Tongue Cancer Patients Can be Distinguished from Healthy Controls by Specific N-Glycopeptides Found in Serum

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http://hdl.handle.net/10138/325748

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Saraswat , M , Mäkitie , A , Tohmola , T , Dickinson , A , Saraswat , S , Joenväärä , S & Renkonen , S 2018 , ' Tongue Cancer Patients Can be Distinguished from Healthy Controls by Specific N-Glycopeptides Found in Serum ' , Proteomics. Clinical applications , vol. 12 , no. 6 , 1800061 . https://doi.org/10.1002/prca.201800061

Title: Tongue Cancer Patients Can be Distinguished from Healthy Controls by Specific N-Glycopeptides Found in Serum
Author: Saraswat, Mayank; Mäkitie, Antti; Tohmola, Tiialotta; Dickinson, Amy; Saraswat, Shruti; Joenväärä, Sakari; Renkonen, Suvi
Contributor organization: HUSLAB
Transplantation Laboratory
Medicum
University of Helsinki
Clinicum
Department of Ophthalmology and Otorhinolaryngology
Korva-, nenä- ja kurkkutautien klinikka
HUS Head and Neck Center
Date: 2018-11
Language: eng
Number of pages: 8
Belongs to series: Proteomics. Clinical applications
ISSN: 1862-8346
DOI: https://doi.org/10.1002/prca.201800061
URI: http://hdl.handle.net/10138/325748
Abstract: Purpose Experimental design There are no blood biomarkers to detect early-stage oral cavity squamous cell carcinoma (OSCC) prior to clinical signs. Most OSCC incidence is associated with significant morbidity and poor survival. The authors aimed to use mass-spectrometry (MS) technology to find specific N-glycopeptides potentially serving as serum biomarkers for preclinical OSCC screening. Serum samples from 14 patients treated for OSCC (stage I or stage IV) with 12 age- and sex-matched controls are collected. Quantitative label-free N-glycoproteomics is performed, with MS/MS analysis of the statistically significantly different N-glycopeptides. Results Conclusions and clinical relevance Combined with a database search using web-based software (GlycopeptideID), MS/MS provided detailed N-glycopeptide information, including glycosylation site, glycan composition, and proposed structures. Thirty-eight tryptic N-glycopeptides are identified, having 19 unique N-glycosylation sites representing 14 glycoproteins. OSCC patients, including stage I tumors, can be differentiated from healthy controls based on the expression levels of these glycoforms. N-glycopeptides of IgG1, IgG4, haptoglobin, and transferrin have statistically significant different abundances between cases and controls. The authors are the first to suggest specific N-glycopeptides to serve as potential serum biomarkers to detect preclinical OSCC in patients. These N-glycopeptides are the lead candidates for validation as future diagnostic modalities of OSCC as early as stage I.
Subject: HNSCC
IgG
N-glycoproteomics
OSCC
transferrin
SQUAMOUS-CELL CARCINOMA
NECK-CANCER
OVARIAN-CANCER
GLYCOPROTEIN
HEAD
GLYCOSYLATION
BIOMARKERS
EXPRESSION
CONTRIBUTE
PROTEINS
3125 Otorhinolaryngology, ophthalmology
3122 Cancers
Peer reviewed: Yes
Rights: unspecified
Usage restriction: openAccess
Self-archived version: acceptedVersion


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