IL-13 alters mucociliary differentiation and ciliary beating of human respiratory epithelial cells

Laoukili, Jamila; Perret, Eric; Willems, Tom; Minty, Adrian; Parthoens, Eef; Houcine, Odile; Coste, A.; Jorissen, Mark; Marano, Francelyne; Caput, Daniel; Tournier, Frédéric

doi:10.1172/jci13557

Cited by 134 publications

(126 citation statements)

References 46 publications

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“…This study has demonstrated mRNA and protein expression of four centrin isoforms in the mammalian retina, and investigations of others have found that centrins are expressed in different cellular systems (14,27,47). Here we show for the first time co-expression of all four centrin species in one and the same cell type.…”

Section: Discussionsupporting

confidence: 70%

“…Now we addressed the subcellular localization of the centrin isoforms in retinal photoreceptor cells. Although in previous immunocytochemical studies the centrin antibodies used were not always isoform-specific, centrin isoforms 1, 3, and 4 were suggested to localize in cilia or their basal bodies, respectively (12,14,27,47). To prove the differential expression of centrin isoforms, immunocytochemical experiments with the preadsorbed antibodies pMmC1 to pMmC4 were performed in retinal cryosections.…”

Section: Subcellular Localization Of the Complex Partners Transducinmentioning

confidence: 99%

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Differential Expression and Interaction with the Visual G-protein Transducin of Centrin Isoforms in Mammalian Photoreceptor Cells

Gießl

Pulvermüller

Trojan

et al. 2004

Journal of Biological Chemistry

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Section: Discussionsupporting

confidence: 70%

Section: Subcellular Localization Of the Complex Partners Transducinmentioning

confidence: 99%

Differential Expression and Interaction with the Visual G-protein Transducin of Centrin Isoforms in Mammalian Photoreceptor Cells

Gießl

Pulvermüller

Trojan

et al. 2004

Journal of Biological Chemistry

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“…IL-13 is produced by innate lymphoid cells and TH2 cells and induces several characteristic changes in the asthmatic airway epithelium resulting in subepithelial fibrosis, mucinous metaplasia, altered ciliated cell differentiation and function and an increase in goblet cells (15)(16)(17). Impairment of ciliary function has previously been shown for IL-13 in human cell culture models (15,18).…”

Section: Discussionmentioning

confidence: 93%

Effect of TH2 cytokines and interferon gamma on beat frequency of human respiratory cilia

et al. 2016

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Background:In asthmatic airways secondary ciliary dyskinesia contributes to impaired mucociliary clearance. To investigate underlying mechanisms, we studied the effects of cytokines associated with asthma phenotype on the ciliary beat frequency (CBF) in a cell culture model of ciliated human respiratory epithelial cells. Methods: Nasal respiratory epithelial cells of 21 patients were used to prepare multicellular cells (spheroids) in the presence of the T helper (TH) 2 cytokines interleukin (IL)-4, IL-5, IL-9 and IL-13, and the TH1 cytokine interferon gamma (IFN-γ). CBF was determined by high-speed video microscopy. results: Addition of IL-4 and IL-13 and IL-4 + IL-13 decreased the mean CBF by 17, 21, and 22%, respectively, compared with untreated controls. Addition of IL-5 and IL-9 lead to an increase in mean CBF (20 and 10%, respectively). Lower concentrations of IFN-γ (0.1 and 1 ng/ml) decreased mean CBF and higher concentrations (10 ng/ml) increased CBF by 6%. Addition of IFN-γ to IL-13 reversed the effect of IL-13 on the CBF of spheroids. conclusion: Cytokines directly influence the ciliary function of respiratory epithelium and contribute to the impaired mucociliary clearance in asthmatic disease. Our study encourages further research to investigate IFN-γ as a treatment option in diseases with impaired mucociliary clearance like asthma.

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“…In sum, there were no evident changes in the pattern of expression of these ERM proteins in CF tissues, suggesting that ERM protein localization was not affected by Pseudomonas infection and inflammation (in disagreement with Laoukili et al, 2001;Maresso et al, 2004), or a defect in ⌬F508 CFTR trafficking. Importantly, failure of ⌬F508 CFTR to localize in the apical PM of CF cells could not be attributed to faulty ERM protein expression.…”

Section: Expression Of Scaffolding Proteins Ezrin and Ebp50 In Airwaymentioning

confidence: 90%

“…However, it has recently been suggested that scaffolding proteins of the ezrin-radixin-moesin (ERM) family must be correctly localized at the PM for proper CFTR trafficking and function (Short et al, 1998;Mohler et al, 1999;Huang et al, 2003). Epithelial inflammation and remodeling have been reported to alter ERM protein expression (Laoukili et al, 2001), which could impair localization of ⌬F508 protein to the apical PM. To date, there have been no colocalization studies of CFTR (WT or ⌬F508) and ERM proteins in the human lung to test this notion.…”

Section: Introductionmentioning

confidence: 99%

Characterization of Wild-Type and ΔF508 Cystic Fibrosis Transmembrane Regulator in Human Respiratory Epithelia

Kreda

Mall

Mengos

et al. 2005

MBoC

234

210

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Previous studies in native tissues have produced conflicting data on the localization and metabolic fate of WT and ⌬F508 cystic fibrosis transmembrane regulator (CFTR) in the lung. Combining immunocytochemical and biochemical studies utilizing new high-affinity CFTR mAbs with ion transport assays, we examined both 1) the cell type and region specific expression of CFTR in normal airways and 2) the metabolic fate of ⌬F508 CFTR and associated ERM proteins in the cystic fibrosis lung. Studies of lungs from a large number of normal subjects revealed that WT CFTR protein localized to the apical membrane of ciliated cells within the superficial epithelium and gland ducts. In contrast, other cell types in the superficial, gland acinar, and alveolar epithelia expressed little WT CFTR protein. No ⌬F508 CFTR mature protein or function could be detected in airway specimens freshly excised from a large number of ⌬F508 homozygous subjects, despite an intact ERM complex. In sum, our data demonstrate that WT CFTR is predominantly expressed in ciliated cells, and ⌬F508 CFTR pathogenesis in native tissues, like heterologous cells, reflects loss of normal protein processing.

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IL-13 alters mucociliary differentiation and ciliary beating of human respiratory epithelial cells

Cited by 134 publications

References 46 publications

Differential Expression and Interaction with the Visual G-protein Transducin of Centrin Isoforms in Mammalian Photoreceptor Cells

Differential Expression and Interaction with the Visual G-protein Transducin of Centrin Isoforms in Mammalian Photoreceptor Cells

Effect of TH2 cytokines and interferon gamma on beat frequency of human respiratory cilia

Characterization of Wild-Type and ΔF508 Cystic Fibrosis Transmembrane Regulator in Human Respiratory Epithelia

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