Glycan reductive isotope-coded amino acid labeling (GRIAL) for mass spectrometry-based quantitative N-glycomics

Cai, Yan; Jiao, Jing; Bin, Zhichao; Zhang, Ying; Yang, Pengyuan; Lu, Haojie

doi:10.1039/c4cc08086f

Cited by 32 publications

(30 citation statements)

References 23 publications

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“…Glycan reductive isotope‐coded amino acid labeling was used for MS analysis of N‐glycans, where the reducing end of the N‐glycan was labeled with isotope‐coded arginine (Arg( 13 C 6 )) . The results showed the glycan reductive isotope‐coded amino acid labeling strategy as an effective method for enhancement of ionization efficiency (3.6‐ to 5.5‐fold).…”

Section: Advancements In Sample Preparation Methodsmentioning

confidence: 99%

Recent advances in mass spectrometric analysis of glycoproteins

et al. 2016

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Glycosylation is one of the most common post-translational modifications of proteins and plays essential roles in various biological processes, including protein folding, host-pathogen interaction, immune response, and inflammation and aberrant protein glycosylation is a well-known event in various disease states including cancer. As a result, it is critical to develop rapid and sensitive methods for the analysis of abnormal glycoproteins associated with diseases. Mass spectrometry in conjugation with different separation methods, such as capillary electrophoresis, ion mobility, and high performance liquid chromatography, has become a popular tool for glycoprotein analysis, providing highly informative fragments for structural identification of glycoproteins. This review provides an overview of the developments and accomplishments in the field of glycomics and glycoproteomics reported between 2014 and 2016.

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Section: Advancements In Sample Preparation Methodsmentioning

confidence: 99%

Recent advances in mass spectrometric analysis of glycoproteins

et al. 2016

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“…The glycan reductive isotope‐coded amino acid labeling (GRIAL) enhanced the ionization efficiency of N‐glycans and offered a large mass difference which avoided inaccurate glycan quantitation due to isotope interference. [ 28 ] Later, by introducing metallic element chelated tags, we achieved multiplex quantitation of N‐glycans from different samples in a single MS run. [ 29 ] To accurately quantify N‐glycans with sialic acid, which is labile and has lower ionization efficiency than neutral glycans, duplex stable isotope labeling (DuSIL) was developed to simultaneously quantify and distinguish sialylated and neutral N‐glycans by MALDI‐MS.…”

Section: Post‐translational Modification Proteomementioning

confidence: 99%

Discover the Post‐Translational Modification Proteome Using Mass Spectrometry

et al. 2021

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Protein post‐translational modifications (PTMs) are chemical modifications on proteins. PTMs play a key role in many cellular processes by influencing the structure of proteins and dynamically regulating their functions. Therefore, characterizing PTMs at proteome level is critical to provide invaluable insight into the functions of proteins underlying different biological processes. Advances in modern proteomics technologies including sample preparation, chromatography separation as well as mass spectrometry have propelled the PTMs proteome to further depths. During the past decade, to better examine the PTMs with high sensitivity and selectivity, our group have developed a series of MS‐based novel analytical approaches to study the protein PTMs. Herein, we mainly introduce these approaches developed by our group and discuss how to overcome the technical obstacles of studying various protein PTMs with mass spectrometry. What is the most favorite and original method developed in your research group? The qualitative and quantitative approaches developed for analysis of PTM proteome. How do you get into this specific field? Could you please share some experiences with our readers? I entered Fudan University in 2003, when the sequencing of human genome was just completed. At that time, the life science entered the post‐genomic era, the era of proteomics. My post‐doctoral work is mainly based on mass spectrometry analysis, which is the core tool for proteome research. Therefore, I began to develop mass spectrometry‐based method for proteome research since then. What is the most important personality for scientific research? Creative, persistence, and collaboration. What's your hobbies? Playing badminton.

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“…The capacity of analysis with isotope labeling is shown to be impeded by the high spectral complexity and the requirement of ultra-high resolving power MS [162]. The introduction of novel isobaric tags enables multiplexed glycan analysis, such as isobaric aldehyde reactive tags (iARTs) [163], quaternary amine-containing isobaric tag for glycan (QUANTITY) [164], aminoxy tandem mass tag (aminoxyTMT) [165], glycan reductive isotope-coded amino acid labeling (GRIAL) [166], and glycan reducing end dual isotopic labeling (GREDIL) [167]. Occasional issues arise, however, such as relatively low reporter ion yield for labeled complex glycans.…”

Section: Glycosylation Studies With Isotopic Labelingmentioning

confidence: 99%

Characterization of Cell Glycocalyx with Mass Spectrometry Methods

Xie

Wong

et al. 2019

Cells

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The cell membrane plays an important role in protecting the cell from its extracellular environment. As such, extensive work has been devoted to studying its structure and function. Crucial intercellular processes, such as signal transduction and immune protection, are mediated by cell surface glycosylation, which is comprised of large biomolecules, including glycoproteins and glycosphingolipids. Because perturbations in glycosylation could result in dysfunction of cells and are related to diseases, the analysis of surface glycosylation is critical for understanding pathogenic mechanisms and can further lead to biomarker discovery. Different mass spectrometry-based techniques have been developed for glycan analysis, ranging from highly specific, targeted approaches to more comprehensive profiling studies. In this review, we summarized the work conducted for extensive analysis of cell membrane glycosylation, particularly those employing liquid chromatography with mass spectrometry (LC-MS) in combination with various sample preparation techniques.

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Glycan reductive isotope-coded amino acid labeling (GRIAL) for mass spectrometry-based quantitative N-glycomics

Abstract: A general and simple labeling method, termed glycan reductive isotope-coded amino acid labeling (GRIAL), was developed for mass spectrometry-based quantitative N-glycomics.

Cited by 32 publications

References 23 publications

Recent advances in mass spectrometric analysis of glycoproteins

Recent advances in mass spectrometric analysis of glycoproteins

Discover the Post‐Translational Modification Proteome Using Mass Spectrometry

Characterization of Cell Glycocalyx with Mass Spectrometry Methods

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