Altered microheterogeneity at several N-glycosylation sites in OPSCC in constant protein expression conditions.

ABSTRACT: Protein glycosylation responds sensitively to disease states. It is implicated in every hallmark of cancer and has recently started to be considered as a hallmark itself. Changes in N-glycosylation microheterogeneity are more dramatic than those of protein expression due to the non-template nature of protein glycosylation. This enables their potential use in serum-based diagnostics. Here, we perform glycopeptidomics on serum from patients with oropharyngeal squamous cell carcinoma (OPSCC), compared to controls and comparing between cancers based on etiology (human papilloma virus- positive or negative). Using MS2, we then targeted glycoforms, significantly different between the groups, to identify their glycopeptide compositions. Simultaneously we investigate the same serum proteins, compa

SUBMITTER: Dickinson A 

PROVIDER: S-EPMC10782471 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature