Glycosylation Changes in Serum Proteins Identify Patients with Pancreatic Cancer.
Anna DrabikAnna Bodzon-KulakowskaPiotr SuderJerzy SilberringJan KuligMarek SierzegaPublished in: Journal of proteome research (2017)
After more than a decade of biomarker discovery using advanced proteomic and genomic approaches, very few biomarkers have been involved in clinical diagnostics. Most candidate biomarkers are focused on the protein component. Targeting post-translational modifications (PTMs) in combination with protein sequences will provide superior diagnostic information with regards to sensitivity and specificity. Glycosylation is one of the most common and functionally important PTMs. It plays a central role in many biological processes, including protein folding, host-pathogen interactions, immune response, and inflammation. Cancer-associated aberrant glycosylation has been identified in various types of cancer. Expression of cancer-specific glycan epitopes represents an excellent opportunity for diagnostics and potentially specific detection of tumors. Here, we report four proteins (LIFR, CE350, VP13A, HPT) found in sera from pancreatic cancer patients carrying aberrant glycan structures as compared to those of controls.
Keyphrases
- papillary thyroid
- immune response
- protein protein
- binding protein
- squamous cell
- oxidative stress
- amino acid
- poor prognosis
- small molecule
- high resolution
- label free
- healthcare
- molecular dynamics simulations
- mass spectrometry
- single cell
- lymph node metastasis
- young adults
- dendritic cells
- long non coding rna
- cell surface
- inflammatory response
- toll like receptor
- single molecule
- loop mediated isothermal amplification
- candida albicans
- sensitive detection
- genome wide