A MALDI-MS-based quantitative targeted glycomics (MALDI-QTaG) for total N-glycan analysis

Kim, Kyoung-Jin; Kim, Yoon-Woo; Hwang, Cheol-Hwan; Park, Han-Gyu; Yang, Yung‐Hun; Koo, Mi-Young; Kim, Yun‐Gon

doi:10.1007/s10529-015-1881-6

Cited by 19 publications

(16 citation statements)

References 15 publications

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Section: Oligosaccharidesmentioning

confidence: 99%

“…The sialoglycoproteins are first modified using acetohydrazide, followed by enzymatic releasing. The reducing ends of both neutral and acidic glycans are then derivatized by 2-aminobenzoic acid (2-AA) or Girard's reagent P. [248][249][250] Another approach that can label sialic acids at a protein level is performed in the presence of EDC using p-toluidine instead of acetohydrazide. 247,251,252 In combination with stable isotope labeling, the method has been used for the quantitative analysis of sialoglycans from cells treated with metabolic label, showing its potential in metabolic glycoengineering.…”

Section: Amidationmentioning

confidence: 99%

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Mass spectrometry for protein sialoglycosylation

Zhang

Wang

et al. 2017

Mass Spectrometry Reviews

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Sialic acids are a family of structurally unique and negatively charged nine-carbon sugars, normally found at the terminal positions of glycan chains on glycoproteins and glycolipids. The glycosylation of proteins is a universal post-translational modification in eukaryotic species and regulates essential biological functions, in which the most common sialic acid is N-acetyl-neuraminic acid (2-keto-5-acetamido-3,5-dideoxy-D-glycero-D-galactononulopyranos-1-onic acid) (Neu5NAc). Because of the properties of sialic acids under general mass spectrometry (MS) conditions, such as instability, ionization discrimination, and mixed adducts, the use of MS in the analysis of protein sialoglycosylation is still challenging. The present review is focused on the application of MS related methodologies to the study of both N- and O-linked sialoglycans. We reviewed MS-based strategies for characterizing sialylation by analyzing intact glycoproteins, proteolytic digested glycopeptides, and released glycans. The review concludes with future perspectives in the field.

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Section: Oligosaccharidesmentioning

confidence: 99%

Section: Amidationmentioning

confidence: 99%

Mass spectrometry for protein sialoglycosylation

Zhang

Wang

et al. 2017

Mass Spectrometry Reviews

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“…Recently, our group has reported MALDI-MS-based quantitative analysis of carbohydrates and bioactive lipids ( e.g ., N-acyl homoserine lactones) that have an aldehyde or ketone group 34 35 36 . Previous studies have demonstrated that chemical derivatization of the target molecules could dramatically enhance the sensitivity (up to 6 × 10 4 times) and allow more accurate quantitative analysis using only MALDI-MS without prior sample purification 36 .…”

Section: Resultsmentioning

confidence: 99%

“…To address these problems, matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), which is an extremely sensitive and robust method that is suitable for the analysis of complex mixtures, could be a great alternative tool for the analysis of endogenous estrones 34 35 . Here, we demonstrate a MALDI-based quantitative platform for the quantitation of endogenous estrogenic hormones in human body fluid and cells ( Fig.…”

mentioning

confidence: 99%

A MALDI-MS-based quantitative analytical method for endogenous estrone in human breast cancer cells

Kim

Park

et al. 2016

Sci Rep

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The level of endogenous estrone, one of the three major naturally occurring estrogens, has a significant correlation with the incidence of post-menopausal breast cancer. However, it is challenging to quantitatively monitor it owing to its low abundance. Here, we develop a robust and highly sensitive mass-assisted laser desorption/ionization mass spectrometry (MALDI-MS)-based quantitative platform to identify the absolute quantities of endogenous estrones in a variety of clinical specimens. The one-step modification of endogenous estrone provided good linearity (R2 > 0.99) and significantly increased the sensitivity of the platform (limit of quantitation: 11 fmol). In addition, we could identify the absolute amount of endogenous estrones in cells of the breast cancer cell line MCF-7 (34 fmol/106 cells) by using a deuterated estrone as an internal standard. Finally, by applying the MALDI-MS-based quantitative method to endogenous estrones, we successfully monitored changes in the metabolic expression level of estrones (17.7 fmol/106 letrozole-treated cells) in MCF-7 cells resulting from treatment with an aromatase inhibitor. Taken together, these results suggest that this MALDI-MS-based quantitative approach may be a general method for the targeted metabolomics of ketone-containing metabolites, which can reflect clinical conditions and pathogenic mechanisms.

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“…Kim and collaborators evaluated the performance of a quantitative MALDI targeting glycomics approach, in the analysis of N -glycans, in both, purified AFP from normal cord blood (control condition) and from HCC cell line—Huh7 cells—(increase of core-fucosylation). It was demonstrated that the results are promising in clinical and bioengineering fields ( 110 ). In 2009, Lattová and collaborators examined serum of animal models with HCC-inducted through MALDI-MS, identifying forty different N -glycans, in which some structures appeared to have highest frequency in HCC samples ( 29 ).…”

Section: Mass Spectrometry (Ms) As a Tool For Glycomics Analysismentioning

confidence: 99%

Use of Mass Spectrometry to Screen Glycan Early Markers in Hepatocellular Carcinoma

2018

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Association between altered glycosylation patterns and poor prognosis in cancer points glycans as potential specific tumor markers. Most proteins are glycosylated and functionally arranged on cell surface and extracellular matrix, mediating interactions and cellular signaling. Thereby, aberrant glycans may be considered a pathological phenotype at least as important as changes in protein expression for cancer and other complex diseases. As most serum glycoproteins have hepatic origin, liver disease phenotypes, such as hepatocellular carcinoma (HCC), may present altered glycan profile and display important modifications. One of the prominent obstacles in HCC is the diagnostic in advanced stages when patients have several liver dysfunctions, limiting treatment options and life expectancy. The characterization of glycomic profiles in pathological conditions by means of mass spectrometry (MS) may lead to the discovery of early diagnostic markers using non-invasive approaches. MS is a powerful analytical technique capable of elucidating many glycobiological issues and overcome limitations of the serological markers currently applied in clinical practice. Therefore, MS-based glycomics of tumor biomarkers is a promising tool to increase early detection and monitoring of disease.

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A MALDI-MS-based quantitative targeted glycomics (MALDI-QTaG) for total N-glycan analysis

Abstract: This MALDI-MS-based glycomics technology has wide applications in many clinical and bioengineering fields requiring sensitive, quantitative and fast N-glycosylation validation.

Cited by 19 publications

References 15 publications

Mass spectrometry for protein sialoglycosylation

Mass spectrometry for protein sialoglycosylation

A MALDI-MS-based quantitative analytical method for endogenous estrone in human breast cancer cells

Use of Mass Spectrometry to Screen Glycan Early Markers in Hepatocellular Carcinoma

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