Mass Spectrometry-Based Proteomics Methods for Systematic Identification and Quantification of Protein...

Area of Science:

• Biochemistry and Molecular Biology
• Proteomics
• Glycoscience

Background:

• Protein O-glycosylation is a prevalent post-translational modification crucial for cellular functions.
• Dysregulation of O-glycosylation is linked to significant diseases, including cancer and neurodegenerative disorders.
• Mass spectrometry (MS)-based proteomics offers powerful tools for O-glycoproteome characterization.

Purpose of the Study:

• To review recent advancements in MS-based proteomics for characterizing protein O-glycosylation.
• To highlight methods overcoming challenges in low abundance, heterogeneity, and sample complexity.
• To discuss tools for global and site-specific O-glycopeptide analysis.

Main Methods:

• Overview of O-glycosylation biosynthetic pathways.
• Discussion of O-glycopeptide enrichment strategies for diverse glycan structures.
• Exploration of MS dissociation techniques for intact glycopeptide profiling.
• Inclusion of quantitative approaches for biological and biomedical research.
• Examination of computational tools for O-glycopeptide identification and site localization.

Main Results:

• Recent MS-based proteomics methods enable more comprehensive characterization of protein O-glycosylation.
• Advances address challenges related to low glycoprotein abundance and glycan heterogeneity.
• Improved enrichment, dissociation, and computational tools enhance O-glycopeptide identification and quantification.
• Progress in MS-based glycoproteomics facilitates deeper understanding of O-glycosylation's biological roles.

Conclusions:

• Advancements in MS-based glycoproteomics are essential for understanding protein O-glycosylation.
• These techniques are critical for gaining insights into the roles of O-glycosylation in human health and disease.
• Further development of MS-based methods will accelerate discoveries in O-glycoproteomics.