A. Ward +7 more
TL;DR: The results demonstrate that the NH2-terminal formyl peptides produced by E. coli, of which formyl-methionyl-leucyl-phenylalanine appears to be the major component, are the peptide mediators responsible for leukocyte chemotactic activity in the bacterial culture extracts.
Journal ArticleDOI
The Lipoxin Receptor ALX: Potent Ligand-Specific and Stereoselective Actions in Vivo
Nan Chiang,Charles N. Serhan,Sven-Erik Dahlén,Jeffrey M. Drazen,Douglas W. P. Hay,G. Enrico Rovati,Takao Shimizu,Takehiko Yokomizo,Charles Brink +8 more
TL;DR: The purpose of this review is to highlight the molecular characterization of the ALX receptor and provide an overview of theALX-LXA4 axis responsible for anti-inflammatory and proresolving signals in vivo.