title: Glycans and glycoproteins as specific biomarkers for cancer.
abstract: Protein glycosylation and other post-translational modifications are involved in potentially all aspects of human growth and development. Defective glycosylation has adverse effects on human physiological conditions and accompanies many chronic and infectious diseases. Altered glycosylation can occur at the onset and/or during tumor progression. Identifying these changes at early disease stages may aid in making decisions regarding treatments, as early intervention can greatly enhance survival. This review highlights some of the efforts being made to identify N- and O-glycosylation profile shifts in cancer using mass spectrometry. The analysis of single or panels of potential glycoprotein cancer markers are covered. Other emerging technologies such as global glycan release and site-specific glycosylation analysis and quantitation are also discussed. Graphical Abstract Steps involved in the biomarker discovery.
authors: Department of Chemistry, University of California, Davis, CA, 95616, USA.
authors: Muchena J
authors: MJ
authors: Kailemia
authors: Department of Chemistry, University of California, Davis, CA, 95616, USA.
authors: Dayoung
authors: D
authors: Park
authors: Department of Chemistry, University of California, Davis, CA, 95616, USA. cblebrilla@ucdavis.edu.
authors: Carlito B
authors: CB
authors: Lebrilla
mesh_terms: D015415:Biomarkers; D006023:Glycoproteins / Q000032:analysis* / Q000737:chemistry; D006801:Humans; D013058:Mass Spectrometry; D009369:Neoplasms / Q000175:diagnosis*; D011134:Polysaccharides / Q000032:analysis* / Q000737:chemistry; D011499:Protein Processing, Post-Translational
chemical_list: D015415:Biomarkers; D006023:Glycoproteins; D011134:Polysaccharides
keywords: Cancer; Disease biomarker; Glycomics; Glycoproteomics; Mass spectrometry; Site-specific glycosylation