Document Detail


α-1 Antitrypsin regulates human neutrophil chemotaxis induced by soluble immune complexes and IL-8.
MedLine Citation:
PMID:  21060150     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Hereditary deficiency of the protein α-1 antitrypsin (AAT) causes a chronic lung disease in humans that is characterized by excessive mobilization of neutrophils into the lung. However, the reason for the increased neutrophil burden has not been fully elucidated. In this study we have demonstrated using human neutrophils that serum AAT coordinates both CXCR1- and soluble immune complex (sIC) receptor-mediated chemotaxis by divergent pathways. We demonstrated that glycosylated AAT can bind to IL-8 (a ligand for CXCR1) and that AAT-IL-8 complex formation prevented IL-8 interaction with CXCR1. Second, AAT modulated neutrophil chemotaxis in response to sIC by controlling membrane expression of the glycosylphosphatidylinositol-anchored (GPI-anchored) Fc receptor FcγRIIIb. This process was mediated through inhibition of ADAM-17 enzymatic activity. Neutrophils isolated from clinically stable AAT-deficient patients were characterized by low membrane expression of FcγRIIIb and increased chemotaxis in response to IL-8 and sIC. Treatment of AAT-deficient individuals with AAT augmentation therapy resulted in increased AAT binding to IL-8, increased AAT binding to the neutrophil membrane, decreased FcγRIIIb release from the neutrophil membrane, and normalization of chemotaxis. These results provide new insight into the mechanism underlying the effect of AAT augmentation therapy in the pulmonary disease associated with AAT deficiency.
Authors:
David A Bergin; Emer P Reeves; Paula Meleady; Michael Henry; Oliver J McElvaney; Tomás P Carroll; Claire Condron; Sanjay H Chotirmall; Martin Clynes; Shane J O'Neill; Noel G McElvaney
Publication Detail:
Type:  In Vitro; Journal Article     Date:  2010-11-08
Journal Detail:
Title:  The Journal of clinical investigation     Volume:  120     ISSN:  1558-8238     ISO Abbreviation:  J. Clin. Invest.     Publication Date:  2010 Dec 
Date Detail:
Created Date:  2010-12-02     Completed Date:  2011-01-14     Revised Date:  2012-02-07    
Medline Journal Info:
Nlm Unique ID:  7802877     Medline TA:  J Clin Invest     Country:  United States    
Other Details:
Languages:  eng     Pagination:  4236-50     Citation Subset:  AIM; IM    
Affiliation:
1Respiratory Research Division, Department of Medicine, Royal College of Surgeons in Ireland, Education and Research Centre, Beaumont Hospital, Dublin, Ireland.
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MeSH Terms
Descriptor/Qualifier:
ADAM Proteins / metabolism
Antigen-Antibody Complex / metabolism
Case-Control Studies
Chemotaxis, Leukocyte / drug effects,  immunology
GPI-Linked Proteins / metabolism
Humans
Interleukin-8 / metabolism
Membrane Microdomains / immunology
Middle Aged
Models, Immunological
Mutation
Neutrophils / drug effects*,  immunology*,  metabolism
Receptors, IgG / metabolism
Receptors, Interleukin-8A / metabolism
Recombinant Proteins / pharmacology
alpha 1-Antitrypsin / genetics,  immunology,  metabolism,  pharmacology*
alpha 1-Antitrypsin Deficiency / drug therapy*,  genetics,  immunology*,  metabolism
Chemical
Reg. No./Substance:
0/Antigen-Antibody Complex; 0/FCGR3B protein, human; 0/GPI-Linked Proteins; 0/IL8 protein, human; 0/Interleukin-8; 0/Receptors, IgG; 0/Receptors, Interleukin-8A; 0/Recombinant Proteins; 0/alpha 1-Antitrypsin; EC 3.4.24.-/ADAM Proteins; EC 3.4.24.-/tumor necrosis factor-alpha convertase

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


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