Recent advances in mass spectrometric analysis of glycoproteins

Banazadeh, Alireza; Veillon, Lucas; Wooding, Kerry M.; Zabet-Moghaddam, Masoud; Mechref, Yehia

doi:10.1002/elps.201600357

Cited by 78 publications

(62 citation statements)

References 134 publications

(120 reference statements)

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“…The most direct approach would be to target regions of interest for digestion with trypsin, followed by extraction and enrichment of glycopeptides from these regions. While great progress has been made in direct glycopeptide analysis to determine both peptide and glycan sequences using high resolution tandem MS [Banazadeh, Veillon, Wooding, Zabet, & Mechref, 2016; Thaysen-Andersen & Packer, 2014], there is still a requirement for large amounts of sample above what can be obtained by isolation of small, focal regions of tissue. A current alternative approach is to use MS imaging of peptides in situ, combined with extracted peptide sequencing identification, to map protein expression to tissue localization.…”

Section: Emerging Applicationsmentioning

confidence: 99%

MALDI Mass Spectrometry Imaging of N-Linked Glycans in Cancer Tissues

Drake

Powers

Jones

et al. 2017

Advances in Cancer Research

129

112

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Glycosylated proteins account for a majority of the post-translation modifications of cell surface, secreted and circulating proteins. Within the tumor microenvironment, the presence of immune cells, extracellular matrix proteins, cell surface receptors and interactions between stroma and tumor cells are all processes mediated by glycan binding and recognition reactions. Changes in glycosylation during tumorigenesis are well documented to occur, and affect all of these associated adhesion and regulatory functions. A MALDI imaging mass spectrometry (MALDI-IMS) workflow for profiling N-linked glycan distributions in fresh/frozen tissues and formalin-fixed paraffin-embedded (FFPE) tissues has recently been developed. The key to the approach is the application of a molecular coating of peptide-N-glycosidase to tissues, an enzyme that cleaves asparagine-linked glycans from their protein carrier. The released N-linked glycans can then be analyzed by MALDI-IMS directly on tissue. Generally 40 or more individual glycan structures are routinely detected, and when combined with histopathology localizations, tumor specific glycans are readily grouped relative to non-tumor regions and other structural features. This technique is a recent development and new approach in glycobiology and mass spectrometry imaging research methodology, thus potential uses such as tumor-specific glycan biomarker panels and other applications are discussed.

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Section: Emerging Applicationsmentioning

confidence: 99%

MALDI Mass Spectrometry Imaging of N-Linked Glycans in Cancer Tissues

Drake

Powers

Jones

et al. 2017

Advances in Cancer Research

129

112

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“…The ability to measure a variety of PTMs is a unique aspect of advanced proteomics technologies. Currently, more than 200 biological relevant PTMs have been reported [47] and several types of them, such as phosphorylation, acetylation, glycosylation, and thiol-based redox modifications, have been studied extensively [24,32,48–50]. …”

Section: Ms-based Ptm Profilingmentioning

confidence: 99%

Mass spectrometry-based proteomics for system-level characterization of biological responses to engineered nanomaterials

et al. 2018

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The widespread use of engineered nanomaterials or nanotechnology makes the characterization of biological responses to nanomaterials an important area of research. The application of omics approaches, such as mass spectrometry-based proteomics, has revealed new insights into the cellular responses of exposure to nanomaterials, including how nanomaterials interact and alter cellular pathways. In addition, exposure to engineered nanomaterials often leads to the generation of reactive oxygen species and cellular oxidative stress, which implicates a redox-dependent regulation of cellular responses under such conditions. In this review, we discuss quantitative proteomics-based approaches, with an emphasis on redox proteomics, as a tool for system-level characterization of the biological responses induced by engineered nanomaterials. Graphical abstract ᅟ.

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“…However, concerning MS-based methods [22][23][24][25], a large panel of methodologies were evaluated, except the CE-ESI-MS approach. Nevertheless, in 2008, Gennaro et al described the development of CE-ESI-MS technology with online LIF detection that allows identification of major and minor glycan species observed in the routine CE-LIF assay.…”

Section: Introductionmentioning

confidence: 99%

Monoclonal antibody N-glycosylation profiling using capillary electrophoresis – Mass spectrometry: Assessment and method validation

Giorgetti

D’Atri

Canonge

et al. 2018

Talanta

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A B S T R A C TCharacterization of therapeutic proteins represents a major challenge for analytical sciences due to their heterogeneity caused by post-translational modifications (PTM). Among these PTM, glycosylation which is possibly the most prominent, require comprehensive identification because of their major influence on protein structure and effector functions of monoclonal antibodies (mAbs). As a consequence, glycosylation profiling must be deeply characterized. For this application, several analytical methods such as separation-based or MS-based methods, were evaluated. However, no CE-ESI-MS approach has been assessed and validated. Here, we illustrate how the use of CE-ESI-MS method permits the comprehensive characterization of mAbs N-glycosylation at the glycopeptide level to perform relative quantitation of N-glycan species. Validation of the CE-ESI-MS method in terms of robustness and reproducibility was demonstrated through the relative quantitation of glycosylation profiles for ten different mAbs produced in different cell lines. Glycosylation patterns obtained for each mAbs were compared to Hydrophilic Interaction Chromatography of 2-aminobenzamide labelled glycans with fluorescence detector (HILIC-FD) analysis considered as a reference method. Very similar glycoprofiling were obtained with the CE-ESI-MS and HILIC-FD demonstrating the attractiveness of CE-ESI-MS method to characterize and quantify the glycosylation heterogeneity of a wide range of therapeutic mAbs with high accuracy and precision.

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Recent advances in mass spectrometric analysis of glycoproteins

Cited by 78 publications

References 134 publications

MALDI Mass Spectrometry Imaging of N-Linked Glycans in Cancer Tissues

MALDI Mass Spectrometry Imaging of N-Linked Glycans in Cancer Tissues

Mass spectrometry-based proteomics for system-level characterization of biological responses to engineered nanomaterials

Monoclonal antibody N-glycosylation profiling using capillary electrophoresis – Mass spectrometry: Assessment and method validation

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