Glycome profiling using modern glycomics technology: technical aspects and applications

2010 ◽  
Vol 391 (2/3) ◽  
Author(s):  
Dieter Vanderschaeghe ◽  
Nele Festjens ◽  
Joris Delanghe ◽  
Nico Callewaert
Keyword(s):  
Mass Spectrometry ◽  
Signal Transduction ◽  
Liquid Chromatography Mass Spectrometry ◽  
Post Translational Modification ◽  
Technical Aspects ◽  
Glycome Profiling ◽  
The Past ◽  
Research Fields ◽  
Research Goal ◽  
Glycan Profiling

Abstract Glycomics research has become indispensable in many research fields such as immunity, signal transduction and development. Moreover, changes in the glycosylation of proteins and lipids have been reported in several diseases including cancer. The analysis of a complex post-translational modification such as glycosylation depends on the availability or development of appropriate analytical technologies. The research goal determines the sensitivity, resolution and throughput requirements and guides the choice of a particular technology. This review highlights the evolution of glycan profiling tools in the past 5 years. We focus on capillary electrophoresis, liquid chromatography, mass spectrometry and lectin microarrays.

scholarly journals Identification of the Protein Glycation Sites in Human Myoglobin as Rapidly Induced by d-Ribose

Molecules ◽  
2021 ◽  
Vol 26 (19) ◽  
pp. 5829
Author(s):  
Jing-Jing Liu ◽  
Yong You ◽  
Shu-Qin Gao ◽  
Shuai Tang ◽  
Lei Chen ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
High Performance ◽  
Protein Glycation ◽  
Valuable Insight ◽  
Liquid Chromatography Mass Spectrometry ◽  
Post Translational Modification ◽  
Lysine Residues ◽  
Human Myoglobin ◽  
And Function ◽  
Insight Into

Protein glycation is an important protein post-translational modification and is one of the main pathogenesis of diabetic angiopathy. Other than glycated hemoglobin, the protein glycation of other globins such as myoglobin (Mb) is less studied. The protein glycation of human Mb with ribose has not been reported, and the glycation sites in the Mb remain unknown. This article reports that d-ribose undergoes rapid protein glycation of human myoglobin (HMb) at lysine residues (K34, K87, K56, and K147) on the protein surface, as identified by ultra-high performance liquid chromatography-mass spectrometry (UHPLC-MS) and electrospray ionization tandem mass spectrometry (ESI-MS/MS). Moreover, glycation by d-ribose at these sites slightly decreased the rate of the met heme (FeIII) in reaction with H2O2 to form a ferryl heme (FeIV=O). This study provides valuable insight into the protein glycation by d-ribose and provides a foundation for studying the structure and function of glycated heme proteins.

scholarly journals The Applications and Features of Liquid Chromatography-Mass Spectrometry in the Analysis of Traditional Chinese Medicine

2016 ◽  
Vol 2016 ◽  
pp. 1-7 ◽  
Author(s):  
Bingyao Pang ◽  
Ying Zhu ◽  
Longqing Lu ◽  
Fangbing Gu ◽  
Hailong Chen
Keyword(s):  
Mass Spectrometry ◽  
Liquid Chromatography ◽  
Chinese Medicine ◽  
Traditional Chinese Medicine ◽  
Qualitative And Quantitative Analysis ◽  
Liquid Chromatography Mass Spectrometry ◽  
Complex Samples ◽  
Qualitative And Quantitative ◽  
Advantages And Disadvantages ◽  
The Past

With increasingly improved separation of complex samples and detection of unknown material capabilities, liquid chromatography coupled with mass spectrometry (LC-MS) has been widely used in traditional Chinese medicine (TCM) research. This article describes the principles of liquid chromatography (LC) and mass spectrometry (MS) and their advantages and disadvantages in qualitative and quantitative analysis of TCM. We retrieved research literatures about the application of LC-MS in TCM published during the past five years at home and abroad. To better guide the analysis of TCM, this review mainly focuses on the applications category of LC-MS, how often different kinds of LC-MS are used, and the qualitative and quantitative ability of various LC-MS in the study of TCM.

Protein CoAlation: a redox-linked post-translational modification

2017 ◽  
Vol 474 (16) ◽  
pp. 2897-2899 ◽  
Author(s):  
Steven C. Ley ◽  
Luiz Pedro S. de Carvalho
Keyword(s):  
Mass Spectrometry ◽  
Signal Transduction ◽  
Metabolic Pathways ◽  
Metabolic Response ◽  
Metabolic Stress ◽  
Regulatory Activity ◽  
Post Translational Modification ◽  
Target Proteins ◽  
Biochemical Journal ◽  
Response To Stress

Regulation of metabolic pathways by signal transduction and transcriptional cascades can alter cellular levels of metabolites. Metabolites themselves can also have regulatory activity as shown in a new study published in the Biochemical Journal. Tsuchiya et al. describe a novel antibody and mass spectrometry-based method for identifying proteins that are reversibly modified with Coenzyme A (CoA). Analysis of the ‘CoAlated proteome’ under conditions of oxidative and metabolic stress revealed a bias towards the modification of metabolic enzymes by CoA. Furthermore, CoAlation was shown to alter the activity of target proteins. These results suggest that CoAlation is a widespread post-translational modification that may have important roles in the metabolic response to stress.

Using Micro Pillar Array Columns (µPAC) for the Analysis of Permethylated Glycans

The Analyst ◽  
2021 ◽  
Author(s):  
Byeong Cho ◽  
Peilin Jiang ◽  
Mona Goli ◽  
Sakshi Gautam ◽  
Yehia Mechref
Keyword(s):  
Mass Spectrometry ◽  
Liquid Chromatography ◽  
Biological Systems ◽  
Liquid Chromatography Mass Spectrometry ◽  
Post Translational Modification ◽  
Pillar Array ◽  
Chromatography Mass Spectrometry

Glycosylation is a complex and common post-translational modification of proteins. To study glycosylation, liquid chromatography-mass spectrometry (LC-MS) is often used to profile and structurally characterize the glycans in biological systems....

How SIMS microscopy can be used in medicine

1992 ◽  
Vol 50 (2) ◽  
pp. 1602-1603
Author(s):  
Philippe Fragu
Keyword(s):  
Mass Spectrometry ◽  
Biomedical Applications ◽  
Secondary Ion Mass Spectrometry ◽  
Chemical Elements ◽  
Biological Applications ◽  
The Past ◽  
Potential Source ◽  
Secondary Ion ◽  
Chemical Integrity ◽  
Scientific Endeavour

The identification, localization and quantification of intracellular chemical elements is an area of scientific endeavour which has not ceased to develop over the past 30 years. Secondary Ion Mass Spectrometry (SIMS) microscopy is widely used for elemental localization problems in geochemistry, metallurgy and electronics. Although the first commercial instruments were available in 1968, biological applications have been gradual as investigators have systematically examined the potential source of artefacts inherent in the method and sought to develop strategies for the analysis of soft biological material with a lateral resolution equivalent to that of the light microscope. In 1992, the prospects offered by this technique are even more encouraging as prototypes of new ion probes appear capable of achieving the ultimate goal, namely the quantitative analysis of micron and submicron regions. The purpose of this review is to underline the requirements for biomedical applications of SIMS microscopy.Sample preparation methodology should preserve both the structural and the chemical integrity of the tissue.

Dicarbonyl derived post-translational modifications: chemistry bridging biology and aging-related disease

2020 ◽  
Vol 64 (1) ◽  
pp. 97-110
Author(s):  
Christian Sibbersen ◽  
Mogens Johannsen
Keyword(s):  
Mass Spectrometry ◽  
Future Research ◽  
Amino Acid Residues ◽  
Post Translational Modification ◽  
Dicarbonyl Compounds ◽  
Protein Targets ◽  
Post Translational Modifications ◽  
Reactive Protein ◽  
Glycation End Products ◽  
Direct Mass Spectrometry

Abstract In living systems, nucleophilic amino acid residues are prone to non-enzymatic post-translational modification by electrophiles. α-Dicarbonyl compounds are a special type of electrophiles that can react irreversibly with lysine, arginine, and cysteine residues via complex mechanisms to form post-translational modifications known as advanced glycation end-products (AGEs). Glyoxal, methylglyoxal, and 3-deoxyglucosone are the major endogenous dicarbonyls, with methylglyoxal being the most well-studied. There are several routes that lead to the formation of dicarbonyl compounds, most originating from glucose and glucose metabolism, such as the non-enzymatic decomposition of glycolytic intermediates and fructosyl amines. Although dicarbonyls are removed continuously mainly via the glyoxalase system, several conditions lead to an increase in dicarbonyl concentration and thereby AGE formation. AGEs have been implicated in diabetes and aging-related diseases, and for this reason the elucidation of their structure as well as protein targets is of great interest. Though the dicarbonyls and reactive protein side chains are of relatively simple nature, the structures of the adducts as well as their mechanism of formation are not that trivial. Furthermore, detection of sites of modification can be demanding and current best practices rely on either direct mass spectrometry or various methods of enrichment based on antibodies or click chemistry followed by mass spectrometry. Future research into the structure of these adducts and protein targets of dicarbonyl compounds may improve the understanding of how the mechanisms of diabetes and aging-related physiological damage occur.

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