Document Detail


Responses of neutrophils to anti-integrin antibodies depends on costimulation through low affinity Fc gamma Rs: full activation requires both integrin and nonintegrin signals.
MedLine Citation:
PMID:  15265942     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The relative contribution of integrin and nonintegrin signals to neutrophil activation is incompletely understood. Immobilized anti-integrin Abs were previously shown to induce robust activation of neutrophils without any additional stimulus, suggesting that cross-linking of integrins is sufficient for full activation of the cells. However, the possible contribution from other receptors has not been tested in this system. In this study, we show that neutrophil responses to anti-integrin Abs requires costimulation through low-affinity Fc gamma Rs. Murine neutrophils lacking the FcR gamma-chain or Fc gamma RIII failed to respond to immobilized Abs against beta(1), beta(2), or beta(3) integrins and the activation of wild-type cells could be prevented by blocking Abs against Fc gamma RII/III. Plate-bound anti-CD18 Abs initiated a respiratory burst from human neutrophils, but this response was abrogated when the F(ab')(2) of the same Abs were used or the cells were preincubated with Fc gamma RIIA-blocking Abs. Lack of Fc gamma RIII or administration of Fc gamma R-blocking Abs had no effect on responses of TNF-stimulated cells plated on fibrinogen or rICAM-1. TNF restored the respiratory burst of Fc gamma RIII-deficient neutrophils plated on anti-CD18 mAbs. The p38 MAPK inhibitor SB203580 attenuated the responses of neutrophils to anti-CD18 mAbs or TNF stimulation on a fibrinogen surface. Taken together, these results indicate that activation of low-affinity Fc gamma Rs is required for neutrophil responses induced by anti-integrin Abs and suggest that a second coactivation signal (e.g., through TNF or FcR ligation) is indispensable for full integrin-mediated activation of neutrophils. These second signals are interchangeable and they may converge on the p38 MAPK.
Authors:
Zoltán Jakus; Giorgio Berton; Erzsébet Ligeti; Clifford A Lowell; Attila Mócsai
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of immunology (Baltimore, Md. : 1950)     Volume:  173     ISSN:  0022-1767     ISO Abbreviation:  J. Immunol.     Publication Date:  2004 Aug 
Date Detail:
Created Date:  2004-07-21     Completed Date:  2004-11-02     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  2985117R     Medline TA:  J Immunol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2068-77     Citation Subset:  AIM; IM    
Affiliation:
Department of Physiology, Semmelweis University School of Medicine, Budapest, Hungary.
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MeSH Terms
Descriptor/Qualifier:
Animals
Antibodies, Monoclonal / pharmacology*
Cell Adhesion / drug effects,  physiology
Enzyme Inhibitors / pharmacology
Fibrinogen / metabolism
Imidazoles / pharmacology
Integrin beta Chains / immunology,  physiology*
Intercellular Adhesion Molecule-1 / genetics,  metabolism
MAP Kinase Signaling System / drug effects,  physiology
Mice
Mice, Inbred C57BL
Mice, Knockout
Mitogen-Activated Protein Kinases / antagonists & inhibitors,  physiology
Neutrophils / drug effects*
Phosphorylation
Protein Processing, Post-Translational / drug effects
Pyridines / pharmacology
Receptor Aggregation
Receptors, IgG / deficiency,  drug effects,  genetics,  immunology,  physiology*
Recombinant Proteins / metabolism
Respiratory Burst / drug effects
Signal Transduction / physiology*
Superoxides / metabolism
p38 Mitogen-Activated Protein Kinases
Grant Support
ID/Acronym/Agency:
DK58066/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Antibodies, Monoclonal; 0/Enzyme Inhibitors; 0/Fcgr1 protein, mouse; 0/Fcgr2b protein, mouse; 0/Fcgr3 protein, mouse; 0/Imidazoles; 0/Integrin beta Chains; 0/Pyridines; 0/Receptors, IgG; 0/Recombinant Proteins; 0/SB 203580; 11062-77-4/Superoxides; 126547-89-5/Intercellular Adhesion Molecule-1; 9001-32-5/Fibrinogen; EC 2.7.11.24/Mitogen-Activated Protein Kinases; EC 2.7.11.24/p38 Mitogen-Activated Protein Kinases

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


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