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

Cell Biosci

Research Team for Geriatric Medicine (Vascular Medicine), Tokyo Metropolitan Institute of Gerontology, 35-2 Sakae-cho, Itabashi-ku, Tokyo, 173-0015 Japan.

Published: February 2016

AI Article Synopsis

  • Glycans are crucial for various biological functions and may serve as indicators of physiological aging; however, specific glycans linked to aging remain largely unknown.
  • Researchers studied glycan changes in human fibroblasts from donors of different ages, finding distinct differences in certain glycans between cells from elderly and fetal sources.
  • The study highlighted a decrease in sialylated glycans associated with aging, suggesting that glycan profiling could be a valuable method for identifying aging biomarkers.

Article Abstract

Background: 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.

Results: 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.

Conclusions: 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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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4757982PMC
http://dx.doi.org/10.1186/s13578-016-0079-5DOI Listing

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