Document Detail


Neutrophil-derived cathelicidin promotes adhesion of classical monocytes.
MedLine Citation:
PMID:  23283724     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
RATIONALE: The leukocyte response in acute inflammation is characterized by an initial recruitment of neutrophils preceding a second wave of monocytes. Neutrophil-derived granule proteins were suggested to hold an important role in this cellular switch. The exact mechanisms by which neutrophils mediate these processes are only partially understood.
OBJECTIVE: To investigate the role of neutrophils and their granule contents in the adhesion of monocyte subpopulations in acute inflammation.
METHODS AND RESULTS: Here, we show that neutrophil-derived cathelicidins (human: LL37, mouse: CRAMP) induce adhesion of classical monocytes but not of nonclassical monocytes in the mouse cremaster muscle and in in vitro flow chamber assays. CRAMP is released from emigrated neutrophils and then transported across the endothelium, where it is presented to rolling leukocytes. Endothelial-bound cathelicidin activates formyl-peptide receptor 2 on classical monocytes, resulting in monocytic β1- and β2-integrin conformational change toward an extended, active conformation that allows for adhesion to their respective ligands, vascular cell adhesion molecule 1 and intercellular adhesion molecule 1.
CONCLUSIONS: These data elucidate a novel mechanism of neutrophil-mediated monocyte recruitment, which could be targeted in conditions where recruitment of classical monocytes plays an unfavorable role.
Authors:
Sarawuth Wantha; Jean-Eric Alard; Remco T A Megens; Anne M van der Does; Yvonne Döring; Maik Drechsler; Christine T N Pham; Ming-Wei Wang; Ji-Min Wang; Richard L Gallo; Philipp von Hundelshausen; Lennart Lindbom; Tilman Hackeng; Christian Weber; Oliver Soehnlein
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2013-01-02
Journal Detail:
Title:  Circulation research     Volume:  112     ISSN:  1524-4571     ISO Abbreviation:  Circ. Res.     Publication Date:  2013 Mar 
Date Detail:
Created Date:  2013-03-01     Completed Date:  2013-06-25     Revised Date:  2014-07-31    
Medline Journal Info:
Nlm Unique ID:  0047103     Medline TA:  Circ Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  792-801     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Antimicrobial Cationic Peptides / genetics,  metabolism*
Cathelicidins / genetics,  metabolism
Cell Adhesion / physiology
Cell Communication / physiology*
Endothelium, Vascular / metabolism
Humans
Inflammation / metabolism,  pathology*
Integrins / metabolism
Mice
Mice, Inbred C57BL
Mice, Knockout
Molecular Sequence Data
Monocytes / metabolism*,  pathology*
Neutrophils / metabolism*,  pathology*
Receptors, Formyl Peptide / metabolism
Receptors, Lipoxin / metabolism
Grant Support
ID/Acronym/Agency:
R01 AI049261/AI/NIAID NIH HHS; R01 AI052453/AI/NIAID NIH HHS; R01 AR052728/AR/NIAMS NIH HHS; R56 AI049261/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Antimicrobial Cationic Peptides; 0/Cathelicidins; 0/FPR2 protein, human; 0/Integrins; 0/Receptors, Formyl Peptide; 0/Receptors, Lipoxin; 0/cathelicidin antimicrobial peptide; 0/formyl peptide receptor 2, mouse; 143108-26-3/CAP18 lipopolysaccharide-binding protein
Comments/Corrections
Comment In:
Circ Res. 2013 Mar 1;112(5):744-5   [PMID:  23449542 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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