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• W2894920234 abstract "N-Glycosylation affects protein functions such as location, stability, and susceptibility to proteases. Desmosomes in keratinocytes are essential to maintain epidermal tissue integrity to protect against environmental insults. However, it is not yet known whether N-glycosylation affects desmosomal functions in primary keratinocytes. Tunicamycin is an inhibitor of N-glycosylation that has been a useful tool in glycobiology. Therefore, we investigated the effect of inhibiting N-glycosylation by tunicamycin treatment on desmosomes in primary keratinocytes. In our experiments, cell–cell adhesive strength was reduced in tunicamycin-treated primary keratinocytes. TEM showed that desmosome formation was impaired by tunicamycin. Desmogleins (Dsgs) 1 and 3, which constitute the core structure of desmosomes, were well transported to the cell–cell borders, but the amount decreased and showed an aberrant distribution at the cell borders in tunicamycin-treated keratinocytes. The stability of both desmoglein proteins was also reduced, and they were degraded through both proteasomal and lysosomal pathways, although inhibiting degradation did not restore the cell–cell adhesion. Finally, tunicamycin induced desmosomal instability, enhancing their disassembly. In conclusion, these results indicate that N-glycosylation is critical to the desmosome complex to maintain cell–cell adhesive strength in primary keratinocytes." @default.
• W2894920234 created "2018-10-12" @default.
• W2894920234 creator A5006498091 @default.
• W2894920234 creator A5056846121 @default.
• W2894920234 date "2018-11-28" @default.
• W2894920234 modified "2023-10-14" @default.
• W2894920234 title "Inhibition of N-glycosylation by tunicamycin attenuates cell–cell adhesion via impaired desmosome formation in normal human epidermal keratinocytes" @default.
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• W2894920234 doi "https://doi.org/10.1042/bsr20171641" @default.
• W2894920234 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6259015" @default.
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