Human eosinophils express a receptor for secretory component. Role in secretory IgA‐dependent activation

Lamkhioued, Bouchaïb; Gounni, Abdelilah Soussi; Gruart, Valérie; Pierce, Annick; Càpron, André; Capron, Moníque

doi:10.1002/eji.1830250121

Cited by 109 publications

(63 citation statements)

References 36 publications

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“…Neutrophils do not have a specific receptor for SC (4), and SC did not interfere with IL-8 binding to specific, CXCR1 and/or CXCR2, receptors on neutrophils. In parallel, SC did not inhibit signaling via the IL-8 receptor.…”

Section: Discussionmentioning

confidence: 91%

IL-8 Released Constitutively by Primary Bronchial Epithelial Cells in Culture Forms an Inactive Complex with Secretory Component

Marshall

Perks

Ferkol

et al. 2001

The Journal of Immunology

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The bronchial epithelium is a source of both α and β chemokines and, uniquely, of secretory component (SC), the extracellular ligand-binding domain of the polymeric IgA receptor. Ig superfamily relatives of SC, such as IgG and α2-macroglobulin, bind IL-8. Therefore, we tested the hypothesis that SC binds IL-8, modifying its activity as a neutrophil chemoattractant. Primary bronchial epithelial cells were cultured under conditions to optimize SC synthesis. The chemokines IL-8, epithelial neutrophil-activating peptide-78, growth-related oncogene α, and RANTES were released constitutively by epithelial cells from both normal and asthmatic donors and detected in high m.w. complexes with SC. There were no qualitative differences in the production of SC-chemokine complexes by epithelial cells from normal or asthmatic donors, and in all cases this was the only form of chemokine detected. SC contains 15% N-linked carbohydrate, and complete deglycosylation with peptide N-glycosidase F abolished IL-8 binding. In micro-Boyden chamber assays, no IL-8-dependent neutrophil chemotactic responses to epithelial culture supernatants could be demonstrated. SC dose-dependently (IC50 ∼0.3 nM) inhibited the neutrophil chemotactic response to rIL-8 (10 nM) in micro-Boyden chamber assays and also inhibited IL-8-mediated neutrophil transendothelial migration. SC inhibited the binding of IL-8 to nonspecific binding sites on polycarbonate filters and endothelial cell monolayers, and therefore the formation of haptotactic gradients, without effects on IL-8 binding to specific receptors on neutrophils. The data indicate that in the airways IL-8 may be solubilized and inactivated by binding to SC.

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Section: Discussionmentioning

confidence: 91%

IL-8 Released Constitutively by Primary Bronchial Epithelial Cells in Culture Forms an Inactive Complex with Secretory Component

Marshall

Perks

Ferkol

et al. 2001

The Journal of Immunology

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“…2A) (17). Eosinophil activation by immobilized secretory component is correlated with the presence of a putative 15-kDa receptor for secretory component on eosinophils that is absent in neutrophils (43). The possibility that immobilized lactoferrin may cross-react with the putative receptor for secretory component on eosinophils (43) cannot yet be excluded.…”

Section: Discussionmentioning

confidence: 99%

Immobilized Lactoferrin Is a Stimulus for Eosinophil Activation

Thomas

Ardon

2002

The Journal of Immunology

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Eosinophils are strongly implicated in the pathogenesis of asthma, particularly in damage to the airway epithelial lining. We examined the potential for lactoferrin, a multifunctional glycoprotein present in the airway surface liquid, to activate eosinophils. Incubating eosinophils in tissue culture wells pretreated with 1–100 μg/ml human lactoferrin stimulated concentration-dependent superoxide production by eosinophils. The same concentrations of immobilized transferrin were without effect. The potency of immobilized lactoferrin was approximately one-third that of immobilized secretory IgA in the same experiments. In contrast, immobilized lactoferrin did not stimulate neutrophil superoxide production. Eosinophils bound lactoferrin as determined by flow cytometry and by binding of 125I-labeled lactoferrin. Transferrin did not block binding of 125I-labeled lactoferrin. Soluble lactoferrin, however, did not activate the eosinophils and did not block superoxide production stimulated by immobilized lactoferrin. Immobilized lactoferrin also stimulated release of eosinophil-derived neurotoxin and low levels of leukotriene C4 production; the latter was significantly enhanced in the presence of 100 pg/ml GM-CSF. GM-CSF also enhanced superoxide production and eosinophil-derived neurotoxin release stimulated by the lower concentrations of immobilized lactoferrin. Pretreatment of the lactoferrin with peptide N-glycosidase F or addition of heparin or chondroitin sulfate to the incubation contents had no or only a minimal effect on the activity of immobilized lactoferrin. These results demonstrate that lactoferrin adherent to the surface epithelium may contribute to the activation of eosinophils that infiltrate the airway lumen in eosinophil-associated disorders such as asthma.

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“…In addition to FcaR, SIgA has been shown to bind to an unidentified IgA receptor on human monocytes and that binding is blocked by galactose [83]. Moreover, a 15 kDa receptor for secretory component (SC) and thus also for SIgA has been identified on eosinophils but not on neutrophils [84]. Using different CD89 transfectant cell models, several studies have reported that pIgA binds more efficiently to FcaR than mIgA [85].…”

Section: Immunoglobulin-a Transportmentioning

confidence: 99%

Lung mucosal immunity: immunoglobulin-A revisited

et al. 2001

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Mucosal defence mechanisms are critical in preventing colonization of the respiratory tract by pathogens and penetration of antigens through the epithelial barrier. Recent research has now illustrated the active contribution of the respiratory epithelium to the exclusion of microbes and particles, but also to the control of the inflammatory and immune responses in the airways and in the alveoli. Epithelial cells also mediate the active transport of polymeric immunoglobulin-A from the lamina propria to the airway lumen through the polymeric immunoglobulin receptor. The role of IgA in the defence of mucosal surfaces has now expanded from a limited role of scavenger of exogenous material to a broader protective function with potential applications in immunotherapy. In addition, the recent identification of receptors for IgA on the surface of blood leukocytes and alveolar macrophages provides an additional mechanism of interaction between the cellular and humoral immune systems at the level of the respiratory tract.

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Human eosinophils express a receptor for secretory component. Role in secretory IgA‐dependent activation

Cited by 109 publications

References 36 publications

IL-8 Released Constitutively by Primary Bronchial Epithelial Cells in Culture Forms an Inactive Complex with Secretory Component

IL-8 Released Constitutively by Primary Bronchial Epithelial Cells in Culture Forms an Inactive Complex with Secretory Component

Immobilized Lactoferrin Is a Stimulus for Eosinophil Activation

Lung mucosal immunity: immunoglobulin-A revisited

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