Chemoenzymatic profiling of multiple glycosylation by a single one-step probe

ABSTRACT: Protein glycosylation, mainly divided into N-glycosylation and O-glycosylation, is the most prevalent and complex protein posttranslational modification. However, profiling of multiple glycosylation types from a given biological sample is still a challenging issue in glycoscience. Here, a “one-step probe”, directly carried enrichment support, was designed and synthesized. This probe could be accepted by two substrate-specific sialyltransferases to label and enrich N-linked glycans and O-linked glycans in a one-step manner. Combing mass spectrometry (MS) technology, multiple glycoproteomes including N-glycosylation, core fucosylation and truncated mucin-type O-glycosylation can be profiled simultaneously. By this strategy, multiple glycosylation from two breast cancer cell lines including less invasive (MCF7) and highly invasive (MDA-MB-468) were profiled. The results showed that core fucosylation changed significantly while mucin-type O-glycosylation also changed to a lesser extent in two cell lines. Protein-protein interaction (PPI) network analysis showed that the core-fucosylated sites of key genes in ferroptosis, a novel type of iron-dependent cell death, were significantly upregulated in MDA-MB-468. These results indicated that core fucosylation could be a potential biomarker and drug target for highly invasive breast cancer.

ORGANISM(S): Homo Sapiens

SUBMITTER: Hu Zhou  

PROVIDER: PXD052125 | iProX | Thu May 09 00:00:00 BST 2024

REPOSITORIES: iProX