N- and O-glycan cell surface protein modifications associated with cellular senescence and human aging

Cell & Bioscience
Yoko ItakuraMasashi Toyoda

Abstract

Glycans play essential roles in biological functions such as differentiation and cancer. Recently, glycans have been considered as biomarkers for physiological aging. However, details regarding the specific glycans involved are limited. Here, we investigated cellular senescence- and human aging-dependent glycan changes in human diploid fibroblasts derived from differently aged skin donors using a lectin microarray. We found that α2-6sialylated glycans in particular differed between elderly- and fetus-derived cells at early passage. However, both cell types exhibited sequentially decreasing α2-3sialylated O-glycan structures during the cellular senescence process and showed similar overall glycan profiles. We observed a senescence-associated decrease in sialylation and increase in galactose exposure. Therefore, glycan profiling using lectin microarrays might be useful for the characterization of biomarkers of aging.

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Citations

Oct 28, 2019·Naunyn-Schmiedeberg's Archives of Pharmacology·Radziejewska Iwona, Supruniuk Katarzyna
Jun 12, 2019·In Vitro Cellular & Developmental Biology. Animal·Tirth UpretyRadhey S Kaushik
Apr 20, 2017·Stem Cell Research & Therapy·Norihiko SasakiMasashi Toyoda
Mar 11, 2020·ChemistryOpen·Kai DangAirong Qian
Sep 23, 2020·The FEBS Journal·Estela González-GualdaDaniel Muñoz-Espín
Jun 15, 2021·Frontiers in Molecular Biosciences·Patricia FranzkaChristian A Hübner

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Methods Mentioned

BETA
glycosylation
PCA
Protein Extraction

Software Mentioned

[UNK] Tools Signal Capture
TIGR MultiExperiment Viewer
[UNK] Tools Pro

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