BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//132.216.98.100//NONSGML kigkonsult.se iCalcreator 2.20.4//
BEGIN:VEVENT
UID:20261101T070225EST-8348LHRvLM@132.216.98.100
DTSTAMP:20261101T120225Z
DESCRIPTION:NADPH oxidases (NOX) represent a family of dedicated oxidant-ge
 nerating enzymes that serve widespread biological roles\, ranging from hos
 t defense\, cell proliferation or differentiation\, to immune regulation. 
 In the lung\, the NOX isoform DUOX1 is expressed primarily within the resp
 iratory epithelium\, and our past studies have demonstrated its role in in
 nate epithelial responses to various injurious triggers (including pathoge
 ns and asthma-inducing allergens)\, by mediating various wound responses v
 ia cellular redox signaling pathways involving tyrosine kinases such as SR
 C and EGFR. Among these DUOX1-mediated injury responses is the epithelial 
 secretion of the alarmin IL-33\, which serves to maintain epithelial integ
 rity by activating type 2 immune responses. We also demonstrated that epit
 helial DUOX1 expression and activation is enhanced during allergic asthma\
 , and contributes to type 2 inflammation and airway remodeling as major fe
 atures of allergic airways disease. More recently\, we also uncovered an a
 pparent functional role for DUOX1 in macrophages\, indicating its contribu
 ting roles in macrophage recruitment and profibrotic activation in models 
 of allergic airway inflammation or pulmonary fibrosis. Lastly\, based on p
 revious studies linking DUOX1 to extracellular oxidative crosslinking proc
 esses in various organisms via activation of secreted heme peroxidases\, w
 e are currently exploring a link between DUOX1 and peroxidasin (PXDN)\, a 
 recently identified heme peroxidase involved in collagen IV crosslinking w
 ithin basement membranes (BM)\, and have obtained preliminary evidence for
  a concerted role of DUOX1 and PXDN in oxidative matrix remodeling that ma
 y promote lung stiffening in fibrotic lung disease. Curiously\, these PXDN
 -mediated cross-linking mechanisms rely on the presence of bromide (Br-)\,
  and also give rise to alternative oxidative ECM modifications\, including
  the formation of 3-bromo-tyrosine (Br-Y) in several BM proteins. The rele
 vance and therapeutic implications of these various oxidative mechanisms f
 or fibrotic lung disease will be discussed.\n\n \n\nThis seminar will take
  place in-person and online ( details in attached poster below) All are we
 lcome!\n
DTSTART:20231201T160000Z
DTEND:20231201T170000Z
LOCATION:Room 1034\, McIntyre Medical Building\, CA\, QC\, Montreal\, H3G 1
 Y6\, 3655 promenade Sir William Osler
SUMMARY:Physiology Seminar\, Co- hosted by Cystic Fibrosis Translational Re
 search Centre: Dr. Albert van der Vliet\, 'The NADPH Oxidase DUOX1 in Redo
 x-Dependent Epithelial Homeostasis\, Extracellular Matrix Remodeling\, and
  Fibrotic lung disease'
URL:https://www.mcgill.ca/physiology/channels/event/physiology-seminar-co-h
 osted-cystic-fibrosis-translational-research-centre-dr-albert-van-der-vlie
 t-352832
END:VEVENT
END:VCALENDAR
