title: Glycosylation Changes in Serum Proteins Identify Patients with Pancreatic Cancer.
abstract: 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.
authors.affiliation: AGH University of Science and Technology , Krakow, Poland.
authors.forename: Anna
authors.identifier: 0000-0002-8108-7595
authors.initials: A
authors.lastname: Drabik
authors.affiliation: AGH University of Science and Technology , Krakow, Poland.
authors.forename: Anna
authors.initials: A
authors.lastname: Bodzon-Kulakowska
authors.affiliation: AGH University of Science and Technology , Krakow, Poland.
authors.forename: Piotr
authors.identifier: 0000-0003-4511-1241
authors.initials: P
authors.lastname: Suder
authors.affiliation: AGH University of Science and Technology , Krakow, Poland.|Centre of Polymer and Carbon Materials, Polish Academy of Sciences , Zabrze, Poland.
authors.forename: Jerzy
authors.initials: J
authors.lastname: Silberring
authors.affiliation: First Department of Surgery, Jagiellonian University Medical College , Krakow, Poland.
authors.forename: Jan
authors.initials: J
authors.lastname: Kulig
authors.affiliation: First Department of Surgery, Jagiellonian University Medical College , Krakow, Poland.
authors.forename: Marek
authors.initials: M
authors.lastname: Sierzega
mesh_terms: D000368:Aged; D014408:Biomarkers, Tumor / Q000097:blood*; D000939:Epitopes / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D005260:Female; D006031:Glycosylation; D006242:Haptoglobins / Q000032:analysis*; D054884:Host-Pathogen Interactions / Q000235:genetics; D006801:Humans; D053680:Leukemia Inhibitory Factor Receptor alpha Subunit / Q000097:blood*; D008297:Male; D008868:Microtubule Proteins / Q000097:blood*; D008875:Middle Aged; D009687:Nuclear Proteins / Q000097:blood*; D010190:Pancreatic Neoplasms / Q000097:blood* / Q000235:genetics / Q000473:pathology; D011134:Polysaccharides / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D017510:Protein Folding; D011499:Protein Processing, Post-Translational / Q000235:genetics; D040901:Proteomics; D033921:Vesicular Transport Proteins / Q000097:blood*
chemical_list: D014408:Biomarkers, Tumor; C509238:CEP350 protein, human; D000939:Epitopes; C485359:HP protein, human; D006242:Haptoglobins; C507840:LIFR protein, human; D053680:Leukemia Inhibitory Factor Receptor alpha Subunit; D008868:Microtubule Proteins; D009687:Nuclear Proteins; D011134:Polysaccharides; C429654:VPS13A protein, human; D033921:Vesicular Transport Proteins
keywords: CE350; HPT; LIFR; VP13A; glycosylation; pancreatic cancer