Abstract
Based on our previous studies, differential analysis of N-glycan expression bound on serum haptoglobin reveals the quantitative variation on gastric cancer patients. In this prospective case-control study, we explore the clinically relevant glycan markers for gastric cancer diagnosis. Serum samples were collected from patients with gastric cancer (n = 44) and healthy control (n = 44). N-glycans alteration was monitored by intact analysis of Hp using liquid chromatography–mass spectrometry followed by immunoaffinity purification with the serum samples. Intensity and frequency markers were defined depending on the mass spectrometry data analysis. Multiple markers were found with high diagnostic efficacy. As intensity markers (I-marker), six markers were discovered with the AUC > 0.8. The high efficiency markers exhibited AUC of 0.93 with a specificity of 86% when the sensitivity was set to 95%. We additionally established frequency marker (f-marker) panels based on the tendency of high N-glycan expression. The AUC to conclude patients and control group were 0.82 and 0.79, respectively. This study suggested that N-glycan variation of serum haptoglobin were associated with patients with gastric cancer and might be a promising marker for the cancer screening.
Highlights
Gastric cancer (GC) is the most frequently occurring malignancy in Korea, and one of the main causes of cancer death [1]
This study suggested that N-glycan variation of serum haptoglobin were associated with patients with gastric cancer and might be a promising marker for the cancer screening
Our results provide further insight into the glycomics based on mass spectrometry (MS) screening in cancer development, and may provoke more detailed investigations leading to identification of a panel of diagnostic serological biomarkers applicable to early detection of cancer
Summary
Gastric cancer (GC) is the most frequently occurring malignancy in Korea, and one of the main causes of cancer death [1]. Aberrant glycosylation is a major post-translational modification (PTM) of proteins, frequently observed in cancer cells and tissues [4,5,6]. A major acute-phase glycoprotein comprising 0.4–2.6% of total blood proteins, consists of two α- and two β-subunits whose glycosylation level changes in various types of cancer and inflammation [8, 9]. Direct analysis of intact glycoprotein has merits such as simple, easy handling of sample preparation and time saving for analysis. This method could have thereby high potential to discover the novel cancer biomarkers with aberrant glycosylation
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