English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Background  Reduction of COL4A3 in asthmatic airways, one of the six isoforms of collagen 4 results in increased inflammation and angiogenesis implicating it as a central part of asthma pathogenesis. However, the path underlying these diminished COL4A3 levels has been elusive to date. This study investigated a possible mechanism underlying the reduction of COL4A3 expression.    Methods  Bronchial biopsies of n=76 asthmatics and n=83 controls were subjected to RNA-sequencing and DNA methylation bead arrays to identify expression and methylation changes. The binding of ZNF263 was analysed by ChiP-Seq coupled with qPCR. Effects of  ZNF263  silencing, using siRNA, on the  COL4A3  expression were studied by qPCR.    Results   COL4A3  expression was significantly reduced in bronchial biopsies compared to healthy controls whereas DNA methylation levels at cg11797365 were increased.  COL4A3  expression levels were significantly low in asthmatics without ICS use whereas the expression was not statistically different between asthmatics using ICS and controls. Methylation levels at cg11797365  in vitro  were increased upon consecutive rhinovirus infections.    Conclusion  Our data indicates an epigenetic modification as a contributing factor for the loss of  COL4A3  expression in asthmatic airway epithelium.

COL4A3 expression in asthmatic epithelium depends on intronic methylation and ZNF263 binding