Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractEffect of the natural winemaking process applied at industrial level on the microbiological and chemical characteristics of wine    Next AbstractEffects of Saccharomyces cerevisiae in association with Torulaspora delbrueckii on the aroma and amino acids in longan wines »

Proc Natl Acad Sci U S A


Title:Characterization of a class of nonformylated Enterococcus faecalis-derived neutrophil chemotactic peptides: the sex pheromones
Author(s):Sannomiya P; Craig RA; Clewell DB; Suzuki A; Fujino M; Till GO; Marasco WA;
Address:"Instituto de Ciencas Biomedicas, Universidade de Sao Paulo, Brazil"
Journal Title:Proc Natl Acad Sci U S A
Year:1990
Volume:87
Issue:1
Page Number:66 - 70
DOI: 10.1073/pnas.87.1.66
ISSN/ISBN:0027-8424 (Print) 1091-6490 (Electronic) 0027-8424 (Linking)
Abstract:"Bacteria produce a heterogeneous mixture of neutrophil chemotactic agents in culture filtrates. Formylmethionyl peptides have been shown to comprise a significant portion of the chemotactic activity in bacterial culture filtrates; however, not all of the chemotactic agents in bacterial culture filtrates are formylated peptides. To examine whether nonformylated peptides derived from bacteria could act as chemotactic agents, we studied several nonformylated hepta- and octapeptide Enterococcus faecalis-derived sex pheromones, their modified derivatives, and their competitive inhibitors for activation of rat peritoneal neutrophils. Several of these peptides, in particular cAM373 and cPD1, proved to be potent chemotactic agents in submicromolar concentrations as well as inducers of lysosomal granule enzyme secretion. Moreover, the more biologically active peptides were able to compete with fMet-Leu-[3H]Phe for binding to the formyl peptide receptor. These studies demonstrate that the formylmethionyl moiety may be an absolute requirement only for the binding of di- and tripeptides to the formyl peptide receptor. Larger peptides that may have or that may allow for additional contact points between the peptide and receptor may require N-formylation only relatively. Indeed, by removing this structural restraint, the formyl peptide receptor may interact with an unlimited number of peptide fragments of both infectious and host origins to then modulate neutrophil responses to infection and inflammation"
Keywords:"Amino Acid Sequence Animals Chemotactic Factors/isolation & purification/*pharmacology Chemotaxis, Leukocyte/*drug effects Enterococcus faecalis/*physiology In Vitro Techniques Kinetics Male Molecular Sequence Data N-Formylmethionine Leucyl-Phenylalanine/;"
Notes:"MedlineSannomiya, P Craig, R A Clewell, D B Suzuki, A Fujino, M Till, G O Marasco, W A eng GM-28499/GM/NIGMS NIH HHS/ GM-33956/GM/NIGMS NIH HHS/ HL-28445/HL/NHLBI NIH HHS/ Research Support, U.S. Gov't, P.H.S. 1990/01/01 Proc Natl Acad Sci U S A. 1990 Jan; 87(1):66-70. doi: 10.1073/pnas.87.1.66"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 21-09-2024