In‐depth investigation of altered glycosylation in human haptoglobin associated cancer by mass spectrometry

Abstract Serum haptoglobin (Hp), a highly sialylated biomolecule with four N‐glycosylation sites, is a positive acute‐phase response glycoprotein that acts as an immunomodulator. Hp has gained considerable attention due to its potential as a signature molecule that exhibits aberrant glycosylation in inflammatory disorders and malignancies. Its glycosylation can be analyzed qualitatively and quantitatively by various methods using mass spectrometry. In this review, we have provided a brief overview of Hp structure and biological function and described mass spectrometry‐based techniques for analyzing glycosylation ranging from macroheterogeneity to microheterogeneity of Hp in diseases and cancer. The sugars on haptoglobin can be a sweet bridge to link the potential of cancer‐specific biomarkers to clinically relevant applications.