Xylose Migration During Tandem Mass Spectrometry of <i>N</i>-Linked Glycans

Hecht, Elizabeth S.; Loziuk, Philip L.; Muddiman, David C.

doi:10.1007/s13361-016-1588-5

Cited by 23 publications

(17 citation statements)

References 24 publications

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“…The structure of this characteristic glycan was determined using periodate oxidation, partial acid hydrolysis (PAH), enzymatic digestion and permethylation. Periodate oxidation products were subjected to MS with sodium adduct ions for inhibition of pentose migration 18 , 19 . The MS 2 spectrum of the periodate-cleaved product from the sodiated precursor ion at m/z 1059 indicated the glycan structure was Hex1-3/4(Pen1-3/4)HexNAc1-4Hex1-3Hex1-4HexNAc-PA (Fig.…”

Section: Resultsmentioning

confidence: 99%

Occurrence of a d-arabinose-containing complex-type free-N-glycan in the urine of cancer patients

Tanaka-Okamoto

Hanzawa

Murakami

et al. 2022

Sci Rep

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Urinary free-glycans are promising markers of disease. In this study, we attempted to identify novel tumor markers by focusing on neutral free-glycans in urine. Free-glycans extracted from the urine of normal subjects and cancer patients with gastric, colorectal, pancreatic and bile duct were fluorescently labeled with 2-aminopyridine. Profiles of these neutral free-glycans constructed using multidimensional high performance liquid chromatography separation were compared between normal controls and cancer patients. The analysis identified one glycan in the urine of cancer patients with a unique structure, which included a pentose residue. To reveal the glycan structure, the linkage fashion, monosaccharide species and enantiomer of the pentose were analyzed by high performance liquid chromatography and mass spectrometry combined with several chemical treatments. The backbone of the glycan was a monoantennary complex-type free-N-glycan containing β1,4-branch. The pentose residue was attached to the antennal GlcNAc and released by α1,3/4-l-fucosidase. Intriguingly, the pentose residue was consistent with d-arabinose. Collectively, this glycan structure was determined to be Galβ1-4(d-Araβ1-3)GlcNAcβ1-4Manα1-3Manβ1-4GlcNAc-PA. Elevation of d-arabinose-containing free-glycans in the urine of cancer patients was confirmed by selected reaction monitoring. This is the first study to unequivocally show the occurrence of a d-arabinose-containing oligosaccharide in human together with its detailed structure.

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Section: Resultsmentioning

confidence: 99%

Occurrence of a d-arabinose-containing complex-type free-N-glycan in the urine of cancer patients

Tanaka-Okamoto

Hanzawa

Murakami

et al. 2022

Sci Rep

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“…PGC-LC–MS/MS has become one of the best methods for separation of underivatized glycan isomers. Nevertheless, the inability to discriminate isomeric structures by low-energy MS/MS fragmentation at positive ionization was reported because of the insufficient branching information generated from glycosidic cleavages and the presence of nonspecific diagnostic fragments caused by the intramolecular migration of monosaccharides such as fucose, hexose, and xylose. − Differentiation of structural isomers is generally achieved by cross-ring cleavages using high-energy collision-induced dissociation (CID) or negative ionization MS/MS, − although these fragments are in relatively low abundances which require expertise for complicated data interpretation. Recently, the unavailability of nanoflow PGC columns has commercially become another problem for high-throughput glycomics.…”

Section: Introductionmentioning

confidence: 99%

Resolving Isomeric Structures of Native Glycans by Nanoflow Porous Graphitized Carbon Chromatography–Mass Spectrometry

She

Tam

et al. 2020

Anal. Chem.

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Characterization of the structural diversity of glycans by liquid chromatography–tandem mass spectrometry (LC–MS/MS) remains an analytical challenge in large-scale glycomics applications because of the presence of heterogeneous composition, ubiquitous isomers, lability of post-translational glycan modifications, and complexity of data interpretation. High-resolution separation of glycan isomers differentiating from positional, linkage, branching, and anomeric structures is often a prerequisite to ensure the comprehensive glycan identification. Here, we developed a straightforward method using self-packed capillary porous graphitic carbon (PGC) columns for nanoflow LC–MS/MS analyses of native glycans released from glycoproteins. The technique enables highly resolved chromatographic separation of over 20 high-mannose glycan isomers in ribonuclease B and a diverse range of hybrid and complex-type sialoglycoforms of fetuin. The distinct structures of anomeric glycans and linkage sialoglycan isomers, α2,3 and α2,6, were identified by the characteristic MS/MS fragment ions. A glycan sequencing strategy utilizing diagnostic ions and complementary fragments specific to branching residues was established to simplify the MS/MS data interpretation of closely related isomeric structures. To promote the PGC-LC–MS/MS-based method for glycome-wide applications, we extended analyses to native sulfoglycans from the egg-propagated and cell culture-derived influenza vaccines and demonstrate the high-resolution separation and structural characterization of underivatized neutral and anionic glycoforms including oligomannosidic glycan anomers, sialoglycan linkage isomers, and regioisomers of afucosylated and fucosylated sulfoglycans containing sulfated-6-GlcNAc and sulfated-4-GalNAc residues.

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“…For more than 20 years, researchers have also been studying glycan rearrangement reactions in tandem MS experiments [29, 30]. Most of these studies are based on the observation of unusual fragment masses that arise from a rearrangement of fucose and occasionally other monosaccharide units such as xylose [31] during the CID process. This phenomenon is also often referred to as internal residue loss (IRL) and has been studied extensively by probing the influence of different adduct ions [32, 33] or an aglycon [34] and different derivatization strategies [35–37].…”

Section: Introductionmentioning

confidence: 99%

The role of the mobile proton in fucose migration

et al. 2019

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Fucose migration reactions represent a substantial challenge in the analysis of fucosylated glycan structures by mass spectrometry. In addition to the well-established observation of transposed fucose residues in glycan-dissociation product ions, recent experiments show that the rearrangement can also occur in intact glycan ions. These results suggest a low-energy barrier for migration of the fucose residue and broaden the relevance of fucose migration to include other types of mass spectrometry experiments, including ion mobility-mass spectrometry and ion spectroscopy. In this work, we utilize cold-ion infrared spectroscopy to provide further insight into glycan scrambling in intact glycan ions. Our results show that the mobility of the proton is a prerequisite for the migration reaction. For the prototypical fucosylated glycans Lewis x and blood group antigen H-2, the formation of adduct ions or the addition of functional groups with variable proton affinity yields significant differences in the infrared spectra. These changes correlate well with the promotion or inhibition of fucose migration through the presence or absence of a mobile proton. Electronic supplementary material The online version of this article (10.1007/s00216-019-01657-w) contains supplementary material, which is available to authorized users.

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Xylose Migration During Tandem Mass Spectrometry of N-Linked Glycans

Cited by 23 publications

References 24 publications

Occurrence of a d-arabinose-containing complex-type free-N-glycan in the urine of cancer patients

Occurrence of a d-arabinose-containing complex-type free-N-glycan in the urine of cancer patients

Resolving Isomeric Structures of Native Glycans by Nanoflow Porous Graphitized Carbon Chromatography–Mass Spectrometry

The role of the mobile proton in fucose migration

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