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- W2896914779 abstract "Mucin glycoproteins on the ocular surface are rich in O-glycans and have important roles in the protection from physical, chemical and microbial impact. In this work, we have cultured human corneal and conjunctival epithelial cells to examine the glycosyltransferase activities that synthesize the O-glycans of mucins. The results indicate that ocular surface epithelial cells have active enzymes that synthesize O-glycans with sialylated core 1, Galβ1-3GalNAcα, and core 2, GlcNAcβ1-6(Galβ1-3)GalNAcα structures which corresponds to previous structural studies. Eye cells also have enzymes that synthesize complex N-glycans that are found on mucins. Results from treatment of eye cells with TNFα suggest that epithelial O-glycosylation changes in a dynamic fashion during inflammatory stimuli of the eye surface." @default.
- W2896914779 created "2018-10-26" @default.
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- W2896914779 creator A5058971301 @default.
- W2896914779 creator A5061857544 @default.
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- W2896914779 date "2018-12-01" @default.
- W2896914779 modified "2023-10-18" @default.
- W2896914779 title "Glycosylation pathways of human corneal and conjunctival epithelial cell mucins" @default.
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- W2896914779 doi "https://doi.org/10.1016/j.carres.2018.10.004" @default.
- W2896914779 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6311131" @default.
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- W2896914779 hasPublicationYear "2018" @default.
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