An insight into the cells' glycans and lectin-glycosensing sites

• 来源期刊: 科学通报（英文版）
• 年，卷（期）: 2016,（2）
• 页码范围: 108-109
• 页数: 2页
• 语种: 中文
• DOI: 10.1007/s11434-015-0933-6

摘要

Glycosylation produces a diverse and abundant repertoire of glycans that help protein folding and cellular secretion [1].Glycoproteins often sprout sialic acid (alias N-acetyl neuraminic acid,abbreviated as Neu5Ac) at the termini of their N-and O-glycans in a process called sialylation [2].Alterations to the normal function of the glycosylation machinery,including increased branching of N-linked glycans and sialylation,are major hallmarks of cancer progression.Particularly,increased sialylation on the cell surface induces tumor proliferation by promoting cell detachment from primary tumors through charge repulsion [3].Despite the potential of increased or altered sialylation as diagnostic and prognostic biomarkers,there is still no early glycosensing platform that can be ubiquitously applied to detect glycans sialylation in diverse bio-samples with high selectivity and sensitivity.