Lung cancer is a severe disease for which better diagnostic and therapeutic approaches
are urgently needed. Increasing evidence implies that aberrant protein glycosylation
plays a crucial role in the pathogenesis and progression of lung cancer. Differences
in glycosylation patterns have been previously observed between healthy and cancerous
samples as well as between different lung cancer subtypes, which suggests untapped
diagnostic potential. In addition, understanding the changes mediated by glycosylation
may shed light on possible novel therapeutic targets and personalized treatment strategies
for lung cancer patients. Mass spectrometry based glycomics and glycoproteomics have
emerged as powerful tools for in‐depth characterization of changes in protein glycosylation,
providing valuable insights into the molecular basis of lung cancer. This paper reviews
the literature on the analysis of protein glycosylation in lung cancer using mass
spectrometry, which is dominated by manuscripts published over the past 5 years. Studies
analyzing N‐glycosylation, O‐glycosylation, and glycosaminoglycan patterns in tissue,
serum, plasma, and rare biological samples of lung cancer patients are highlighted.
The current knowledge on the potential utility of glycan and glycoprotein biomarkers
is also discussed.
