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IL-13 Impairs Tight Junctions in Airway Epithelia

IL-13 Impairs Tight Junctions in Airway Epithelia

Hanna Schmidt, Peter Braubach, Carolin Schilpp, Robin Lochbaum, Kathrin Neuland, Kristin Thompson, Danny Jonigk, Manfred Frick, Paul Dietl, Oliver H Wittekindt

Int J Mol Sci. 2019 Jun 30;20(13):3222.

PMID: 31262043

Abstract:

Interleukin-13 (IL-13) drives symptoms in asthma with high levels of T-helper type 2 cells (Th2-cells). Since tight junctions (TJ) constitute the epithelial diffusion barrier, we investigated the effect of IL-13 on TJ in human tracheal epithelial cells. We observed that IL-13 increases paracellular permeability, changes claudin expression pattern and induces intracellular aggregation of the TJ proteins zonlua occludens protein 1, as well as claudins. Furthermore, IL-13 treatment increases expression of ubiquitin conjugating E2 enzyme UBE2Z. Co-localization and proximity ligation assays further showed that ubiquitin and the proteasomal marker PSMA5 co-localize with TJ proteins in IL-13 treated cells, showing that TJ proteins are ubiquitinated following IL-13 exposure. UBE2Z upregulation occurs within the first day after IL-13 exposure. Proteasomal aggregation of ubiquitinated TJ proteins starts three days after IL-13 exposure and transepithelial electrical resistance (TEER) decrease follows the time course of TJ-protein aggregation. Inhibition of JAK/STAT signaling abolishes IL-13 induced effects. Our data suggest that that IL-13 induces ubiquitination and proteasomal aggregation of TJ proteins via JAK/STAT dependent expression of UBE2Z, resulting in opening of TJs. This may contribute to barrier disturbances in pulmonary epithelia and lung damage of patients with inflammatory lung diseases.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP454675764	13,6-N-Sulfinylacetamidopentacene		454675-76-4	Price
IAR4241405	Ubiquitin Carrier Protein H2 human			Price

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