Recent advances in hydrophilic interaction liquid chromatography (HILIC) for structural glycomics

Zauner, Gerhild; Deelder, André M.; Wuhrer, Manfred

doi:10.1002/elps.201100247

Cited by 174 publications

(113 citation statements)

References 58 publications

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“…HILIC columns provide an alternative separation strategy in that the glycoforms interact with the hydrophilic column; thus, the glycoforms for a given peptide are more readily separated. Advances in the use of HILIC columns for glycopeptide analysis have been reviewed separately (30).…”

Section: Emerging Methods Supporting Glycopeptide Analysismentioning

confidence: 99%

Glycopeptide Analysis, Recent Developments and Applications

Desaire

2013

Molecular & Cellular Proteomics

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Glycopeptide-based analysis is used to inform researchers about the glycans on one or more proteins. The method's key attractive feature is its ability to link glycosylation information to exact locations (glycosylation sites) on proteins. Numerous applications for glycopeptide analysis are known, and several examples are described herein. The techniques used to characterize glycopeptides are still emerging, and recently, research focused on facilitating aspects of glycopeptide analysis has advanced significantly in the areas of sample preparation, MS fragmentation, and automation of data analysis. These recent developments, described herein, provide the foundation for the growth of glycopeptide analysis as a blossoming field. Molecular & Cellular

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Section: Emerging Methods Supporting Glycopeptide Analysismentioning

confidence: 99%

Glycopeptide Analysis, Recent Developments and Applications

Desaire

2013

Molecular & Cellular Proteomics

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“…7 The technology is robust, uses minimal glycoprotein material and the technology has been optimized to enable 80 short separation times. 7,20,21 The fluorescence detection is sensitive, allowing for detection of femtomolar concentrations. 22 HILIC separation is based on a polar stationary phase and a non-polar mobile phase.…”

Section: Introductionmentioning

confidence: 99%

Comparison of separation techniques for the elucidation of IgG N-glycans pooled from healthy mammalian species

Adamczyk

Tharmalingam-Jaikaran

Schomberg

et al. 2014

Carbohydrate Research

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a b s t r a c tThe IgG N-glycome provides sufficient complexity and information content to serve as an excellent source for biomarker discovery in mammalian health. Since oligosaccharides play a significant role in many biological processes it is very important to understand their structure. The glycosylation is cell type specific as well as highly variable depending on the species producing the IgG. We evaluated the variation of N-linked glycosylation of human, bovine, ovine, equine, canine and feline IgG using three orthogonal glycan separation techniques: hydrophilic interaction liquid chromatography (HILIC)-UPLC, reversed phase (RP)-UPLC and capillary electrophoresis with laser induced fluorescence detection (CE-LIF). The separation of the glycans by these high resolution methods yielded different profiles due to diverse chemistries. However, the % abundance of structures obtained by CE-LIF and HILIC-UPLC were similar, whereas the analysis by RP-UPLC was difficult to compare as the structures were separated by classes of glycans (highly mannosylated, fucosylated, bisected, fucosylated and bisected) resulting in the co-elution of many structures. The IgGs from various species were selected due to the complexity and variation in their N-glycan composition thereby highlighting the complementarity of these separation techniques.

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“…Recent advancements in mass spectrometry have overcome the limitations inherent to earlier glycan profiling methodologies (32)(33)(34)(35)(36)(37)(38)(39)(40)(41)(42)(43)(44). Herein we employ an MS-based analytical approach utilizing nano-LC separation with high resolution TOF MS for accurate detection of compounds, enabling rapid identification and quantitation of N-glycan alterations during Caco-2 cell differentiation.…”

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confidence: 99%

Characteristic Changes in Cell Surface Glycosylation Accompany Intestinal Epithelial Cell (IEC) Differentiation: High Mannose Structures Dominate the Cell Surface Glycome of Undifferentiated Enterocytes

Park

Brune

Mitra

et al. 2015

Molecular & Cellular Proteomics

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Changes in cell surface glycosylation occur during the development and differentiation of cells and have been widely correlated with the progression of several diseases. Because of their structural diversity and sensitivity to intra-and extracellular conditions, glycans are an indispensable tool for analyzing cellular transformations. Glycans present on the surface of intestinal epithelial cells (IEC) mediate interactions with billions of native microorganisms, which continuously populate the mammalian gut. A distinct feature of IECs is that they differentiate as they migrate upwards from the crypt base to the villus tip. In this study, nano-LC/ESI QTOF MS profiling was used to characterize the changes in glycosylation that correspond to Caco-2 cell differentiation. As Caco-2 cells differentiate to form a brush border membrane, a decrease in high mannose type glycans and a concurrent increase in fucosylated and sialylated complex/hybrid type glycans were observed. At day 21, when cells appear to be completely differentiated, remodeling of the cell surface glycome ceases. Differential expression of glycans during IEC maturation appears to play a key functional role in regulating the membrane-associated hydrolases and contributes to the mucosal surface innate defense mechanisms. Developing methodologies to rapidly identify changes in IEC surface glycans may lead to a rapid screen-

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Recent advances in hydrophilic interaction liquid chromatography (HILIC) for structural glycomics

Cited by 174 publications

References 58 publications

Glycopeptide Analysis, Recent Developments and Applications

Glycopeptide Analysis, Recent Developments and Applications

Comparison of separation techniques for the elucidation of IgG N-glycans pooled from healthy mammalian species

Characteristic Changes in Cell Surface Glycosylation Accompany Intestinal Epithelial Cell (IEC) Differentiation: High Mannose Structures Dominate the Cell Surface Glycome of Undifferentiated Enterocytes

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