Free glycans derived from glycoproteins present in human sera

Iwatsuka, Kinya; Watanabe, Sakie; Kinoshita, Mitsuhiro; Kamisue, Kazuya; Yamada, Keita; Hayakawa, Tetsuo; Suzuki, Tadashi; Kakehi, Kazuaki

doi:10.1016/j.jchromb.2013.03.010

Cited by 19 publications

(12 citation statements)

References 25 publications

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“…C). As reported previously , the major component of complex‐type fOSs in human serum was Hex 2 HexNAc 2 Neu5Ac 2 +Man 3 GlcNAc 2 (FOS‐13), which was also found to be a major N‐glycan structure in human serum (N‐47). The possibility that FOS‐13 is derived from N‐glycans artificially may be ruled out as complex fOSs were not detected in mouse serum, although the concentrations of N‐glycans were comparable between human and mouse.…”

Section: Resultssupporting

confidence: 57%

“…In contrast to the N‐glycome, there have been few studies on the serum fOS‐glycome. To the authors’ knowledge, two studies have investigated the human serum fOSs: one detected complex‐type fOSs, the generation pathway of which is poorly understood, in normal human serum , and the other detected HM/PM‐type fOSs in mouse serum and plasma of a patient suffering from Niemann–Pick disease . HM‐ and PM‐type fOSs are known to be generated from either misfolded glycoproteins or dolichol‐linked oligosaccharides during protein N‐glycosylation, and two forms of fOS, Gn2 (with di‐GlcNAc at the reducing termini) and Gn1 (with a single GlcNAc at the reducing termini, produced by ENGase from Gn2), are known to be present .…”

Section: Resultsmentioning

confidence: 99%

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Quantitative analysis of total serum glycome in human and mouse

et al. 2016

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Model mice are frequently used in drug discovery research. Knowledge of similarities and differences between the mouse and human glycomes is critical when model mice are used for the discovery of glycan-related biomarkers and targets for therapeutic intervention. Since few comparative glycomic studies between human and mouse have been conducted, we performed a comprehensive comparison of the major classes of glycans in human and mouse sera using mass spectrometric and liquid chromatographic analyses. Up to 131 serum glycans, including N-glycans, free oligosaccharides (fOSs), glycosaminoglycans, O-glycans, and glycosphingolipid (GSL)-glycans, were quantified. In both serum samples, N-glycans were the most abundant in the total serum glycome, while fOSs were the least abundant. As expected, the diversity of sialic acid (i.e. Neu5Ac vs. Neu5Gc) was the major species difference between human and mouse in terms of N- and O-glycosylation, while GSL-glycomic profiles were completely different, even when the sialic acid diversity was taken into consideration. Furthermore, total serum glycomics of STAM mouse were unveiled as an initial step to identify novel biomarkers of liver diseases, with which we could identify several glycans with expression significantly increased or decreased expression.

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Section: Resultssupporting

confidence: 57%

Section: Resultsmentioning

confidence: 99%

Quantitative analysis of total serum glycome in human and mouse

et al. 2016

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“…(b) Typical extracellular (serum) FNGs observed in human sera. 78,80 These FNGs are most likely derived from hepatocytes, and they retain N,N´-diacetylchitobiose structure at their reducing termini (Gn2-type). (c) Schematic view of FNGs as a potential biomarker to dictate liver functionality.…”

Section: Resultsmentioning

confidence: 99%

“…These FNGs are assumed to be degradation intermediates, mostly Gn1‐type, bearing a single N ‐acetylglucosamine at their reducing termini. (b) Typical extracellular (serum) FNGs observed in human sera . These FNGs are most likely derived from hepatocytes, and they retain N,N´ ‐diacetylchitobiose structure at their reducing termini (Gn2‐type).…”

Section: “Free” N‐glycans May Serve As a Biomarker Of Liver Functionamentioning

confidence: 99%

Functional glycomics: Application to medical science and hepatology

Miyoshi

Kamada

Suzuki

2019

Hepatology Research

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Glycomics refers to the comprehensive analysis of glycans. Recent progress in glycotechnology enables the determination of a variety of biological functions of glycans. Among different glycosylation patterns, certain types of aberrant glycosylation are linked to cancer and/or inflammation, and thus have biological importance. Glycotechnology has been applied to many fields of medical science, including hepatology. In particular, dramatic changes in glycosylation are observed in the progression of liver diseases. As the liver produces so many serum glycoproteins, changes in glycosylation of these proteins might provide useful disease biomarkers. Furthermore, many patients with genetic diseases of glycosylation who have liver dysfunction have been found as a result from whole genome sequencing, and various kinds of glycotherapy have been developed, especially in immunotherapy. In this review, we describe our basic knowledge of glycobiology and discuss the application of these data to medical science, especially hepatology.

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“…free oligosaccharides that are structurally related to N-glycans). Although Iwatsuka et al (33) reported the detection of extracellular FOGs with structures similar to mucintype O-glycan chains in human sera, the occurrence of intracellular FOGs has not been reported in any system. In this study, we serendipitously discovered that a series of novel free glycans that are structurally related to O-mannosyl glycans are produced only when the yeast cells are cultured in media containing mannose as the sole carbon source.…”

Section: Discussionmentioning

confidence: 98%