N- and O-glycan cell surface protein modifications associated with cellular senescence and human aging.
N- and O-glycan cell surface protein modifications associated with cellular senescence and human aging.
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DOI：
10.1186/s13578-016-0079-5
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发表时间：
2016
影响因子：
7.5
通讯作者：
Toyoda M
中科院分区：
文献类型：
--
作者：
Itakura Y;Sasaki N;Kami D;Gojo S;Umezawa A;Toyoda M
聚糖在分化和癌症等生物学功能中发挥着重要作用。最近，聚糖被认为是生理衰老的生物标志物。然而，有关所涉及的特定聚糖的细节是有限的。在这里，我们使用凝集素微阵列研究了来自不同年龄皮肤供体的人二倍体成纤维细胞中的细胞衰老和人类衰老依赖性聚糖变化。我们发现，早期传代时，老年细胞和胎儿来源的细胞中的 α2-6 唾液酸化聚糖尤其不同。然而，两种细胞类型在细胞衰老过程中均表现出α2-3唾液酸化O-聚糖结构依次减少，并表现出相似的总体聚糖谱。我们观察到与衰老相关的唾液酸化减少和半乳糖暴露增加。因此，使用凝集素微阵列进行聚糖分析可能有助于表征衰老生物标志物。本文的在线版本 (doi:10.1186/s13578-016-0079-5) 包含补充材料，可供授权用户使用。
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. The online version of this article (doi:10.1186/s13578-016-0079-5) contains supplementary material, which is available to authorized users.