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    α-1 Antitrypsin regulates human neutrophil chemotaxis induced by soluble immune complexes and IL-8.

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    Authors
    Bergin, David A
    Reeves, Emer P
    Meleady, Paula
    Henry, Michael
    McElvaney, Oliver J
    Carroll, Tomás P
    Condron, Claire
    Chotirmall, Sanjay H
    Clynes, Martin
    O'Neill, Shane J
    McElvaney, Noel G
    Show allShow less
    Affiliation
    Respiratory Research Division, Department of Medicine, Royal College of Surgeons in Ireland, Education and Research Centre, Beaumont Hospital, Dublin, Ireland.
    Issue Date
    2010-12-01
    Keywords
    GENETICS
    RESPIRATORY DISORDER
    MeSH
    ADAM Proteins
    Antigen-Antibody Complex
    Case-Control Studies
    Chemotaxis, Leukocyte
    GPI-Linked Proteins
    Humans
    Interleukin-8
    Membrane Microdomains
    Middle Aged
    Models, Immunological
    Mutation
    Neutrophils
    Receptors, IgG
    Receptors, Interleukin-8A
    Recombinant Proteins
    alpha 1-Antitrypsin
    alpha 1-Antitrypsin Deficiency
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    Citation
    α-1 Antitrypsin regulates human neutrophil chemotaxis induced by soluble immune complexes and IL-8. 2010, 120 (12):4236-50 J. Clin. Invest.
    Journal
    The Journal of clinical investigation
    URI
    http://hdl.handle.net/10147/120887
    DOI
    10.1172/JCI41196
    PubMed ID
    21060150
    Abstract
    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.
    Item Type
    Article
    Language
    en
    ISSN
    1558-8238
    ae974a485f413a2113503eed53cd6c53
    10.1172/JCI41196
    Scopus Count
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