Document Detail


A cathelicidin family of human antibacterial peptide LL-37 induces mast cell chemotaxis.
MedLine Citation:
PMID:  11972628     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The mast cell is one of the major effector cells in inflammatory reactions and can be found in most tissues throughout the body. During inflammation, an increase in the number of mast cells in the local milieu occurs, and such accumulation requires directed migration of this cell population. As it has previously been reported that the human cathelicidin-derived antibacterial peptide, LL-37, stimulates the degranulation of mast cells, we hypothesized that LL-37 could be a mast cell chemotaxin. The present study shows that LL-37 is a potent chemotactic factor for mast cells. The chemotactic response was dose-dependent and bell-shaped, reaching an optimal concentration of 5 microg/ml. In addition, checkerboard analysis showed that cell migration towards this peptide was chemotactic rather than chemokinetic. Moreover, Scatchard analysis using 125I-labelled LL-37-derived peptide revealed that LL-37 has at least two classes of receptors, namely high- and low-affinity receptors, on mast cells. Furthermore, the competitive binding assay suggested that LL-37 is unlikely to utilize formyl peptide receptor-like 1 (FPRL1), a functional LL-37 receptor for neutrophil and monocyte migration, on mast cells. In addition, the treatment of cells with pertussis toxin and phospholipase C inhibitor, U-73122, inhibited LL-37-mediated migration, indicating that LL-37 induces mast cell chemotaxis through a Gi protein-phospholipase C signalling pathway. These results show that besides its antibacterial activities, LL-37 may have the potential to recruit mast cells to inflammation foci.
Authors:
François Niyonsaba; Kazuhisa Iwabuchi; Akimasa Someya; Michimasa Hirata; Hiroshi Matsuda; Hideoki Ogawa; Isao Nagaoka
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Immunology     Volume:  106     ISSN:  0019-2805     ISO Abbreviation:  Immunology     Publication Date:  2002 May 
Date Detail:
Created Date:  2002-04-25     Completed Date:  2002-06-10     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0374672     Medline TA:  Immunology     Country:  England    
Other Details:
Languages:  eng     Pagination:  20-6     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Juntendo University, School of Medicine, Tokyo, Japan.
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MeSH Terms
Descriptor/Qualifier:
Animals
Antimicrobial Cationic Peptides / immunology*
Binding, Competitive / immunology
Calcium / metabolism
Chemotactic Factors / immunology*
Chemotaxis / immunology*
Dose-Response Relationship, Immunologic
Estrenes
Immune Sera / immunology
Male
Mast Cells / immunology*,  metabolism
Pertussis Toxin
Phosphodiesterase Inhibitors / pharmacology
Prodrugs / pharmacology*
Pyrrolidinones
Rats
Rats, Sprague-Dawley
Signal Transduction / immunology
Virulence Factors, Bordetella / pharmacology
Chemical
Reg. No./Substance:
0/Antimicrobial Cationic Peptides; 0/Chemotactic Factors; 0/Estrenes; 0/Immune Sera; 0/Phosphodiesterase Inhibitors; 0/Prodrugs; 0/Pyrrolidinones; 0/Virulence Factors, Bordetella; 0/cathelicidin antimicrobial peptide; 112648-68-7/1-(6-((3-methoxyestra-1,3,5(10)-trien-17-yl)amino)hexyl)-1H-pyrrole-2,5-dione; 143108-26-3/CAP18 lipopolysaccharide-binding protein; 7440-70-2/Calcium; EC 2.4.2.31/Pertussis Toxin
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