Protection of Human Corneal Epithelial Cells from Hypoxia-Induced Disruption of Barrier Function by Keratinocyte Growth Factor

2008 ◽  
Vol 49 (6) ◽  
pp. 2432 ◽  
Author(s):  
Shinichiro Teranishi ◽  
Kazuhiro Kimura ◽  
Koji Kawamoto ◽  
Teruo Nishida
Keyword(s):  
Growth Factor ◽  
Epithelial Cells ◽  
Barrier Function ◽  
Keratinocyte Growth Factor ◽  
Corneal Epithelial Cells ◽  
Corneal Epithelial ◽  
Human Corneal Epithelial Cells

scholarly journals The O-GlcNAc modification promotes terminal differentiation of human corneal epithelial cells

Glycobiology ◽  
2020 ◽  
Vol 30 (11) ◽  
pp. 872-880 ◽  
Author(s):  
Nicole M McColgan ◽  
Marissa N Feeley ◽  
Ashley M Woodward ◽  
Damien Guindolet ◽  
Pablo Argüeso
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Ocular Surface ◽  
Barrier Function ◽  
Terminal Differentiation ◽  
Corneal Epithelial Cell ◽  
Corneal Epithelial Cells ◽  
Corneal Epithelial ◽  
Human Corneal Epithelial Cells ◽  
Glcnac Transferase

Abstract Dynamic modification of nuclear and cytoplasmic proteins with O-linked β-N-acetylglucosamine (O-GlcNAc) plays an important role in orchestrating the transcriptional activity of eukaryotic cells. Here, we report that the O-GlcNAc modification contributes to maintaining ocular surface epithelial homeostasis by promoting mucin biosynthesis and barrier function. We found that induction of human corneal epithelial cell differentiation stimulated the global transfer of O-GlcNAc to both nuclear and cytosolic proteins. Inflammatory conditions, on the other hand, were associated with a reduction in the expression of O-GlcNAc transferase at the ocular surface epithelia. Loss- and gain-of-function studies using small interfering RNA targeting O-GlcNAc transferase, or Thiamet G, a selective inhibitor of O-GlcNAc hydrolase, respectively, revealed that the presence of O-GlcNAc was necessary to promote glycocalyx barrier function. Moreover, we found that Thiamet G triggered a correlative increase in both surface expression of MUC16 and apical epithelial cell area while reducing paracellular permeability. Collectively, these results identify intracellular protein O-glycosylation as a novel pathway responsible for promoting the terminal differentiation of human corneal epithelial cells.

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