title: Mass spectrometry methods for studying glycosylation in cancer.
abstract: Protein glycosylation is a highly complex and regulated posttranslational modification. In this process several glycosyltransferase families are involved. In cancer this delicate equilibrium is disrupted leading to glycosylation changes on glycoconjugates, namely, glycoproteins. One of the major consequences is the increase of sialylated oligosaccharide chains in glycoproteins. Here we describe an experimental methodology focused in the enrichment and characterization of sialic acid containing glycopeptides by MALDI mass spectrometry and the subsequent data analysis.
authors.affiliation: Institute of Molecular Pathology and Immunology of the University of Porto (IPATIMUP), Porto, Portugal.
authors.forename: Hugo
authors.initials: H
authors.lastname: Osório
authors.forename: Celso A
authors.initials: CA
authors.lastname: Reis
mesh_terms: D014408:Biomarkers, Tumor / Q000097:blood; D001798:Blood Proteins / Q000737:chemistry*; D006020:Glycopeptides / Q000737:chemistry*; D006031:Glycosylation; D006801:Humans; D019158:N-Acetylneuraminic Acid / Q000032:analysis* / Q000737:chemistry; D009369:Neoplasms / Q000097:blood*; D009844:Oligosaccharides / Q000032:analysis* / Q000737:chemistry; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
chemical_list: D014408:Biomarkers, Tumor; D001798:Blood Proteins; D006020:Glycopeptides; D009844:Oligosaccharides; D019158:N-Acetylneuraminic Acid